GenomeNet

Database: PDB
Entry: 4EAI
LinkDB: 4EAI
Original site: 4EAI 
HEADER    TRANSFERASE                             22-MAR-12   4EAI              
TITLE     CO-CRYSTAL STRUCTURE OF AN AMPK CORE WITH AMP                         
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-2;            
COMPND  14 CHAIN: B;                                                            
COMPND  15 FRAGMENT: UNP RESIDUES 189-272;                                      
COMPND  16 SYNONYM: AMPK SUBUNIT BETA-2;                                        
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: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: PRKAB2;                                                        
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 4EAI    1       COMPND SOURCE                            
REVDAT   2   12-MAR-14 4EAI    1       JRNL                                     
REVDAT   1   06-JUN-12 4EAI    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.    2.29 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) : 2.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.55                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.060                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23163                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1172                            
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 29.5498 -  4.5649    0.94     3020   154  0.1946 0.2498        
REMARK   3     2  4.5649 -  3.6254    0.96     2952   152  0.1609 0.1952        
REMARK   3     3  3.6254 -  3.1677    0.96     2925   148  0.1870 0.2722        
REMARK   3     4  3.1677 -  2.8784    0.94     2813   156  0.1967 0.2597        
REMARK   3     5  2.8784 -  2.6722    0.92     2783   157  0.2047 0.2812        
REMARK   3     6  2.6722 -  2.5148    0.90     2658   146  0.2106 0.2718        
REMARK   3     7  2.5148 -  2.3889    0.85     2567   125  0.2260 0.2763        
REMARK   3     8  2.3889 -  2.2849    0.77     2273   134  0.2485 0.3038        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 43.80                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.29                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.35330                                              
REMARK   3    B22 (A**2) : -2.07530                                             
REMARK   3    B33 (A**2) : -7.27800                                             
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      :  0.004           3694                                  
REMARK   3   ANGLE     :  0.908           5017                                  
REMARK   3   CHIRALITY :  0.055            591                                  
REMARK   3   PLANARITY :  0.004            604                                  
REMARK   3   DIHEDRAL  : 17.181           1341                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 394:425)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8809  39.2871 -13.5484              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0844 T22:  -0.0295                                     
REMARK   3      T33:   0.1458 T12:  -0.1653                                     
REMARK   3      T13:  -0.1837 T23:  -0.1208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7152 L22:   1.1019                                     
REMARK   3      L33:   1.0385 L12:   0.1211                                     
REMARK   3      L13:   0.8511 L23:  -0.0870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0046 S12:  -0.0976 S13:   0.1917                       
REMARK   3      S21:   0.2197 S22:   0.0675 S23:   0.3190                       
REMARK   3      S31:  -0.5542 S32:  -0.2712 S33:   0.1366                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 426:445)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6419  28.7851 -18.6338              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0260 T22:   0.1197                                     
REMARK   3      T33:   0.4210 T12:  -0.0066                                     
REMARK   3      T13:   0.0028 T23:   0.0579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0348 L22:   3.0236                                     
REMARK   3      L33:   1.8196 L12:   0.3104                                     
REMARK   3      L13:  -0.1526 L23:  -1.9025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3440 S12:  -0.0350 S13:   0.4778                       
REMARK   3      S21:   0.0073 S22:  -0.3405 S23:  -0.1823                       
REMARK   3      S31:  -0.0201 S32:   0.4830 S33:   0.0404                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 446:472)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   0.3875  36.4146 -20.9768              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1288 T22:   0.1304                                     
REMARK   3      T33:   0.2397 T12:  -0.0190                                     
REMARK   3      T13:  -0.0545 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9826 L22:   5.4990                                     
REMARK   3      L33:   0.7847 L12:  -2.5241                                     
REMARK   3      L13:   0.4143 L23:  -0.6139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2084 S12:   0.2776 S13:  -0.0620                       
REMARK   3      S21:   0.4091 S22:  -0.0124 S23:   0.1292                       
