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Database: PDB
Entry: 4NM3
LinkDB: 4NM3
Original site: 4NM3 
HEADER    TRANSFERASE/PEPTIDE                     14-NOV-13   4NM3              
TITLE     CRYSTAL STRUCTURE OF GSK-3/AXIN COMPLEX BOUND TO PHOSPHORYLATED N-    
TITLE    2 TERMINAL AUTO-INHIBITORY PS9 PEPTIDE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN SYNTHASE KINASE-3 BETA;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-383 WITH PHOSPHOYLATED SER9;                    
COMPND   5 SYNONYM: GSK-3 BETA, SERINE/THREONINE-PROTEIN KINASE GSK3B;          
COMPND   6 EC: 2.7.11.26, 2.7.11.1;                                             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: AXIN-1;                                                    
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: RESIDUES 383-402;                                          
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: GSK3B;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)  CODON-PLUS RIL;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET29B(+);                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: AXIN, AXIN1;                                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)  CODON-PLUS RIL;                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: MODIFIED PGEX-KG                          
KEYWDS    WNT, LRP6, AUTO-INHIBITED, GSK-3, AXIN, KINASE, PRIMED SUBSTRATE,     
KEYWDS   2 PHOSPHORYLATED N-TERMINAL AUTO-INHIBITORY PS9 PEPTIDE, TRANSFERASE-  
KEYWDS   3 PEPTIDE COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.L.-H.CHU,J.L.STAMOS,M.D.ENOS,N.SHAH,W.I.WEIS                        
REVDAT   2   23-APR-14 4NM3    1       JRNL                                     
REVDAT   1   26-MAR-14 4NM3    0                                                
JRNL        AUTH   J.L.STAMOS,M.L.CHU,M.D.ENOS,N.SHAH,W.I.WEIS                  
JRNL        TITL   STRUCTURAL BASIS OF GSK-3 INHIBITION BY N-TERMINAL           
JRNL        TITL 2 PHOSPHORYLATION AND BY THE WNT RECEPTOR LRP6.                
JRNL        REF    ELIFE                         V.   3 01998 2014              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   24642411                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.900                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 32924                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1658                            
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 38.9698 -  4.8051    1.00     2895   152  0.1944 0.2304        
REMARK   3     2  4.8051 -  3.8150    1.00     2687   148  0.1533 0.1952        
REMARK   3     3  3.8150 -  3.3330    1.00     2647   134  0.1703 0.2187        
REMARK   3     4  3.3330 -  3.0284    1.00     2632   124  0.1875 0.2407        
REMARK   3     5  3.0284 -  2.8114    1.00     2593   125  0.2094 0.2936        
REMARK   3     6  2.8114 -  2.6457    1.00     2596   142  0.1931 0.2365        
REMARK   3     7  2.6457 -  2.5132    1.00     2556   134  0.2135 0.2645        
REMARK   3     8  2.5132 -  2.4039    1.00     2544   147  0.2431 0.3191        
REMARK   3     9  2.4039 -  2.3113    1.00     2544   140  0.2565 0.3227        
REMARK   3    10  2.3113 -  2.2316    1.00     2553   137  0.2995 0.3343        
REMARK   3    11  2.2316 -  2.1618    1.00     2513   145  0.3355 0.3615        
REMARK   3    12  2.1618 -  2.1000    0.99     2506   130  0.3875 0.4281        
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)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.080           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.02                          
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      :  0.005           3174                                  
REMARK   3   ANGLE     :  0.910           4336                                  
REMARK   3   CHIRALITY :  0.056            497                                  
REMARK   3   PLANARITY :  0.004            550                                  
REMARK   3   DIHEDRAL  : 11.943           1170                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 6 through 10 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -20.8559  44.6289 -23.0835              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3195 T22:   1.8097                                     
REMARK   3      T33:   1.0189 T12:   0.0829                                     
REMARK   3      T13:  -0.2290 T23:  -0.2833                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1455 L22:   1.6820                                     
