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Entry: 4EAG
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HEADER    TRANSFERASE                             22-MAR-12   4EAG              
TITLE     CO-CRYSTAL STRUCTURE OF AN CHIMERIC AMPK CORE WITH ATP                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EG:132E8.2 PROTEIN;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 458-582;                                      
COMPND   5 SYNONYM: FI03728P, SNF1A/AMP-ACTIVATED PROTEIN KINASE, SNF1A/AMP-    
COMPND   6 ACTIVATED PROTEIN KINASE, ISOFORM A, SNF1A/AMP-ACTIVATED PROTEIN     
COMPND   7 KINASE, ISOFORM B, SNF1A/AMP-ACTIVATED PROTEIN KINASE, ISOFORM C;    
COMPND   8 EC: 2.7.11.-, 2.7.11.16;                                             
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1;            
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: UNP RESIDUES 187-270;                                      
COMPND  14 SYNONYM: AMPK SUBUNIT BETA-1, AMPKB, 5'-AMP-ACTIVATED PROTEIN KINASE 
COMPND  15 40 KDA SUBUNIT;                                                      
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  19 CHAIN: C;                                                            
COMPND  20 SYNONYM: AMPK GAMMA1, AMPK SUBUNIT GAMMA-1, AMPKG;                   
COMPND  21 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 GENE: SNF1A, EG:132E8.2, SNF1A-RA, CG3051, DMEL_CG3051;              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  11 ORGANISM_COMMON: RAT;                                                
SOURCE  12 ORGANISM_TAXID: 10116;                                               
SOURCE  13 GENE: PRKAB1;                                                        
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  19 ORGANISM_COMMON: RAT;                                                
SOURCE  20 ORGANISM_TAXID: 10116;                                               
SOURCE  21 GENE: PRKAG1;                                                        
SOURCE  22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    AMPK, TRANSFERASE                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.CHEN,J.WANG,Y.-Y.ZHANG,S.F.YAN,D.NEUMANN,U.SCHLATTNER,Z.-X.WANG,J.- 
AUTHOR   2 W.WU                                                                 
REVDAT   2   12-MAR-14 4EAG    1       JRNL                                     
REVDAT   1   06-JUN-12 4EAG    0                                                
JRNL        AUTH   L.CHEN,J.WANG,Y.-Y.ZHANG,S.F.YAN,D.NEUMANN,U.SCHLATTNER,     
JRNL        AUTH 2 Z.-X.WANG,J.-W.WU                                            
JRNL        TITL   AMP-ACTIVATED PROTEIN KINASE UNDERGOES NUCLEOTIDE-DEPENDENT  
JRNL        TITL 2 CONFORMATIONAL CHANGES                                       
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  19   716 2012              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   22659875                                                     
JRNL        DOI    10.1038/NSMB.2319                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 19448                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 982                             
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 29.8625 -  5.1590    0.99     3493   191  0.2223 0.2555        
REMARK   3     2  5.1590 -  4.0982    1.00     3409   193  0.1633 0.1865        
REMARK   3     3  4.0982 -  3.5812    1.00     3385   171  0.1957 0.2516        
REMARK   3     4  3.5812 -  3.2542    0.93     3155   170  0.2327 0.3090        
REMARK   3     5  3.2542 -  3.0212    0.72     2410   123  0.2491 0.3005        
REMARK   3     6  3.0212 -  2.8432    0.51     1724    86  0.2374 0.2691        
REMARK   3     7  2.8432 -  2.7009    0.27      890    48  0.2148 0.2990        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 32.86                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.18230                                             
REMARK   3    B22 (A**2) : -10.62930                                            
REMARK   3    B33 (A**2) : -5.85320                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           3748                                  
REMARK   3   ANGLE     :  1.348           5081                                  
REMARK   3   CHIRALITY :  0.083            598                                  
REMARK   3   PLANARITY :  0.006            604                                  
REMARK   3   DIHEDRAL  : 20.637           1368                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 458:496)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -60.0422 -11.6987   6.8957              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1505 T22:   0.0837                                     
REMARK   3      T33:   0.2073 T12:   0.3038                                     
REMARK   3      T13:   0.0785 T23:   0.1264                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0001 L22:   0.0143                                     