REMARK   3      S31:  -0.1227 S32:   0.0425 S33:   0.2255                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 473:493)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0457  26.6322 -11.7315              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0987 T22:   0.0983                                     
REMARK   3      T33:   0.1607 T12:   0.0199                                     
REMARK   3      T13:  -0.0426 T23:  -0.0275                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1442 L22:   2.0881                                     
REMARK   3      L33:   0.7819 L12:   2.0985                                     
REMARK   3      L13:   0.3377 L23:   0.1196                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0969 S12:   0.0112 S13:  -0.3217                       
REMARK   3      S21:   0.0903 S22:  -0.0414 S23:  -0.5582                       
REMARK   3      S31:   0.0501 S32:  -0.0243 S33:   0.0578                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 204:210)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5889  44.0105 -27.2138              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3328 T22:   0.3539                                     
REMARK   3      T33:   0.5176 T12:  -0.0772                                     
REMARK   3      T13:  -0.1251 T23:   0.0793                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6463 L22:   3.7223                                     
REMARK   3      L33:   0.5961 L12:   3.6353                                     
REMARK   3      L13:   0.9506 L23:   0.6725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0434 S12:  -0.0952 S13:   0.6105                       
REMARK   3      S21:  -0.4926 S22:  -0.3426 S23:   0.3659                       
REMARK   3      S31:   0.0473 S32:   0.0408 S33:   0.3308                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 211:236)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -13.3313  34.7628 -22.6496              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2691 T22:   0.1350                                     
REMARK   3      T33:   0.3359 T12:   0.0519                                     
REMARK   3      T13:  -0.0729 T23:   0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3307 L22:   2.4631                                     
REMARK   3      L33:   2.5288 L12:   1.2608                                     
REMARK   3      L13:   1.0739 L23:  -1.3238                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2023 S12:  -0.0225 S13:   0.5985                       
REMARK   3      S21:   0.0785 S22:  -0.0582 S23:   0.5171                       
REMARK   3      S31:   0.4394 S32:   0.2028 S33:  -0.1267                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 237:245)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4364  30.5676 -19.0715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0755 T22:   0.1137                                     
REMARK   3      T33:   0.1392 T12:  -0.0392                                     
REMARK   3      T13:   0.0202 T23:   0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2959 L22:   2.2870                                     
REMARK   3      L33:   3.8055 L12:   0.3945                                     
REMARK   3      L13:   1.0024 L23:   0.5558                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1222 S12:   0.0336 S13:  -0.0032                       
REMARK   3      S21:  -0.0193 S22:  -0.0800 S23:  -0.3933                       
REMARK   3      S31:  -0.1551 S32:   0.3898 S33:   0.1550                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 246:251)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.8470  30.4925  -2.3433              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4897 T22:   0.3192                                     
REMARK   3      T33:   0.3307 T12:   0.0104                                     
REMARK   3      T13:  -0.0024 T23:  -0.1492                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1551 L22:   0.0149                                     
REMARK   3      L33:   0.4975 L12:  -0.0478                                     
REMARK   3      L13:   0.2790 L23:  -0.0833                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2534 S12:  -0.0965 S13:   0.2133                       
REMARK   3      S21:  -0.2561 S22:  -0.1803 S23:   0.0945                       
REMARK   3      S31:   0.0537 S32:   0.0199 S33:  -0.0815                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 252:271)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1204  21.0839 -19.4253              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1300 T22:   0.1507                                     
REMARK   3      T33:   0.0796 T12:  -0.0087                                     
REMARK   3      T13:   0.0226 T23:  -0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3653 L22:   0.4518                                     
REMARK   3      L33:   0.2611 L12:   0.0937                                     
REMARK   3      L13:   0.1138 L23:  -0.2751                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1300 S12:   0.0410 S13:   0.0335                       
REMARK   3      S21:  -0.1216 S22:  -0.1427 S23:  -0.0216                       