REMARK   3      L33:   1.2010 L12:  -0.0557                                     
REMARK   3      L13:   0.8478 L23:  -1.2885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6824 S12:  -0.5660 S13:   0.4849                       
REMARK   3      S21:   0.3718 S22:   0.7012 S23:  -1.1534                       
REMARK   3      S31:   0.3197 S32:  -0.0107 S33:  -1.2520                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 26 through 88 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8151  45.6900   2.4732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4606 T22:   0.5990                                     
REMARK   3      T33:   0.4285 T12:  -0.1257                                     
REMARK   3      T13:   0.1088 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1448 L22:   4.7919                                     
REMARK   3      L33:   2.9013 L12:   1.9560                                     
REMARK   3      L13:  -0.6675 L23:  -0.5034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1616 S12:  -0.3950 S13:   0.9766                       
REMARK   3      S21:   0.4283 S22:   0.0521 S23:   0.3824                       
REMARK   3      S31:  -0.4850 S32:  -0.1533 S33:  -0.0286                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 89 through 96 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -24.5598  46.2167 -16.6065              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8171 T22:   1.4555                                     
REMARK   3      T33:   1.7308 T12:  -0.1699                                     
REMARK   3      T13:  -0.1507 T23:  -0.0299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0676 L22:   2.2788                                     
REMARK   3      L33:   4.6130 L12:  -0.4019                                     
REMARK   3      L13:  -1.7568 L23:  -0.2625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3040 S12:   0.2521 S13:  -0.9045                       
REMARK   3      S21:  -0.0578 S22:  -0.6581 S23:  -1.0424                       
REMARK   3      S31:  -1.1054 S32:  -0.2952 S33:   0.8201                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 97 through 136 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -17.5936  39.7060  -3.8508              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3249 T22:   0.3984                                     
REMARK   3      T33:   0.3323 T12:  -0.1414                                     
REMARK   3      T13:   0.0431 T23:   0.0541                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0359 L22:   5.2110                                     
REMARK   3      L33:   4.9717 L12:  -1.9785                                     
REMARK   3      L13:  -1.2057 L23:   3.7772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0070 S12:  -0.1519 S13:   0.2520                       
REMARK   3      S21:   0.6143 S22:  -0.2130 S23:   0.8086                       
REMARK   3      S31:   0.4152 S32:  -0.3263 S33:   0.1931                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 137 through 218 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5298  33.0370 -14.5813              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3619 T22:   0.2806                                     
REMARK   3      T33:   0.2448 T12:   0.0162                                     
REMARK   3      T13:  -0.0576 T23:  -0.0275                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0667 L22:   3.6951                                     
REMARK   3      L33:   3.8390 L12:   0.9490                                     
REMARK   3      L13:   0.4870 L23:   0.3606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1528 S12:  -0.1741 S13:  -0.1025                       
REMARK   3      S21:   0.2273 S22:  -0.0921 S23:   0.0647                       
REMARK   3      S31:   0.4392 S32:  -0.1579 S33:  -0.0357                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 219 through 383 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.4739  26.7170 -24.9527              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4784 T22:   0.2641                                     
REMARK   3      T33:   0.4114 T12:   0.0277                                     
REMARK   3      T13:  -0.1032 T23:  -0.0590                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4430 L22:   1.8680                                     
REMARK   3      L33:   4.8787 L12:   0.4348                                     
REMARK   3      L13:  -0.6417 L23:  -0.5502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0401 S12:  -0.1456 S13:  -0.4920                       
