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Database: PDB
Entry: 4EAK
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HEADER    TRANSFERASE                             22-MAR-12   4EAK              
TITLE     CO-CRYSTAL STRUCTURE OF AN AMPK CORE WITH ATP                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AMPK SUBUNIT ALPHA-1,ACETYL-COA CARBOXYLASE KINASE,ACACA    
COMPND   5 KINASE,HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE,HMGCR KINASE,TAU-  
COMPND   6 PROTEIN KINASE PRKAA1;                                               
COMPND   7 EC: 2.7.11.1,2.7.11.27,2.7.11.31,2.7.11.26;                          
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: CHIMERA PROTEIN OF RESIDUES 405-479 AND RESIDUES 540- 
COMPND  10 559 FROM 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1   
COMPND  11 (UNIPROT P54645), LINKED BY LINKER GGGGGG;                           
COMPND  12 MOL_ID: 2;                                                           
COMPND  13 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1;            
COMPND  14 CHAIN: B;                                                            
COMPND  15 FRAGMENT: UNP RESIDUES 200-270;                                      
COMPND  16 SYNONYM: AMPKB,5'-AMP-ACTIVATED PROTEIN KINASE 40 KDA SUBUNIT;       
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 3;                                                           
COMPND  19 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  20 CHAIN: C;                                                            
COMPND  21 SYNONYM: AMPKG;                                                      
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: PRKAA1, AMPK1;                                                 
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   3   21-JUN-17 4EAK    1       COMPND SOURCE                            
REVDAT   2   12-MAR-14 4EAK    1       JRNL                                     
REVDAT   1   06-JUN-12 4EAK    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.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.5_2                                         
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.130                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 17922                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.238                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 908                             
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 28.6328 -  4.5325    1.00     3065   165  0.2392 0.2529        
REMARK   3     2  4.5325 -  3.5998    0.99     2971   166  0.2033 0.2026        
REMARK   3     3  3.5998 -  3.1454    0.98     2900   176  0.2312 0.2680        
REMARK   3     4  3.1454 -  2.8581    0.96     2849   122  0.2467 0.2832        
REMARK   3     5  2.8581 -  2.6534    0.92     2709   144  0.2643 0.2878        
REMARK   3     6  2.6534 -  2.4971    0.86     2520   135  0.2666 0.2876        
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              : 0.34                                          
REMARK   3   B_SOL              : 70.49                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 57.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.90110                                              
REMARK   3    B22 (A**2) : 5.52090                                              
REMARK   3    B33 (A**2) : -9.42190                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -7.39090                                             
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           3530                                  
REMARK   3   ANGLE     :  0.964           4791                                  
REMARK   3   CHIRALITY :  0.055            567                                  
REMARK   3   PLANARITY :  0.008            574                                  
REMARK   3   DIHEDRAL  : 19.743           1293                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 17                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 396:406)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  30.1286 395.6968 -20.6769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5288 T22:   0.8658                                     
REMARK   3      T33:   0.6283 T12:  -0.0203                                     
REMARK   3      T13:  -0.1307 T23:   0.3285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8950 L22:   0.5744                                     
REMARK   3      L33:   0.6541 L12:  -0.2240                                     
REMARK   3      L13:   0.1941 L23:   0.3277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1302 S12:   0.0051 S13:  -0.6701                       
REMARK   3      S21:  -0.2228 S22:  -0.4312 S23:   0.0103                       
REMARK   3      S31:  -0.2575 S32:   0.3030 S33:   0.3768                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 407:414)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  35.7301 402.6054 -11.4011              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4340 T22:   1.5940                                     
REMARK   3      T33:   0.6084 T12:  -0.2642                                     
REMARK   3      T13:  -0.2558 T23:   0.2710                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0020 L22:   0.6470                                     