REMARK   3      S31:  -0.0556 S32:   0.1104 S33:   0.1914                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 26:106)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7825  10.8941  -8.1631              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0916 T22:   0.1021                                     
REMARK   3      T33:   0.0769 T12:   0.0360                                     
REMARK   3      T13:  -0.0169 T23:  -0.0209                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2352 L22:   0.2804                                     
REMARK   3      L33:   0.3507 L12:   0.0676                                     
REMARK   3      L13:   0.1405 L23:  -0.2483                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0406 S12:  -0.0555 S13:  -0.0063                       
REMARK   3      S21:   0.0645 S22:  -0.0502 S23:  -0.0075                       
REMARK   3      S31:  -0.0515 S32:  -0.0614 S33:   0.0488                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 107:126)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.8511  11.9455   5.2964              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3580 T22:   0.3302                                     
REMARK   3      T33:   0.0575 T12:  -0.1126                                     
REMARK   3      T13:  -0.0223 T23:  -0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5643 L22:   1.3998                                     
REMARK   3      L33:   0.3561 L12:  -0.5907                                     
REMARK   3      L13:  -0.3665 L23:   0.6853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4063 S12:  -0.1031 S13:  -0.0123                       
REMARK   3      S21:  -0.3879 S22:  -0.4247 S23:   0.1210                       
REMARK   3      S31:  -0.0908 S32:  -0.5442 S33:   0.0063                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 127:222)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -18.5743  -1.3887 -16.4731              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1876 T22:   0.0751                                     
REMARK   3      T33:   0.0737 T12:   0.0068                                     
REMARK   3      T13:  -0.0250 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1896 L22:   0.4455                                     
REMARK   3      L33:   0.5771 L12:   0.6777                                     
REMARK   3      L13:   0.1474 L23:   0.4542                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0083 S12:  -0.0416 S13:  -0.0504                       
REMARK   3      S21:  -0.0093 S22:   0.0365 S23:  -0.0920                       
REMARK   3      S31:   0.3139 S32:  -0.0974 S33:  -0.0213                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 223:265)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -32.8492   5.3928  -2.7993              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1222 T22:   0.3068                                     
REMARK   3      T33:   0.1336 T12:   0.0595                                     
REMARK   3      T13:  -0.0757 T23:  -0.1601                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4821 L22:   0.6479                                     
REMARK   3      L33:   1.8423 L12:   0.3842                                     
REMARK   3      L13:   0.6517 L23:   0.9234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1876 S12:  -0.4113 S13:   0.0215                       
REMARK   3      S21:  -0.0390 S22:  -0.2632 S23:   0.0330                       
REMARK   3      S31:  -0.0220 S32:  -0.5955 S33:   0.3708                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 266:273)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -36.7860  12.5655 -12.0587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0736 T22:   0.7381                                     
REMARK   3      T33:   0.5313 T12:  -0.0590                                     
REMARK   3      T13:  -0.2319 T23:  -0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7641 L22:   0.6913                                     
REMARK   3      L33:   1.2161 L12:   0.0173                                     
REMARK   3      L13:   0.0554 L23:   0.1404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2956 S12:   0.2696 S13:  -0.0791                       
REMARK   3      S21:   0.5141 S22:   0.4116 S23:  -0.0906                       
REMARK   3      S31:  -0.2051 S32:  -0.0691 S33:  -0.6328                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 274:324)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6575  -5.8549 -17.9458              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1794 T22:   0.1802                                     
REMARK   3      T33:   0.1154 T12:  -0.0707                                     
REMARK   3      T13:  -0.0275 T23:  -0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9858 L22:   1.0253                                     
REMARK   3      L33:   0.3962 L12:   0.5873                                     
REMARK   3      L13:  -0.1575 L23:   0.3382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1352 S12:   0.1023 S13:  -0.0076                       
REMARK   3      S21:  -0.1245 S22:  -0.2102 S23:  -0.0126                       
REMARK   3      S31:   0.1540 S32:  -0.1924 S33:   0.0540                       
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 4EAI 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 DEPOSITION ID IS D_1000071374.                                   