REMARK   3      S21:  -0.1115 S22:   0.0222 S23:   0.0378                       
REMARK   3      S31:   0.8249 S32:   0.1430 S33:  -0.0424                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resid 383 through 401 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.4179  43.2416 -44.2805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5931 T22:   0.3391                                     
REMARK   3      T33:   0.3220 T12:  -0.0805                                     
REMARK   3      T13:  -0.0726 T23:  -0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6473 L22:   5.6406                                     
REMARK   3      L33:   4.7204 L12:   2.3400                                     
REMARK   3      L13:  -1.3464 L23:  -2.5158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0179 S12:   0.6128 S13:   1.0063                       
REMARK   3      S21:   0.0307 S22:   0.0362 S23:   0.0896                       
REMARK   3      S31:  -0.5853 S32:   0.2324 S33:  -0.0215                       
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 4NM3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB083373.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : SI(III)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33093                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.963                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 18.600                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 17.90                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 4.88100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 4NM7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 35,000, 20MM TRIS 7.5, 300MM     
REMARK 280  NACL, 5% GLYCEROL, 10MM MGCL2, 200UM ATP, AND 5MM DTT,              
REMARK 280  MICRODIALYSIS, TEMPERATURE 277K                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.69500            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      187.39000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      140.54250            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      234.23750            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       46.84750            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       93.69500            
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        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      187.39000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      234.23750            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      140.54250            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       46.84750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 3760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     CYS A    14                                                      
REMARK 465     LYS A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     GLN A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     PHE A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     ASP A    31                                                      
REMARK 465     LYS A    32                                                      
REMARK 465     ASP A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     GLU A   121                                                      
REMARK 465     HIS A   385                                                      
REMARK 465     HIS A   386                                                      
REMARK 465     HIS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     HIS A   389                                                      
REMARK 465     GLY B   379                                                      
REMARK 465     GLY B   380                                                      
REMARK 465     ILE B   381                                                      
REMARK 465     LEU B   382                                                      
REMARK 465     THR B   402                                                      
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     ARG A   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  27    CG   CD   CE   NZ                                   
REMARK 470     ARG A  30    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  35    OG                                                  
REMARK 470     GLN A  89    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 103    CG   CD   CE   NZ                                   
REMARK 470     SER A 119    OG                                                  