REMARK   3      L33:  -0.0103 L12:  -0.0125                                     
REMARK   3      L13:  -0.0057 L23:   0.0031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0065 S12:   0.0472 S13:   0.0335                       
REMARK   3      S21:  -0.0056 S22:   0.0311 S23:  -0.0432                       
REMARK   3      S31:  -0.1525 S32:   0.0071 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain A and resid 497:500)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -62.6022 -24.0907  10.2762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1709 T22:   0.1680                                     
REMARK   3      T33:   0.2327 T12:   0.1893                                     
REMARK   3      T13:   0.0375 T23:  -0.0501                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0028 L22:   0.0011                                     
REMARK   3      L33:   0.0035 L12:  -0.0009                                     
REMARK   3      L13:  -0.0007 L23:   0.0007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0031 S12:   0.0002 S13:  -0.0039                       
REMARK   3      S21:  -0.0037 S22:   0.0091 S23:  -0.0028                       
REMARK   3      S31:  -0.0063 S32:   0.0018 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain A and resid 501:526)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -57.4971 -15.8079  10.5462              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1323 T22:   0.0941                                     
REMARK   3      T33:   0.0135 T12:   0.2029                                     
REMARK   3      T13:  -0.0496 T23:   0.1762                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0085 L22:   0.0027                                     
REMARK   3      L33:   0.0106 L12:  -0.0024                                     
REMARK   3      L13:  -0.0008 L23:  -0.0112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0422 S12:   0.1368 S13:   0.0485                       
REMARK   3      S21:  -0.0217 S22:  -0.0025 S23:  -0.0219                       
REMARK   3      S31:   0.0166 S32:   0.0105 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain A and resid 527:582)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -52.1316 -23.9571   7.9899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0819 T22:  -0.2989                                     
REMARK   3      T33:   0.0260 T12:   0.2735                                     
REMARK   3      T13:   0.0052 T23:   0.0655                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0171 L22:   0.0049                                     
REMARK   3      L33:  -0.0066 L12:   0.0059                                     
REMARK   3      L13:   0.0078 L23:  -0.0022                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0669 S12:   0.0917 S13:  -0.0334                       
REMARK   3      S21:  -0.0777 S22:   0.0769 S23:   0.0216                       
REMARK   3      S31:  -0.1164 S32:  -0.0464 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (chain B and resid 191:207)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -59.581   -3.957   15.859              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3581 T22:   0.3444                                     
REMARK   3      T33:   0.4461 T12:   0.2820                                     
REMARK   3      T13:  -0.0581 T23:  -0.0607                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0034 L22:  -0.0053                                     
REMARK   3      L33:  -0.0038 L12:   0.0041                                     
REMARK   3      L13:   0.0053 L23:   0.0105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0484 S12:   0.0271 S13:  -0.0927                       
REMARK   3      S21:   0.0169 S22:   0.0464 S23:   0.0305                       
REMARK   3      S31:   0.0414 S32:  -0.0224 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (chain B and resid 211:215)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -42.8199  -6.8006  16.2999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4950 T22:   0.4282                                     
REMARK   3      T33:   0.5270 T12:  -0.0077                                     
REMARK   3      T13:   0.0575 T23:   0.0429                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0001 L22:   0.0010                                     
REMARK   3      L33:  -0.0005 L12:   0.0002                                     
REMARK   3      L13:  -0.0004 L23:  -0.0006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0049 S12:  -0.0019 S13:  -0.0030                       
REMARK   3      S21:   0.0039 S22:  -0.0010 S23:  -0.0027                       
REMARK   3      S31:   0.0009 S32:  -0.0114 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (chain B and resid 220:233)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -43.3056 -13.0144  25.1009              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4138 T22:   0.3591                                     
