GenomeNet

Database: PDB
Entry: 4II5
LinkDB: 4II5
Original site: 4II5 
HEADER    TRANSFERASE/CELL CYCLE                  19-DEC-12   4II5              
TITLE     STRUCTURE OF PCDK2/CYCLINA BOUND TO ADP AND 1 MAGNESIUM ION           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;         
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 165-422;                                      
COMPND  11 SYNONYM: CYCLIN-A;                                                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: CCNA, CCNA2, CYCA;                                             
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ADP AND MAGNESIUM BINDING, T160 PHOSPHORYLATION, TRANSFERASE-CELL     
KEYWDS   2 CYCLE COMPLEX                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.M.JACOBSEN,Z.-Q.BAO,P.J.O'BRIEN,C.L.BROOKS III,M.A.YOUNG            
REVDAT   1   23-JAN-13 4II5    0                                                
JRNL        AUTH   D.M.JACOBSEN,Z.-Q.BAO,P.J.O'BRIEN,C.L.BROOKS III,M.A.YOUNG   
JRNL        TITL   PRICE TO BE PAID FOR TWO-METAL CATALYSIS: MAGNESIUM IONS     
JRNL        TITL 2 THAT ACCELERATE CHEMISTRY UNAVOIDABLY LIMIT PRODUCT RELEASE  
JRNL        TITL 3 FROM A PROTEIN KINASE                                        
JRNL        REF    J.AM.CHEM.SOC.                V. 134 15357 2012              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   22891849                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.56                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 83087                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.420                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2007                            
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 29.5600 -  5.1732    0.98     6069   144  0.1929 0.1933        
REMARK   3     2  5.1732 -  4.1096    0.99     6045   152  0.1550 0.1557        
REMARK   3     3  4.1096 -  3.5912    0.99     6048   154  0.1708 0.2110        
REMARK   3     4  3.5912 -  3.2633    0.99     6036   148  0.1809 0.2258        
REMARK   3     5  3.2633 -  3.0296    0.99     5995   144  0.1822 0.2277        
REMARK   3     6  3.0296 -  2.8512    0.99     5991   142  0.1913 0.2437        
REMARK   3     7  2.8512 -  2.7085    0.98     5994   154  0.1965 0.2339        
REMARK   3     8  2.7085 -  2.5907    0.97     5902   155  0.2245 0.2491        
REMARK   3     9  2.5907 -  2.4910    0.96     5860   139  0.2333 0.2928        
REMARK   3    10  2.4910 -  2.4051    0.94     5663   146  0.2550 0.3038        
REMARK   3    11  2.4051 -  2.3299    0.92     5544   139  0.2576 0.2540        
REMARK   3    12  2.3299 -  2.2633    0.90     5433   117  0.2879 0.3302        
REMARK   3    13  2.2633 -  2.2038    0.88     5281   144  0.3168 0.3139        
REMARK   3    14  2.2038 -  2.1500    0.86     5219   129  0.3383 0.3501        
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   : 0.72                                          
REMARK   3   K_SOL              : 0.39                                          
REMARK   3   B_SOL              : 52.64                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.640           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.61800                                              
REMARK   3    B22 (A**2) : -7.66020                                             
REMARK   3    B33 (A**2) : -1.95770                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 5.18100                                              
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      :  0.010           9230                                  
REMARK   3   ANGLE     :  1.168          12540                                  
REMARK   3   CHIRALITY :  0.086           1415                                  
REMARK   3   PLANARITY :  0.006           1565                                  
REMARK   3   DIHEDRAL  : 16.036           3440                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 1:17)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  15.3563 -76.8196 -29.7356              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6333 T22:   0.2619                                     
REMARK   3      T33:   0.7137 T12:  -0.0753                                     
REMARK   3      T13:   0.2942 T23:  -0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9530 L22:   0.3850                                     
REMARK   3      L33:   1.5839 L12:   0.4144                                     
REMARK   3      L13:   0.8780 L23:   0.7551                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6166 S12:   0.0552 S13:  -0.2907                       
REMARK   3      S21:   0.7757 S22:   0.0122 S23:   0.0108                       
REMARK   3      S31:  -0.2409 S32:   0.1220 S33:  -0.2257                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 18:45)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4645 -76.9965 -26.3784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3128 T22:   0.1755                                     
REMARK   3      T33:   0.3486 T12:  -0.0461                                     
REMARK   3      T13:   0.0584 T23:   0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0405 L22:   0.4381                                     
REMARK   3      L33:   0.4349 L12:  -0.2254                                     
REMARK   3      L13:   0.0332 L23:  -0.2525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2429 S12:  -0.0533 S13:  -0.0211                       
REMARK   3      S21:  -0.1157 S22:  -0.1597 S23:  -0.6677                       
REMARK   3      S31:   0.2014 S32:  -0.0091 S33:  -0.1078                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 46:158)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5207 -67.8802 -36.0153              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3229 T22:   0.1510                                     
REMARK   3      T33:   0.1881 T12:  -0.0195                                     
REMARK   3      T13:   0.0786 T23:   0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4132 L22:   0.7453                                     
REMARK   3      L33:   0.8131 L12:   0.0774                                     
REMARK   3      L13:   0.3425 L23:   0.0153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0667 S12:  -0.0285 S13:  -0.0657                       
REMARK   3      S21:  -0.0519 S22:   0.0134 S23:  -0.1634                       
REMARK   3      S31:   0.3018 S32:  -0.1206 S33:   0.0534                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 159:296)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1711 -48.9364 -41.6772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2213 T22:   0.1256                                     
REMARK   3      T33:   0.1773 T12:   0.0003                                     
REMARK   3      T13:   0.0515 T23:   0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5645 L22:   1.6062                                     
REMARK   3      L33:   0.3346 L12:   0.5945                                     
REMARK   3      L13:  -0.1421 L23:  -0.2124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0134 S12:   0.0327 S13:   0.1957                       