REMARK 470     LYS A 122    CG   CD   CE   NZ                                   
REMARK 470     LYS A 123    CG   CD   CE   NZ                                   
REMARK 470     ASP A 124    CG   OD1  OD2                                       
REMARK 470     GLU A 125    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     LYS A 297    CG   CD   CE   NZ                                   
REMARK 470     ARG A 308    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 347    CG   OD1  ND2                                       
REMARK 470     LYS A 349    CG   CD   CE   NZ                                   
REMARK 470     HIS A 384    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL B 383    CG1  CG2                                            
REMARK 470     ARG B 401    CG   CD   NE   CZ   NH1  NH2                        
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 A   636     O    HOH A   661              2.18            
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    SER A  29     -169.06   -119.20                                   
REMARK 500    ASP A 181       40.21   -150.85                                   
REMARK 500    ASP A 200       87.87     63.17                                   
REMARK 500    CYS A 218      145.47     70.53                                   
REMARK 500    TYR A 221      -31.11     86.00                                   
REMARK 500    ASN A 370       74.58   -163.40                                   
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                              MG A 405  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 671   O                                                      
REMARK 620 2 ADP A 409   O1A 101.7                                              
REMARK 620 3 ASN A 186   OD1  94.0  88.0                                        
REMARK 620 4 ASP A 200   OD2 161.0  84.8 104.1                                  
REMARK 620 5 HOH A 584   O    90.9 165.6  98.2  81.0                            
REMARK 620 6 ADP A 409   O1B  89.2  92.3 176.7  72.6  80.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 406  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 409   O3B                                                    
REMARK 620 2 ASP A 200   OD1 104.2                                              
REMARK 620 3 HOH A 532   O    68.6 120.9                                        
REMARK 620 4 HOH A 533   O   140.6  72.3  79.6                                  
REMARK 620 5 ASP A 200   OD2  81.6  48.6  72.7  66.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 407                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 409                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4NM0   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IS A PEPTIDE INHIBITOR-FREE GSK-3/AXIN              
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 4NM5   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PHOSPHORYLATED WNT RECEPTOR          
REMARK 900 LRP6 C-MOTIF                                                         
REMARK 900 RELATED ID: 4NM7   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PHOSPHORYLATED WNT RECEPTOR          
REMARK 900 LRP6 E-MOTIF                                                         
REMARK 900 RELATED ID: 4NU1   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ITS OWN PHOSPHORYLATED N-            
REMARK 900 TERMINAL AUTO-INHIBITORY PS9 PEPTIDE AND ALF3 IS A                   
REMARK 900 TRANSITION STATE MIMICRY                                             
DBREF  4NM3 A    1   383  UNP    P49841   GSK3B_HUMAN      1    383             
DBREF  4NM3 B  383   402  UNP    O15169   AXIN1_HUMAN    383    402             
SEQADV 4NM3 HIS A  384  UNP  P49841              EXPRESSION TAG                 
SEQADV 4NM3 HIS A  385  UNP  P49841              EXPRESSION TAG                 
SEQADV 4NM3 HIS A  386  UNP  P49841              EXPRESSION TAG                 
SEQADV 4NM3 HIS A  387  UNP  P49841              EXPRESSION TAG                 
SEQADV 4NM3 HIS A  388  UNP  P49841              EXPRESSION TAG                 
SEQADV 4NM3 HIS A  389  UNP  P49841              EXPRESSION TAG                 
SEQADV 4NM3 GLY B  379  UNP  O15169              EXPRESSION TAG                 
SEQADV 4NM3 GLY B  380  UNP  O15169              EXPRESSION TAG                 
SEQADV 4NM3 ILE B  381  UNP  O15169              EXPRESSION TAG                 
SEQADV 4NM3 LEU B  382  UNP  O15169              EXPRESSION TAG                 
SEQRES   1 A  389  MET SER GLY ARG PRO ARG THR THR SEP PHE ALA GLU SER          