REMARK   3      T33:   0.3878 T12:   0.0374                                     
REMARK   3      T13:   0.0242 T23:  -0.1208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0054 L22:   0.0176                                     
REMARK   3      L33:   0.0010 L12:   0.0064                                     
REMARK   3      L13:  -0.0006 L23:  -0.0029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0035 S12:   0.0013 S13:   0.0013                       
REMARK   3      S21:   0.0025 S22:  -0.0042 S23:   0.0003                       
REMARK   3      S31:  -0.0003 S32:  -0.0025 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (chain B and resid 234:270)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -43.8270 -19.7054  12.9155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1396 T22:  -0.0415                                     
REMARK   3      T33:  -0.4452 T12:   0.0931                                     
REMARK   3      T13:   0.3790 T23:  -0.0339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0040 L22:   0.0079                                     
REMARK   3      L33:   0.0019 L12:  -0.0130                                     
REMARK   3      L13:  -0.0130 L23:   0.0028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0641 S12:   0.0426 S13:   0.1810                       
REMARK   3      S21:  -0.0789 S22:   0.0049 S23:   0.0376                       
REMARK   3      S31:  -0.0293 S32:   0.0319 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (chain C and resid 26:106)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -32.1570 -31.8302   7.3449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1898 T22:  -0.0548                                     
REMARK   3      T33:  -0.4960 T12:   0.0153                                     
REMARK   3      T13:   0.1565 T23:  -0.1246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0548 L22:  -0.0116                                     
REMARK   3      L33:   0.0073 L12:   0.0027                                     
REMARK   3      L13:   0.0256 L23:  -0.0239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1643 S12:   0.0508 S13:  -0.0607                       
REMARK   3      S21:  -0.0263 S22:  -0.2442 S23:  -0.0434                       
REMARK   3      S31:  -0.0073 S32:   0.1008 S33:   0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (chain C and resid 107:125)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -34.4054 -34.2942  -5.6615              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0184 T22:   0.1678                                     
REMARK   3      T33:   0.0548 T12:   0.0955                                     
REMARK   3      T13:  -0.0564 T23:  -0.0475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0048 L22:  -0.0006                                     
REMARK   3      L33:   0.0037 L12:  -0.0053                                     
REMARK   3      L13:  -0.0021 L23:  -0.0023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0078 S12:   0.0655 S13:   0.0112                       
REMARK   3      S21:  -0.0079 S22:   0.0040 S23:  -0.0122                       
REMARK   3      S31:   0.0433 S32:   0.0069 S33:   0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (chain C and resid 126:202)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -27.4742 -40.7562  22.2100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.9877 T22:  -0.9461                                     
REMARK   3      T33:  -0.0922 T12:   0.7421                                     
REMARK   3      T13:   0.0159 T23:   0.1045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0064 L22:  -0.0239                                     
REMARK   3      L33:  -0.0345 L12:  -0.0255                                     
REMARK   3      L13:   0.0265 L23:  -0.0160                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0024 S12:  -0.2252 S13:   0.0087                       
REMARK   3      S21:   0.0059 S22:  -0.0407 S23:   0.1035                       
REMARK   3      S31:   0.1810 S32:   0.4196 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (chain C and resid 203:265)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2830 -34.2561   1.7213              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3366 T22:   0.1581                                     
REMARK   3      T33:  -0.0311 T12:   0.0263                                     
REMARK   3      T13:   0.0283 T23:  -0.0339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0024 L22:  -0.0141                                     
REMARK   3      L33:  -0.0011 L12:  -0.0005                                     
REMARK   3      L13:  -0.0018 L23:  -0.0073                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0175 S12:   0.0596 S13:   0.0514                       
REMARK   3      S21:   0.0391 S22:   0.0129 S23:   0.0066                       