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                             : 6.26                               
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   : 24647                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.285                              
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     (%) : 96.8                               
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) : 2.29                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.230                              
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   (%): 46.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, 16% IPP, 1% 1,4-BUTANEDIOL, PH      
REMARK 280  6.26, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298 K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       48.79700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.66700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.79700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.66700            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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     GLN A   494                                                      
REMARK 465     MET B   188                                                      
REMARK 465     TYR B   189                                                      
REMARK 465     GLY B   190                                                      
REMARK 465     GLN B   191                                                      
REMARK 465     GLU B   192                                                      
REMARK 465     MET B   193                                                      
REMARK 465     TYR B   194                                                      
REMARK 465     ALA B   195                                                      
REMARK 465     PHE B   196                                                      
REMARK 465     ARG B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     GLU B   199                                                      
REMARK 465     GLU B   200                                                      
REMARK 465     ARG B   201                                                      
REMARK 465     PHE B   202                                                      
REMARK 465     LYS B   203                                                      
REMARK 465     LYS B   219                                                      
REMARK 465     ASP B   220                                                      
REMARK 465     THR B   221                                                      
REMARK 465     ASN B   222                                                      
REMARK 465     ILE B   223                                                      
REMARK 465     SER B   224                                                      
REMARK 465     CYS B   225                                                      
REMARK 465     ASP B   226                                                      
REMARK 465     PRO B   227                                                      
REMARK 465     ALA B   228                                                      
REMARK 465     LEU B   229                                                      
REMARK 465     LEU B   230                                                      
REMARK 465     PRO B   231                                                      
REMARK 465     GLU B   232                                                      
REMARK 465     PRO B   233                                                      
REMARK 465     ASN B   234                                                      
REMARK 465     HIS B   235                                                      
REMARK 465     ILE B   272                                                      
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     LEU C   121                                                      
REMARK 465     GLN C   122                                                      
REMARK 465     ASP C   123                                                      
REMARK 465     SER C   124                                                      
REMARK 465     PHE C   125                                                      
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     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    LEU A 492     -136.57    -66.26                                   
REMARK 500    ASN B 239       -0.98     73.77                                   
REMARK 500    LYS B 260     -130.04     52.29                                   
REMARK 500    GLU C 109      -72.14    -53.86                                   
REMARK 500    ASP C 231     -159.51   -112.57                                   
REMARK 500    LEU C 265       40.43    -90.07                                   
REMARK 500    HIS C 267       25.74    -77.75                                   
REMARK 500    ARG C 268       99.56    -54.40                                   
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 AMP C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP C 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EAG   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  4EAI A  394   468  UNP    P54645   AAPK1_RAT      405    479             
DBREF  4EAI A  475   494  UNP    P54645   AAPK1_RAT      540    559             
DBREF  4EAI B  189   272  UNP    O43741   AAKB2_HUMAN    189    272             