SEQRES   2 A  389  CYS LYS PRO VAL GLN GLN PRO SER ALA PHE GLY SER MET          
SEQRES   3 A  389  LYS VAL SER ARG ASP LYS ASP GLY SER LYS VAL THR THR          
SEQRES   4 A  389  VAL VAL ALA THR PRO GLY GLN GLY PRO ASP ARG PRO GLN          
SEQRES   5 A  389  GLU VAL SER TYR THR ASP THR LYS VAL ILE GLY ASN GLY          
SEQRES   6 A  389  SER PHE GLY VAL VAL TYR GLN ALA LYS LEU CYS ASP SER          
SEQRES   7 A  389  GLY GLU LEU VAL ALA ILE LYS LYS VAL LEU GLN ASP LYS          
SEQRES   8 A  389  ARG PHE LYS ASN ARG GLU LEU GLN ILE MET ARG LYS LEU          
SEQRES   9 A  389  ASP HIS CYS ASN ILE VAL ARG LEU ARG TYR PHE PHE TYR          
SEQRES  10 A  389  SER SER GLY GLU LYS LYS ASP GLU VAL TYR LEU ASN LEU          
SEQRES  11 A  389  VAL LEU ASP TYR VAL PRO GLU THR VAL TYR ARG VAL ALA          
SEQRES  12 A  389  ARG HIS TYR SER ARG ALA LYS GLN THR LEU PRO VAL ILE          
SEQRES  13 A  389  TYR VAL LYS LEU TYR MET TYR GLN LEU PHE ARG SER LEU          
SEQRES  14 A  389  ALA TYR ILE HIS SER PHE GLY ILE CYS HIS ARG ASP ILE          
SEQRES  15 A  389  LYS PRO GLN ASN LEU LEU LEU ASP PRO ASP THR ALA VAL          
SEQRES  16 A  389  LEU LYS LEU CYS ASP PHE GLY SER ALA LYS GLN LEU VAL          
SEQRES  17 A  389  ARG GLY GLU PRO ASN VAL SER TYR ILE CYS SER ARG TYR          
SEQRES  18 A  389  TYR ARG ALA PRO GLU LEU ILE PHE GLY ALA THR ASP TYR          
SEQRES  19 A  389  THR SER SER ILE ASP VAL TRP SER ALA GLY CYS VAL LEU          
SEQRES  20 A  389  ALA GLU LEU LEU LEU GLY GLN PRO ILE PHE PRO GLY ASP          
SEQRES  21 A  389  SER GLY VAL ASP GLN LEU VAL GLU ILE ILE LYS VAL LEU          
SEQRES  22 A  389  GLY THR PRO THR ARG GLU GLN ILE ARG GLU MET ASN PRO          
SEQRES  23 A  389  ASN TYR THR GLU PHE LYS PHE PRO GLN ILE LYS ALA HIS          
SEQRES  24 A  389  PRO TRP THR LYS VAL PHE ARG PRO ARG THR PRO PRO GLU          
SEQRES  25 A  389  ALA ILE ALA LEU CYS SER ARG LEU LEU GLU TYR THR PRO          
SEQRES  26 A  389  THR ALA ARG LEU THR PRO LEU GLU ALA CYS ALA HIS SER          
SEQRES  27 A  389  PHE PHE ASP GLU LEU ARG ASP PRO ASN VAL LYS LEU PRO          
SEQRES  28 A  389  ASN GLY ARG ASP THR PRO ALA LEU PHE ASN PHE THR THR          
SEQRES  29 A  389  GLN GLU LEU SER SER ASN PRO PRO LEU ALA THR ILE LEU          
SEQRES  30 A  389  ILE PRO PRO HIS ALA ARG HIS HIS HIS HIS HIS HIS              
SEQRES   1 B   24  GLY GLY ILE LEU VAL GLU PRO GLN LYS PHE ALA GLU GLU          
SEQRES   2 B   24  LEU ILE HIS ARG LEU GLU ALA VAL GLN ARG THR                  
MODRES 4NM3 SEP A    9  SER  PHOSPHOSERINE                                      
HET    SEP  A   9      10                                                       
HET    GOL  A 401       6                                                       
HET    GOL  A 402       6                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET     MG  A 405       1                                                       
HET     MG  A 406       1                                                       
HET     CL  A 407       1                                                       
HET    DTT  A 408       8                                                       
HET    ADP  A 409      27                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  GOL    4(C3 H8 O3)                                                  
FORMUL   7   MG    2(MG 2+)                                                     
FORMUL   9   CL    CL 1-                                                        
FORMUL  10  DTT    C4 H10 O2 S2                                                 
FORMUL  11  ADP    C10 H15 N5 O10 P2                                            
FORMUL  12  HOH   *197(H2 O)                                                    
HELIX    1   1 ARG A   96  ARG A  102  1                                   7    
HELIX    2   2 VAL A  139  ALA A  149  1                                  11    
HELIX    3   3 PRO A  154  SER A  174  1                                  21    
HELIX    4   4 LYS A  183  GLN A  185  5                                   3    
HELIX    5   5 ALA A  224  PHE A  229  1                                   6    
HELIX    6   6 SER A  236  GLY A  253  1                                  18    
HELIX    7   7 SER A  261  GLY A  274  1                                  14    
HELIX    8   8 THR A  277  ASN A  285  1                                   9    
HELIX    9   9 PRO A  286  THR A  289  5                                   4    
HELIX   10  10 PRO A  300  PHE A  305  1                                   6    
HELIX   11  11 PRO A  310  LEU A  321  1                                  12    
HELIX   12  12 THR A  324  ARG A  328  5                                   5    