REMARK   3      L33:   0.0823 L12:  -0.0200                                     
REMARK   3      L13:   0.0138 L23:  -0.2342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0652 S12:  -0.5424 S13:   0.2191                       
REMARK   3      S21:  -0.0128 S22:  -0.2844 S23:  -0.4221                       
REMARK   3      S31:  -0.4512 S32:   0.9802 S33:   0.2451                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 415:439)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3628 403.4301  -4.1787              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5308 T22:   1.2514                                     
REMARK   3      T33:   0.6221 T12:  -0.1987                                     
REMARK   3      T13:  -0.1646 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5148 L22:   2.0732                                     
REMARK   3      L33:   2.8695 L12:   0.7791                                     
REMARK   3      L13:  -1.4227 L23:  -0.1179                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0953 S12:  -1.0594 S13:  -0.0669                       
REMARK   3      S21:   0.3113 S22:   0.0212 S23:   0.3322                       
REMARK   3      S31:  -0.0807 S32:   1.3608 S33:  -0.0378                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 440:458)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9462 396.6461 -10.6189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6366 T22:   0.8106                                     
REMARK   3      T33:   0.5183 T12:  -0.0956                                     
REMARK   3      T13:  -0.0870 T23:   0.2399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8080 L22:   1.0575                                     
REMARK   3      L33:   1.8292 L12:   0.8085                                     
REMARK   3      L13:  -0.5178 L23:  -1.2415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2463 S12:   0.1701 S13:  -0.5422                       
REMARK   3      S21:   0.4778 S22:  -1.0302 S23:  -0.1840                       
REMARK   3      S31:  -0.7186 S32:   0.7533 S33:   0.4510                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 459:467)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4307 393.6037 -11.4138              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3472 T22:   0.5844                                     
REMARK   3      T33:   0.7065 T12:  -0.0413                                     
REMARK   3      T13:  -0.0917 T23:   0.2153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8371 L22:   0.5594                                     
REMARK   3      L33:   0.5298 L12:   0.7637                                     
REMARK   3      L13:  -0.5570 L23:  -0.5228                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2269 S12:  -0.8023 S13:  -0.4644                       
REMARK   3      S21:  -0.1153 S22:  -0.0224 S23:   0.4756                       
REMARK   3      S31:   0.2031 S32:   0.0900 S33:  -0.3660                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 529:548)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7494 403.6304 -13.4959              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2827 T22:   0.3175                                     
REMARK   3      T33:   0.2153 T12:  -0.1129                                     
REMARK   3      T13:  -0.0220 T23:  -0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1358 L22:   1.3003                                     
REMARK   3      L33:   0.7936 L12:   0.0738                                     
REMARK   3      L13:  -0.6316 L23:  -0.1728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1222 S12:  -0.4079 S13:   0.0208                       
REMARK   3      S21:   0.5446 S22:  -0.0198 S23:  -0.0578                       
REMARK   3      S31:   0.0089 S32:   0.4721 S33:  -0.1214                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 202:235)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2496 385.7075 -13.1832              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9723 T22:   0.6588                                     
REMARK   3      T33:   0.9821 T12:   0.4045                                     
REMARK   3      T13:   0.0468 T23:   0.1391                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7998 L22:   3.1936                                     
REMARK   3      L33:   2.2822 L12:  -1.0416                                     
REMARK   3      L13:  -0.0079 L23:   0.5216                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6763 S12:   0.0089 S13:  -0.1547                       
REMARK   3      S21:  -0.1548 S22:  -0.4713 S23:   1.3778                       
REMARK   3      S31:   0.3565 S32:   0.0443 S33:   0.5599                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 236:243)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4796 392.6997 -17.8311              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6202 T22:   0.4464                                     
REMARK   3      T33:   0.5175 T12:   0.0240                                     
REMARK   3      T13:  -0.0661 T23:   0.0877                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2965 L22:   2.2287                                     
REMARK   3      L33:   1.1114 L12:  -0.6654                                     