REMARK   3      S31:   0.0273 S32:   0.0872 S33:   0.0000                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (chain C and resid 266:324)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -11.5151 -37.9314  20.0859              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4914 T22:  -0.2716                                     
REMARK   3      T33:  -0.0189 T12:   0.4816                                     
REMARK   3      T13:   0.2370 T23:  -0.2578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0035 L22:   0.0002                                     
REMARK   3      L33:  -0.0080 L12:   0.0007                                     
REMARK   3      L13:  -0.0105 L23:   0.0058                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0202 S12:   0.0091 S13:   0.0475                       
REMARK   3      S21:  -0.0629 S22:  -0.0340 S23:   0.0198                       
REMARK   3      S31:  -0.1075 S32:   0.2341 S33:  -0.0000                       
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 4EAG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071372.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.02                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99583                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19457                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 15.1                               
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: PDB ENTRY 2V8Q                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, 12% METHANOL, 2% 1,4-BUTANODIOL,    
REMARK 280  PH 6.02 , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.66150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.66150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       54.33400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       75.64150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       54.33400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       75.64150            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       54.66150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       54.33400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       75.64150            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.66150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       54.33400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       75.64150            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   453                                                      
REMARK 465     PRO A   454                                                      
REMARK 465     HIS A   455                                                      
REMARK 465     MET A   456                                                      
REMARK 465     GLY A   457                                                      
REMARK 465     ASN A   532                                                      
REMARK 465     ASP A   533                                                      
REMARK 465     GLU A   534                                                      
REMARK 465     VAL A   535                                                      
REMARK 465     GLU A   536                                                      
REMARK 465     GLN A   537                                                      
REMARK 465     GLY A   538                                                      
REMARK 465     ASP A   539                                                      
REMARK 465     ASP A   540                                                      
REMARK 465     VAL A   541                                                      
REMARK 465     ILE A   542                                                      
REMARK 465     MET A   543                                                      
REMARK 465     GLU A   544                                                      
REMARK 465     SER A   545                                                      
REMARK 465     LEU A   546                                                      
REMARK 465     THR A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     PRO A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     LEU A   551                                                      
REMARK 465     SER A   552                                                      
REMARK 465     VAL A   553                                                      
REMARK 465     SER A   554                                                      
REMARK 465     GLY A   555                                                      
REMARK 465     VAL A   556                                                      
REMARK 465     MET A   557                                                      
REMARK 465     PRO A   558                                                      
REMARK 465     TYR B   192                                                      