HELIX   13  13 THR A  330  ALA A  336  1                                   7    
HELIX   14  14 HIS A  337  ASP A  345  5                                   9    
HELIX   15  15 ASN A  370  PRO A  372  5                                   3    
HELIX   16  16 LEU A  373  ILE A  378  1                                   6    
HELIX   17  18 GLU B  384  ARG B  401  1                                  18    
SHEET    1   A 8 LYS A  27  SER A  29  0                                        
SHEET    2   A 8 VAL A  37  PRO A  44 -1  O  VAL A  37   N  SER A  29           
SHEET    3   A 8 LEU A 112  SER A 118 -1  O  PHE A 115   N  THR A  43           
SHEET    4   A 8 TYR A 127  ASP A 133 -1  O  TYR A 127   N  SER A 118           
SHEET    5   A 8 LEU A  81  LEU A  88 -1  N  VAL A  87   O  LEU A 128           
SHEET    6   A 8 GLY A  68  LEU A  75 -1  N  VAL A  69   O  LYS A  86           
SHEET    7   A 8 GLN A  52  GLY A  65 -1  N  LYS A  60   O  GLN A  72           
SHEET    8   A 8 VAL A  37  PRO A  44 -1  N  VAL A  40   O  VAL A  54           
SHEET    1   B 3 GLU A 137  THR A 138  0                                        
SHEET    2   B 3 LEU A 187  ASP A 190 -1  O  LEU A 189   N  GLU A 137           
SHEET    3   B 3 VAL A 195  LEU A 198 -1  O  LYS A 197   N  LEU A 188           
SHEET    1   C 2 ILE A 177  CYS A 178  0                                        
SHEET    2   C 2 LYS A 205  GLN A 206 -1  O  LYS A 205   N  CYS A 178           
LINK         C   THR A   8                 N   SEP A   9     1555   1555  1.33  
LINK         C   SEP A   9                 N   PHE A  10     1555   1555  1.33  
LINK        MG    MG A 405                 O   HOH A 671     1555   1555  2.05  
LINK        MG    MG A 405                 O1A ADP A 409     1555   1555  2.09  
LINK         OD1 ASN A 186                MG    MG A 405     1555   1555  2.13  
LINK        MG    MG A 406                 O3B ADP A 409     1555   1555  2.20  
LINK         OD2 ASP A 200                MG    MG A 405     1555   1555  2.22  
LINK         OD1 ASP A 200                MG    MG A 406     1555   1555  2.31  
LINK        MG    MG A 405                 O   HOH A 584     1555   1555  2.32  
LINK        MG    MG A 405                 O1B ADP A 409     1555   1555  2.35  
LINK        MG    MG A 406                 O   HOH A 532     1555   1555  2.49  
LINK        MG    MG A 406                 O   HOH A 533     1555   1555  2.80  
LINK         OD2 ASP A 200                MG    MG A 406     1555   1555  2.85  
SITE     1 AC1  5 TYR A  56  TYR A  71  LYS A  86  SER A 118                    
SITE     2 AC1  5 ASN A 129                                                     
SITE     1 AC2  7 ARG A 144  SER A 147  ARG A 148  LEU A 252                    
SITE     2 AC2  7 GLN A 254  PRO A 255  VAL A 304                               
SITE     1 AC3  9 ASP A  49  ARG A  50  PRO A  51  VAL A 142                    
SITE     2 AC3  9 TYR A 146  LEU A 153  TYR A 157  TYR A 161                    
SITE     3 AC3  9 PRO A 191                                                     
SITE     1 AC4  3 LYS A 271  HIS A 299  HOH A 656                               
SITE     1 AC5  5 ASN A 186  ASP A 200  ADP A 409  HOH A 584                    
SITE     2 AC5  5 HOH A 671                                                     
SITE     1 AC6  4 ASP A 200  ADP A 409  HOH A 532  HOH A 533                    
SITE     1 AC7  2 ILE A 296  LYS A 297                                          
SITE     1 AC8  5 ARG A 319  THR A 326  ARG A 328  THR A 330                    
SITE     2 AC8  5 GLU A 333                                                     
SITE     1 AC9 25 GLY A  63  ASN A  64  GLY A  65  SER A  66                    
SITE     2 AC9 25 PHE A  67  GLY A  68  VAL A  70  ALA A  83                    
SITE     3 AC9 25 LYS A  85  VAL A 110  ASP A 133  TYR A 134                    
SITE     4 AC9 25 VAL A 135  THR A 138  ARG A 141  GLN A 185                    
SITE     5 AC9 25 ASN A 186  LEU A 188  ASP A 200   MG A 405                    
SITE     6 AC9 25  MG A 406  HOH A 516  HOH A 532  HOH A 584                    
SITE     7 AC9 25 HOH A 671                                                     
CRYST1   81.032   81.032  281.085  90.00  90.00 120.00 P 61 2 2     12          
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      0.012341  0.007125  0.000000        0.00000                         
SCALE2      0.000000  0.014250  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003558        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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