DBREF  4EAI C    1   330  UNP    P80385   AAKG1_RAT        1    330             
SEQADV 4EAI GLY A  389  UNP  P54645              EXPRESSION TAG                 
SEQADV 4EAI PRO A  390  UNP  P54645              EXPRESSION TAG                 
SEQADV 4EAI HIS A  391  UNP  P54645              EXPRESSION TAG                 
SEQADV 4EAI MET A  392  UNP  P54645              EXPRESSION TAG                 
SEQADV 4EAI GLY A  393  UNP  P54645              EXPRESSION TAG                 
SEQADV 4EAI GLY A  469  UNP  P54645              LINKER                         
SEQADV 4EAI GLY A  470  UNP  P54645              LINKER                         
SEQADV 4EAI GLY A  471  UNP  P54645              LINKER                         
SEQADV 4EAI GLY A  472  UNP  P54645              LINKER                         
SEQADV 4EAI GLY A  473  UNP  P54645              LINKER                         
SEQADV 4EAI GLY A  474  UNP  P54645              LINKER                         
SEQADV 4EAI MET B  188  UNP  O43741              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   85  MET TYR GLY GLN GLU MET TYR ALA PHE ARG SER GLU GLU          
SEQRES   2 B   85  ARG PHE LYS SER PRO PRO ILE LEU PRO PRO HIS LEU LEU          
SEQRES   3 B   85  GLN VAL ILE LEU ASN LYS ASP THR ASN 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 SER 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    AMP  C 401      23                                                       
HET    AMP  C 402      23                                                       
HET    AMP  C 403      23                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   4  AMP    3(C10 H14 N5 O7 P)                                           
FORMUL   7  HOH   *102(H2 O)                                                    
HELIX    1   1 ARG A  405  ASP A  421  1                                  17    
HELIX    2   2 SER A  476  LEU A  492  1                                  17    
HELIX    3   3 VAL C   27  SER C   34  1                                   8    
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 ILE C   87  VAL C  103  1                                  17    
HELIX    7   7 LYS C  112  TYR C  120  1                                   9    
HELIX    8   8 SER C  136  LYS C  148  1                                  13    
HELIX    9   9 THR C  167  ILE C  179  1                                  13    
HELIX   10  10 PRO C  185  LYS C  190  5                                   6    
HELIX   11  11 SER C  191  GLN C  196  1                                   6    
HELIX   12  12 PRO C  211  ARG C  223  1                                  13    
HELIX   13  13 PHE C  243  ALA C  250  5                                   8    
HELIX   14  14 SER C  260  LEU C  265  1                                   6    
HELIX   15  15 THR C  283  GLU C  295  1                                  13    
HELIX   16  16 LEU C  314  LEU C  323  1                                  10    
SHEET    1   A 8 VAL B 215  LEU B 217  0                                        
SHEET    2   A 8 LYS A 395  LEU A 398 -1  N  TRP A 396   O  ILE B 216           
SHEET    3   A 8 TYR B 242  LEU B 244 -1  O  ALA B 243   N  HIS A 397           
SHEET    4   A 8 MET B 251  TYR B 259 -1  O  SER B 254   N  TYR B 242           
SHEET    5   A 8 LYS B 262  LYS B 270 -1  O  LYS B 270   N  MET B 251           
SHEET    6   A 8 SER C  44  ASP C  51  1  O  VAL C  49   N  LEU B 267           
SHEET    7   A 8 ALA C  70  TRP C  74  1  O  TRP C  74   N  PHE C  50           
SHEET    8   A 8 PHE C  81  THR C  86 -1  O  GLY C  83   N  LEU C  73           
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  GLN A 450   O  ASP A 462           
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  LYS A 425   O  ARG A 433           
SHEET    1   C 2 LEU C 152  ILE C 155  0                                        
SHEET    2   C 2 THR C 162  LEU C 166 -1  O  LEU C 163   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  ASP C 238   N  VAL C 229           
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 302   N  CYS C 278           
SHEET    3   E 3 VAL C 308  SER C 313 -1  O  VAL C 312   N  LEU C 299           
CISPEP   1 PHE C  182    PRO C  183          0         6.19                     
SITE     1 AC1 15 ARG C  69  LYS C 169  ILE C 239  SER C 241                    
SITE     2 AC1 15 PHE C 243  ASP C 244  ARG C 268  PHE C 272                    
SITE     3 AC1 15 GLY C 274  VAL C 275  LEU C 276  VAL C 296                    
SITE     4 AC1 15 HIS C 297  ARG C 298  HOH C 558                               
SITE     1 AC2 15 MET C  84  THR C  86  THR C  88  ASP C  89                    
SITE     2 AC2 15 LYS C 126  PRO C 127  LEU C 128  VAL C 129                    
SITE     3 AC2 15 ILE C 149  HIS C 150  ARG C 151  PRO C 153                    
SITE     4 AC2 15 HOH C 508  HOH C 528  HOH C 536                               
SITE     1 AC3 13 HIS C 150  THR C 199  ILE C 203  ALA C 204                    
SITE     2 AC3 13 VAL C 224  SER C 225  ALA C 226  HIS C 297                    
SITE     3 AC3 13 SER C 313  SER C 315  ASP C 316  HOH C 516                    
SITE     4 AC3 13 HOH C 518                                                     
CRYST1   97.594  115.334   48.522  90.00  90.00  90.00 P 21 21 2     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      0.010247  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008670  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020609        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system