REMARK 465     ILE B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     LYS B   195                                                      
REMARK 465     PRO B   196                                                      
REMARK 465     GLU B   197                                                      
REMARK 465     GLU B   198                                                      
REMARK 465     ARG B   199                                                      
REMARK 465     PHE B   200                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     PRO B   208                                                      
REMARK 465     HIS B   209                                                      
REMARK 465     LEU B   210                                                      
REMARK 465     ASN B   216                                                      
REMARK 465     LYS B   217                                                      
REMARK 465     ASP B   218                                                      
REMARK 465     THR B   219                                                      
REMARK 465     CYS B   223                                                      
REMARK 465     ASP B   224                                                      
REMARK 465     PRO B   225                                                      
REMARK 465     ALA B   226                                                      
REMARK 465     LEU B   227                                                      
REMARK 465     LEU B   228                                                      
REMARK 465     PRO B   229                                                      
REMARK 465     GLU B   230                                                      
REMARK 465     PRO B   231                                                      
REMARK 465     ASN B   232                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     GLU C    13                                                      
REMARK 465     ASN C    14                                                      
REMARK 465     GLU C    15                                                      
REMARK 465     HIS C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     GLN C    18                                                      
REMARK 465     GLU C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     PRO C    21                                                      
REMARK 465     GLU C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     ASN C    24                                                      
REMARK 465     SER C    25                                                      
REMARK 465     GLU C   251                                                      
REMARK 465     LYS C   252                                                      
REMARK 465     THR C   253                                                      
REMARK 465     TYR C   254                                                      
REMARK 465     ASN C   255                                                      
REMARK 465     SER C   269                                                      
REMARK 465     HIS C   270                                                      
REMARK 465     TYR C   271                                                      
REMARK 465     PHE C   272                                                      
REMARK 465     GLU C   273                                                      
REMARK 465     GLY C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLU C   327                                                      
REMARK 465     LYS C   328                                                      
REMARK 465     LYS C   329                                                      
REMARK 465     PRO C   330                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 492      166.82    167.78                                   
REMARK 500    PRO A 493       12.63    -65.60                                   
REMARK 500    TYR A 494       12.65   -142.58                                   
REMARK 500    ASP A 519     -140.42   -122.19                                   
REMARK 500    PHE A 569      -70.45    -51.63                                   
REMARK 500    GLN B 212      -49.30    159.22                                   
REMARK 500    ASN B 237        0.95     91.31                                   
REMARK 500    ALA B 253      137.84   -179.20                                   
REMARK 500    LYS B 258     -127.28     57.90                                   
REMARK 500    VAL C  56      -54.01    -28.28                                   
REMARK 500    GLU C 110       34.48   -148.92                                   
REMARK 500    LYS C 126       77.35   -117.78                                   
REMARK 500    LYS C 190      172.04    -53.66                                   
REMARK 500    THR C 210      134.35    -39.40                                   
REMARK 500    ARG C 223       67.83     61.88                                   