REMARK   3      L13:   0.8540 L23:  -0.2039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4989 S12:  -0.0866 S13:  -0.3416                       
REMARK   3      S21:  -0.6441 S22:  -0.0957 S23:  -0.2686                       
REMARK   3      S31:   0.1061 S32:  -0.1594 S33:  -0.1513                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 244:256)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6763 398.0009 -20.9610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5416 T22:   0.4313                                     
REMARK   3      T33:   0.3993 T12:   0.0411                                     
REMARK   3      T13:   0.0674 T23:   0.0328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6710 L22:   1.0293                                     
REMARK   3      L33:   1.8974 L12:  -0.5048                                     
REMARK   3      L13:   0.4406 L23:  -0.5003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1713 S12:  -0.0306 S13:  -0.2709                       
REMARK   3      S21:  -0.0511 S22:  -0.4019 S23:   0.2490                       
REMARK   3      S31:  -0.0491 S32:   0.5036 S33:   0.2421                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 257:270)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   8.7105 393.9159 -15.7158              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2391 T22:   0.2618                                     
REMARK   3      T33:   0.3690 T12:   0.0597                                     
REMARK   3      T13:   0.0102 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4973 L22:   1.4089                                     
REMARK   3      L33:   0.1598 L12:   0.8149                                     
REMARK   3      L13:  -0.1043 L23:  -0.5383                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1573 S12:   0.1024 S13:  -0.2164                       
REMARK   3      S21:   0.0653 S22:  -0.1441 S23:  -0.1912                       
REMARK   3      S31:  -0.0162 S32:  -0.0258 S33:  -0.0935                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 23:94)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5397 398.1005 -19.2701              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3470 T22:   0.1925                                     
REMARK   3      T33:   0.2257 T12:   0.0174                                     
REMARK   3      T13:   0.0204 T23:  -0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8225 L22:  -0.0717                                     
REMARK   3      L33:   0.3928 L12:   0.1448                                     
REMARK   3      L13:  -0.1789 L23:  -0.4414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0634 S12:  -0.0615 S13:   0.0286                       
REMARK   3      S21:  -0.1285 S22:  -0.0240 S23:   0.0258                       
REMARK   3      S31:  -0.0643 S32:  -0.0134 S33:  -0.0042                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 95:111)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.4615 416.4443 -31.8801              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0293 T22:   0.4650                                     
REMARK   3      T33:   0.8367 T12:   0.0513                                     
REMARK   3      T13:   0.2425 T23:   0.0655                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1605 L22:   0.0181                                     
REMARK   3      L33:   0.3803 L12:  -0.1981                                     
REMARK   3      L13:   0.2594 L23:  -0.0608                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0124 S12:   0.0003 S13:   0.7625                       
REMARK   3      S21:  -0.9574 S22:   0.0435 S23:   0.0220                       
REMARK   3      S31:  -0.2424 S32:   0.0611 S33:   0.0131                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 112:180)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6289 398.3392 -15.1504              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2028 T22:   0.1490                                     
REMARK   3      T33:   0.1937 T12:   0.0437                                     
REMARK   3      T13:   0.0433 T23:  -0.0697                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4805 L22:   0.3753                                     
REMARK   3      L33:   0.5234 L12:   0.0769                                     
REMARK   3      L13:   0.2813 L23:  -0.3908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0460 S12:  -0.1036 S13:   0.1014                       
REMARK   3      S21:  -0.0355 S22:  -0.0952 S23:  -0.1144                       
REMARK   3      S31:  -0.0818 S32:  -0.1002 S33:   0.0512                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 181:196)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2132 381.7267 -19.5384              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5528 T22:   0.9779                                     
REMARK   3      T33:   0.3747 T12:  -0.3172                                     
REMARK   3      T13:  -0.3202 T23:  -0.2292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9247 L22:   1.3310                                     
REMARK   3      L33:   1.9142 L12:   0.9606                                     
REMARK   3      L13:  -1.1212 L23:   0.9054                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1373 S12:   0.7048 S13:   0.8048                       