REMARK 500    ASP C 238     -156.95   -170.60                                   
REMARK 500    ALA C 249       65.32    -56.56                                   
REMARK 500    LEU C 257       -6.26     82.97                                   
REMARK 500    HIS C 267       31.47    178.59                                   
REMARK 500    GLU C 295      -17.11     84.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAM C 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EAI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EAJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EAK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EAL   RELATED DB: PDB                                   
DBREF  4EAG A  458   582  UNP    O18645   O18645_DROME   458    582             
DBREF  4EAG B  187   270  UNP    P80386   AAKB1_RAT      187    270             
DBREF  4EAG C    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQADV 4EAG GLY A  453  UNP  O18645              EXPRESSION TAG                 
SEQADV 4EAG PRO A  454  UNP  O18645              EXPRESSION TAG                 
SEQADV 4EAG HIS A  455  UNP  O18645              EXPRESSION TAG                 
SEQADV 4EAG MET A  456  UNP  O18645              EXPRESSION TAG                 
SEQADV 4EAG GLY A  457  UNP  O18645              EXPRESSION TAG                 
SEQADV 4EAG MET B  186  UNP  P80386              EXPRESSION TAG                 
SEQRES   1 A  130  GLY PRO HIS MET GLY ALA LYS TRP HIS LEU GLY ILE ARG          
SEQRES   2 A  130  SER GLN SER LYS PRO ASN ASP ILE MET LEU GLU VAL TYR          
SEQRES   3 A  130  ARG ALA MET LYS ALA LEU SER TYR GLU TRP LYS ILE ILE          
SEQRES   4 A  130  ASN PRO TYR HIS VAL ARG VAL ARG ARG GLN ASN VAL LYS          
SEQRES   5 A  130  THR GLY LYS PHE SER LYS MET SER LEU GLN LEU TYR GLN          
SEQRES   6 A  130  VAL ASP ALA LYS SER TYR LEU LEU ASP PHE LYS SER LEU          
SEQRES   7 A  130  THR ASN ASP GLU VAL GLU GLN GLY ASP ASP VAL ILE MET          
SEQRES   8 A  130  GLU SER LEU THR PRO PRO PRO LEU SER VAL SER GLY VAL          
SEQRES   9 A  130  MET PRO LEU GLN PRO THR GLY HIS HIS THR MET GLU PHE          
SEQRES  10 A  130  PHE GLU MET CYS ALA ALA LEU ILE ILE GLN LEU ALA ARG          
SEQRES   1 B   85  MET TYR HIS GLN GLU PRO TYR ILE SER LYS PRO GLU GLU          
SEQRES   2 B   85  ARG PHE LYS ALA PRO PRO ILE LEU PRO PRO HIS LEU LEU          
SEQRES   3 B   85  GLN VAL ILE LEU ASN LYS ASP THR GLY ILE SER CYS ASP          
SEQRES   4 B   85  PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET LEU ASN          
SEQRES   5 B   85  HIS LEU TYR ALA LEU SER ILE LYS ASP GLY VAL MET VAL          
SEQRES   6 B   85  LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR VAL THR          
SEQRES   7 B   85  THR LEU LEU TYR LYS PRO ILE                                  
SEQRES   1 C  330  MET GLU SER VAL ALA ALA GLU SER ALA PRO ALA PRO GLU          
SEQRES   2 C  330  ASN GLU HIS SER GLN GLU THR PRO GLU SER ASN SER SER          
SEQRES   3 C  330  VAL TYR THR THR PHE MET LYS SER HIS ARG CYS TYR ASP          
SEQRES   4 C  330  LEU ILE PRO THR SER SER LYS LEU VAL VAL PHE ASP THR          
SEQRES   5 C  330  SER LEU GLN VAL LYS LYS ALA PHE PHE ALA LEU VAL THR          
SEQRES   6 C  330  ASN GLY VAL ARG ALA ALA PRO LEU TRP ASP SER LYS LYS          
SEQRES   7 C  330  GLN SER PHE VAL GLY MET LEU THR ILE THR ASP PHE ILE          
SEQRES   8 C  330  ASN ILE LEU HIS ARG TYR TYR LYS SER ALA LEU VAL GLN          
SEQRES   9 C  330  ILE TYR GLU LEU GLU GLU HIS LYS ILE GLU THR TRP ARG          
SEQRES  10 C  330  GLU VAL TYR LEU GLN ASP SER PHE LYS PRO LEU VAL CYS          
SEQRES  11 C  330  ILE SER PRO ASN ALA SER LEU PHE ASP ALA VAL SER SER          
SEQRES  12 C  330  LEU ILE ARG ASN LYS ILE HIS ARG LEU PRO VAL ILE ASP          
SEQRES  13 C  330  PRO GLU SER GLY ASN THR LEU TYR ILE LEU THR HIS LYS          
SEQRES  14 C  330  ARG ILE LEU LYS PHE LEU LYS LEU PHE ILE THR GLU PHE          
SEQRES  15 C  330  PRO LYS PRO GLU PHE MET SER LYS SER LEU GLU GLU LEU          
SEQRES  16 C  330  GLN ILE GLY THR TYR ALA ASN ILE ALA MET VAL ARG THR          
SEQRES  17 C  330  THR THR PRO VAL TYR VAL ALA LEU GLY ILE PHE VAL GLN          
SEQRES  18 C  330  HIS ARG VAL SER ALA LEU PRO VAL VAL ASP GLU LYS GLY          
SEQRES  19 C  330  ARG VAL VAL ASP ILE TYR SER LYS PHE ASP VAL ILE ASN          
SEQRES  20 C  330  LEU ALA ALA GLU LYS THR TYR ASN ASN LEU ASP VAL SER          
SEQRES  21 C  330  VAL THR LYS ALA LEU GLN HIS ARG SER HIS TYR PHE GLU          
SEQRES  22 C  330  GLY VAL LEU LYS CYS TYR LEU HIS GLU THR LEU GLU ALA          
SEQRES  23 C  330  ILE ILE ASN ARG LEU VAL GLU ALA GLU VAL HIS ARG LEU          
SEQRES  24 C  330  VAL VAL VAL ASP GLU HIS ASP VAL VAL LYS GLY ILE VAL          
SEQRES  25 C  330  SER LEU SER ASP ILE LEU GLN ALA LEU VAL LEU THR GLY          
SEQRES  26 C  330  GLY GLU LYS LYS PRO                                          
HET    ATP  C 401      31                                                       