REMARK   3      S21:   0.7179 S22:   0.3364 S23:   0.4195                       
REMARK   3      S31:  -0.0191 S32:  -1.0687 S33:  -0.0994                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 197:251)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -19.0559 403.8841 -37.1389              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3295 T22:   0.4292                                     
REMARK   3      T33:   0.3108 T12:   0.1477                                     
REMARK   3      T13:  -0.0530 T23:  -0.0690                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0522 L22:   0.9405                                     
REMARK   3      L33:   0.8765 L12:   0.4047                                     
REMARK   3      L13:  -0.0842 L23:   0.2154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1467 S12:   0.1694 S13:  -0.1751                       
REMARK   3      S21:  -0.0194 S22:  -0.2221 S23:   0.0604                       
REMARK   3      S31:  -0.3966 S32:  -0.3601 S33:   0.1163                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 252:296)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -17.7087 393.1943 -36.9261              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3051 T22:   0.4572                                     
REMARK   3      T33:   0.2849 T12:  -0.0739                                     
REMARK   3      T13:  -0.0576 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2362 L22:   0.4022                                     
REMARK   3      L33:   1.4712 L12:  -0.0736                                     
REMARK   3      L13:  -0.5286 L23:  -0.1372                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0948 S12:   0.2934 S13:  -0.0574                       
REMARK   3      S21:  -0.3485 S22:  -0.1147 S23:  -0.0239                       
REMARK   3      S31:   0.3694 S32:  -0.3535 S33:  -0.0210                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 297:324)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -25.1702 392.6125 -28.0591              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2309 T22:   0.7146                                     
REMARK   3      T33:   0.3563 T12:  -0.0469                                     
REMARK   3      T13:   0.0360 T23:  -0.0484                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7090 L22:   0.7324                                     
REMARK   3      L33:   0.6593 L12:  -0.2193                                     
REMARK   3      L13:  -0.3639 L23:  -0.4685                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3499 S12:   0.6421 S13:  -0.1728                       
REMARK   3      S21:   0.0764 S22:   0.3341 S23:  -0.2254                       
REMARK   3      S31:  -0.0156 S32:  -0.7072 S33:  -0.1207                       
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 4EAK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-APR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071376.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.9                                
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) : NULL                               
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   : 18796                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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   (%): 47.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 5.9, 18% IPP, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298 K                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       88.27900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.25400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       88.27900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       20.25400            
REMARK 290   SMTRY3   4  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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   389                                                      
REMARK 465     PRO A   390                                                      
REMARK 465     HIS A   391                                                      
REMARK 465     MET A   392                                                      
REMARK 465     GLY A   393                                                      
REMARK 465     ALA A   394                                                      
REMARK 465     LYS A   395                                                      
REMARK 465     ASP A   522                                                      
REMARK 465     GLY A   523                                                      
REMARK 465     GLY A   524                                                      
REMARK 465     GLY A   525                                                      
REMARK 465     GLY A   526                                                      
REMARK 465     GLY A   527                                                      
REMARK 465     GLY A   528                                                      
REMARK 465     MET B   199                                                      
REMARK 465     PHE B   200                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     LEU B   206                                                      