HET    ATP  C 402      31                                                       
HET    TAM  C 403      11                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     TAM TRIS(HYDROXYETHYL)AMINOMETHANE                                   
FORMUL   4  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   6  TAM    C7 H17 N O3                                                  
FORMUL   7  HOH   *81(H2 O)                                                     
HELIX    1   1 LYS A  469  LEU A  484  1                                  16    
HELIX    2   2 HIS A  564  ARG A  582  1                                  19    
HELIX    3   3 VAL C   27  LYS C   33  1                                   7    
HELIX    4   4 ARG C   36  ILE C   41  5                                   6    
HELIX    5   5 GLN C   55  ASN C   66  1                                  12    
HELIX    6   6 THR C   86  SER C  100  1                                  15    
HELIX    7   7 LEU C  102  GLU C  107  1                                   6    
HELIX    8   8 LYS C  112  TYR C  120  1                                   9    
HELIX    9   9 LEU C  121  LYS C  126  1                                   6    
HELIX   10  10 SER C  136  ASN C  147  1                                  12    
HELIX   11  11 THR C  167  GLU C  181  1                                  15    
HELIX   12  12 GLU C  186  LYS C  190  5                                   5    
HELIX   13  13 SER C  191  GLN C  196  1                                   6    
HELIX   14  14 PRO C  211  ARG C  223  1                                  13    
HELIX   15  15 LYS C  242  ALA C  249  1                                   8    
HELIX   16  16 SER C  260  LEU C  265  1                                   6    
HELIX   17  17 THR C  283  GLU C  295  1                                  13    
HELIX   18  18 LEU C  314  VAL C  322  1                                   9    
SHEET    1   A 8 VAL B 213  ILE B 214  0                                        
SHEET    2   A 8 TRP A 460  LEU A 462 -1  N  TRP A 460   O  ILE B 214           
SHEET    3   A 8 TYR B 240  LEU B 242 -1  O  ALA B 241   N  HIS A 461           
SHEET    4   A 8 VAL B 248  TYR B 257 -1  O  SER B 252   N  TYR B 240           
SHEET    5   A 8 LYS B 260  PRO B 269 -1  O  LYS B 268   N  MET B 249           
SHEET    6   A 8 SER C  44  ASP C  51  1  O  VAL C  49   N  LEU B 265           
SHEET    7   A 8 ALA C  71  ASP C  75  1  O  TRP C  74   N  PHE C  50           
SHEET    8   A 8 SER C  80  LEU C  85 -1  O  LEU C  85   N  ALA C  71           
SHEET    1   B 4 GLU A 487  ASN A 492  0                                        
SHEET    2   B 4 HIS A 495  GLN A 501 -1  O  ARG A 499   N  GLU A 487           
SHEET    3   B 4 PHE A 508  GLN A 517 -1  O  LEU A 513   N  VAL A 496           
SHEET    4   B 4 TYR A 523  SER A 529 -1  O  LYS A 528   N  SER A 512           
SHEET    1   C 2 ILE B 221  SER B 222  0                                        
SHEET    2   C 2 VAL B 234  MET B 235  1  O  VAL B 234   N  SER B 222           
SHEET    1   D 2 LEU C 152  ILE C 155  0                                        
SHEET    2   D 2 THR C 162  LEU C 166 -1  O  TYR C 164   N  VAL C 154           
SHEET    1   E 3 VAL C 206  ARG C 207  0                                        
SHEET    2   E 3 ALA C 226  VAL C 230  1  O  PRO C 228   N  VAL C 206           
SHEET    3   E 3 VAL C 236  SER C 241 -1  O  TYR C 240   N  LEU C 227           
SHEET    1   F 3 LYS C 277  CYS C 278  0                                        
SHEET    2   F 3 ARG C 298  VAL C 302  1  O  VAL C 302   N  CYS C 278           
SHEET    3   F 3 VAL C 308  SER C 313 -1  O  VAL C 312   N  LEU C 299           
SITE     1 AC1 17 MET C  84  THR C  86  ILE C  87  THR C  88                    
SITE     2 AC1 17 ASP C  89  GLN C 122  PRO C 127  LEU C 128                    
SITE     3 AC1 17 VAL C 129  ILE C 149  HIS C 150  ARG C 151                    
SITE     4 AC1 17 PRO C 153  SER C 225  PHE C 243  HOH C 509                    
SITE     5 AC1 17 HOH C 539                                                     
SITE     1 AC2 15 HIS C 150  THR C 199  ALA C 204  VAL C 224                    
SITE     2 AC2 15 SER C 225  ALA C 226  PRO C 228  HIS C 297                    
SITE     3 AC2 15 ARG C 298  SER C 313  LEU C 314  SER C 315                    
SITE     4 AC2 15 ASP C 316  HOH C 515  HOH C 538                               
SITE     1 AC3 11 VAL C  68  ARG C  69  ARG C 151  THR C 167                    
SITE     2 AC3 11 LYS C 169  ARG C 170  HIS C 297  HOH C 503                    
SITE     3 AC3 11 HOH C 521  HOH C 527  HOH C 536                               
CRYST1  108.668  151.283  109.323  90.00  90.00  90.00 C 2 2 21      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      0.009202  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006610  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009147        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system