REMARK 465     PRO B   207                                                      
REMARK 465     PRO B   208                                                      
REMARK 465     HIS B   209                                                      
REMARK 465     LEU B   210                                                      
REMARK 465     LEU B   211                                                      
REMARK 465     GLN B   212                                                      
REMARK 465     VAL B   213                                                      
REMARK 465     ILE B   214                                                      
REMARK 465     LEU B   215                                                      
REMARK 465     ASN B   216                                                      
REMARK 465     LYS B   217                                                      
REMARK 465     ASP B   218                                                      
REMARK 465     THR B   219                                                      
REMARK 465     GLY B   220                                                      
REMARK 465     ILE B   221                                                      
REMARK 465     SER B   222                                                      
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     TYR C    97                                                      
REMARK 465     TYR C    98                                                      
REMARK 465     LYS C    99                                                      
REMARK 465     SER C   100                                                      
REMARK 465     ALA C   101                                                      
REMARK 465     LEU C   102                                                      
REMARK 465     VAL C   103                                                      
REMARK 465     GLN C   104                                                      
REMARK 465     ILE C   105                                                      
REMARK 465     TYR C   106                                                      
REMARK 465     TYR C   254                                                      
REMARK 465     ASN C   255                                                      
REMARK 465     HIS C   270                                                      
REMARK 465     TYR C   271                                                      
REMARK 465     PHE C   272                                                      
REMARK 465     GLU C   273                                                      
REMARK 465     GLY C   274                                                      
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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 203   C   -  N   -  CD  ANGL. DEV. = -14.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU B 236      119.23    -29.84                                   
REMARK 500    ASN B 237        3.34     86.28                                   
REMARK 500    LYS B 258     -125.57     56.48                                   
REMARK 500    LYS C 126       76.51   -114.07                                   
REMARK 500    PRO C 183      134.01    -38.97                                   
REMARK 500    LEU C 257      -25.50     80.32                                   
REMARK 500    ARG C 268      179.97    -54.77                                   
REMARK 500    GLU C 295       38.05     38.62                                   
REMARK 500    ASP C 306        7.87     84.55                                   
REMARK 500    VAL C 322      -64.83    -91.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 549        DISTANCE =  6.71 ANGSTROMS                       
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: 4EAG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EAI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EAJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EAL   RELATED DB: PDB                                   
DBREF  4EAK A  394   522  UNP    P54645   AAPK1_RAT      405    479             
DBREF  4EAK A  529   548  UNP    P54645   AAPK1_RAT      540    559             
DBREF  4EAK B  200   270  UNP    P80386   AAKB1_RAT      200    270             
DBREF  4EAK C    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQADV 4EAK GLY A  389  UNP  P54645              EXPRESSION TAG                 
SEQADV 4EAK PRO A  390  UNP  P54645              EXPRESSION TAG                 
SEQADV 4EAK HIS A  391  UNP  P54645              EXPRESSION TAG                 
SEQADV 4EAK MET A  392  UNP  P54645              EXPRESSION TAG                 
SEQADV 4EAK GLY A  393  UNP  P54645              EXPRESSION TAG                 
SEQADV 4EAK GLY A  523  UNP  P54645              LINKER                         
SEQADV 4EAK GLY A  524  UNP  P54645              LINKER                         
SEQADV 4EAK GLY A  525  UNP  P54645              LINKER                         
SEQADV 4EAK GLY A  526  UNP  P54645              LINKER                         
SEQADV 4EAK GLY A  527  UNP  P54645              LINKER                         
SEQADV 4EAK GLY A  528  UNP  P54645              LINKER                         
SEQADV 4EAK MET B  199  UNP  P80386              EXPRESSION TAG                 
SEQRES   1 A  106  GLY PRO HIS MET GLY ALA LYS TRP HIS LEU GLY ILE ARG          
SEQRES   2 A  106  SER GLN SER ARG PRO ASN ASP ILE MET ALA GLU VAL CYS          
SEQRES   3 A  106  ARG ALA ILE LYS GLN LEU ASP TYR GLU TRP LYS VAL VAL          
SEQRES   4 A  106  ASN PRO TYR TYR LEU ARG VAL ARG ARG LYS ASN PRO VAL          
SEQRES   5 A  106  THR SER THR PHE SER LYS MET SER LEU GLN LEU TYR GLN          
SEQRES   6 A  106  VAL ASP SER ARG THR TYR LEU LEU ASP PHE ARG SER ILE          
SEQRES   7 A  106  ASP ASP GLY GLY GLY GLY GLY GLY GLY SER HIS THR ILE          
SEQRES   8 A  106  GLU PHE PHE GLU MET CYS ALA ASN LEU ILE LYS ILE LEU          
SEQRES   9 A  106  ALA GLN                                                      
SEQRES   1 B   72  MET PHE LYS ALA PRO PRO ILE LEU PRO PRO HIS LEU LEU          
SEQRES   2 B   72  GLN VAL ILE LEU ASN LYS ASP THR GLY ILE SER CYS ASP          
SEQRES   3 B   72  PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET LEU ASN          
SEQRES   4 B   72  HIS LEU TYR ALA LEU SER ILE LYS ASP GLY VAL MET VAL          
SEQRES   5 B   72  LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR VAL THR          
SEQRES   6 B   72  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   *74(H2 O)                                                     
HELIX    1   1 ARG A  405  ASP A  421  1                                  17    
HELIX    2   2 SER A  530  GLN A  548  1                                  19    
HELIX    3   3 SER C   26  HIS C   35  1                                  10    
HELIX    4   4 ARG C   36  ILE C   41  5                                   6    
HELIX    5   5 GLN C   55  GLY C   67  1                                  13    
HELIX    6   6 THR C   86  HIS C   95  1                                  10    
HELIX    7   7 LYS C  112  TYR C  120  1                                   9    
HELIX    8   8 LEU C  121  LYS C  126  1                                   6    
HELIX    9   9 SER C  136  ASN C  147  1                                  12    
HELIX   10  10 THR C  167  PHE C  182  1                                  16    
HELIX   11  11 PRO C  185  SER C  189  5                                   5    
HELIX   12  12 SER C  191  GLN C  196  1                                   6    
HELIX   13  13 PRO C  211  ARG C  223  1                                  13    
HELIX   14  14 LYS C  242  GLU C  251  1                                  10    
HELIX   15  15 SER C  260  GLN C  266  1                                   7    
HELIX   16  16 THR C  283  ALA C  294  1                                  12    
HELIX   17  17 LEU C  314  VAL C  322  1                                   9    
SHEET    1   A 7 HIS A 397  LEU A 398  0                                        
SHEET    2   A 7 TYR B 240  ALA B 241 -1  O  ALA B 241   N  HIS A 397           
SHEET    3   A 7 VAL B 248  TYR B 257 -1  O  SER B 252   N  TYR B 240           
SHEET    4   A 7 LYS B 260  PRO B 269 -1  O  LYS B 260   N  TYR B 257           
SHEET    5   A 7 SER C  44  ASP C  51  1  O  VAL C  49   N  LEU B 265           
SHEET    6   A 7 ALA C  71  ASP C  75  1  O  TRP C  74   N  PHE C  50           
SHEET    7   A 7 SER C  80  LEU C  85 -1  O  SER C  80   N  ASP C  75           
SHEET    1   B 5 ILE A 400  SER A 402  0                                        
SHEET    2   B 5 TYR A 459  SER A 465 -1  O  LEU A 461   N  ILE A 400           
SHEET    3   B 5 PHE A 444  GLN A 453 -1  N  SER A 448   O  ARG A 464           
SHEET    4   B 5 TYR A 431  LYS A 437 -1  N  LEU A 432   O  LEU A 449           
SHEET    5   B 5 GLU A 423  ASN A 428 -1  N  GLU A 423   O  ARG A 435           
SHEET    1   C 2 LEU C 152  ILE C 155  0                                        
SHEET    2   C 2 THR C 162  LEU C 166 -1  O  TYR C 164   N  VAL C 154           
SHEET    1   D 3 VAL C 206  ARG C 207  0                                        
SHEET    2   D 3 ALA C 226  VAL C 230  1  O  VAL C 230   N  VAL C 206           
SHEET    3   D 3 VAL C 236  SER C 241 -1  O  TYR C 240   N  LEU C 227           
SHEET    1   E 3 LYS C 277  CYS C 278  0                                        
SHEET    2   E 3 ARG C 298  VAL C 302  1  O  VAL C 300   N  CYS C 278           
SHEET    3   E 3 VAL C 308  SER C 313 -1  O  GLY C 310   N  VAL C 301           
SITE     1 AC1 17 ARG C  69  MET C  84  THR C  86  ILE C  87                    
SITE     2 AC1 17 THR C  88  ASP C  89  GLN C 122  PRO C 127                    
SITE     3 AC1 17 VAL C 129  ILE C 149  HIS C 150  ARG C 151                    
SITE     4 AC1 17 PRO C 153  PHE C 243  HOH C 501  HOH C 506                    
SITE     5 AC1 17 HOH C 520                                                     
SITE     1 AC2 15 HIS C 150  THR C 199  ILE C 203  ALA C 204                    
SITE     2 AC2 15 VAL C 224  SER C 225  ALA C 226  HIS C 297                    
SITE     3 AC2 15 ARG C 298  ILE C 311  SER C 313  LEU C 314                    
SITE     4 AC2 15 SER C 315  ASP C 316  HOH C 502                               
SITE     1 AC3  4 ARG C  69  LYS C 169  ARG C 170  HIS C 297                    
CRYST1  176.558   40.508   77.598  90.00 105.11  90.00 C 1 2 1       4          
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      0.005664  0.000000  0.001530        0.00000                         
SCALE2      0.000000  0.024686  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013349        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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