REMARK   3      S21:  -0.0377 S22:  -0.0025 S23:  -0.0472                       
REMARK   3      S31:   0.0698 S32:  -0.0749 S33:  -0.0216                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 175:192)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -19.4335 -66.4169 -28.3889              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3866 T22:   0.3015                                     
REMARK   3      T33:   0.1698 T12:  -0.0801                                     
REMARK   3      T13:   0.0658 T23:   0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6300 L22:   0.5604                                     
REMARK   3      L33:   0.1836 L12:  -0.2385                                     
REMARK   3      L13:  -0.0869 L23:   0.1249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0818 S12:   0.4444 S13:  -0.0198                       
REMARK   3      S21:  -0.1197 S22:  -0.1809 S23:  -0.1634                       
REMARK   3      S31:  -0.0810 S32:  -0.4339 S33:   0.0461                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 193:268)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1148 -70.7831  -5.5110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4430 T22:   0.1457                                     
REMARK   3      T33:   0.1490 T12:  -0.0188                                     
REMARK   3      T13:   0.0923 T23:   0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1128 L22:   0.1553                                     
REMARK   3      L33:   0.3527 L12:   0.0971                                     
REMARK   3      L13:   0.2863 L23:  -0.1089                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0593 S12:  -0.0047 S13:  -0.0007                       
REMARK   3      S21:   0.3488 S22:   0.0935 S23:   0.1531                       
REMARK   3      S31:  -0.0371 S32:  -0.1330 S33:   0.0203                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 269:310)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5307 -68.9280  -8.0772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4651 T22:   0.1590                                     
REMARK   3      T33:   0.2014 T12:  -0.0368                                     
REMARK   3      T13:   0.0183 T23:  -0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1983 L22:   0.4015                                     
REMARK   3      L33:   0.2003 L12:  -0.0523                                     
REMARK   3      L13:   0.1988 L23:  -0.0019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0795 S12:   0.0498 S13:  -0.1185                       
REMARK   3      S21:   0.2101 S22:   0.0861 S23:  -0.1010                       
REMARK   3      S31:   0.0269 S32:   0.0702 S33:  -0.0490                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 311:399)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -28.1208 -60.7024 -13.7560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4108 T22:   0.3373                                     
REMARK   3      T33:   0.2107 T12:   0.0193                                     
REMARK   3      T13:   0.1280 T23:   0.0539                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4588 L22:   0.1431                                     
REMARK   3      L33:   0.6379 L12:   0.2029                                     
REMARK   3      L13:   0.1248 L23:   0.3340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1293 S12:  -0.0823 S13:  -0.0519                       
REMARK   3      S21:   0.1192 S22:   0.1693 S23:   0.1195                       
REMARK   3      S31:  -0.1465 S32:  -0.4615 S33:  -0.2744                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 400:430)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -23.7693 -54.5117  -0.7846              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6167 T22:   0.3061                                     
REMARK   3      T33:  -0.2133 T12:   0.2163                                     
REMARK   3      T13:   0.4594 T23:  -0.0328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0549 L22:   0.0563                                     
REMARK   3      L33:   0.4529 L12:  -0.0804                                     
REMARK   3      L13:   0.0580 L23:   0.2224                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9713 S12:  -0.2436 S13:   1.0225                       
REMARK   3      S21:   0.6322 S22:   0.2863 S23:  -0.4138                       
REMARK   3      S31:  -0.6140 S32:  -0.3480 S33:  -0.0925                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 1:17)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6583 -14.2940   1.8859              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0575 T22:   0.1330                                     
REMARK   3      T33:   0.4963 T12:  -0.0281                                     
REMARK   3      T13:  -0.2607 T23:   0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2605 L22:   0.0283                                     
REMARK   3      L33:   0.0399 L12:   0.1011                                     
REMARK   3      L13:  -0.0360 L23:  -0.0003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0801 S12:   0.0829 S13:   0.0807                       
REMARK   3      S21:   0.2284 S22:  -0.1961 S23:   0.4411                       
REMARK   3      S31:   0.6500 S32:  -0.2113 S33:   0.0447                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 18:45)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2845 -14.0622   6.8317              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5597 T22:   0.1959                                     
REMARK   3      T33:   0.3610 T12:  -0.0351                                     
REMARK   3      T13:  -0.0602 T23:   0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2260 L22:   0.1148                                     
REMARK   3      L33:   0.2482 L12:  -0.2888                                     
REMARK   3      L13:  -0.0304 L23:  -0.0297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1012 S12:  -0.0720 S13:   0.1379                       
REMARK   3      S21:  -0.6298 S22:  -0.0104 S23:   0.4186                       
REMARK   3      S31:   0.1430 S32:  -0.0265 S33:  -0.1032                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 46:158)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2983 -22.9848   4.9545              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4430 T22:   0.1705                                     
REMARK   3      T33:   0.1626 T12:   0.0058                                     
REMARK   3      T13:   0.0140 T23:  -0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3084 L22:   0.7069                                     
REMARK   3      L33:   0.5366 L12:   0.1714                                     
REMARK   3      L13:  -0.0308 L23:   0.0426                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0591 S12:   0.0522 S13:   0.0405                       
REMARK   3      S21:  -0.4733 S22:   0.0145 S23:   0.0005                       
REMARK   3      S31:  -0.2644 S32:   0.0362 S33:   0.0034                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 159:296)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9617 -41.8714   1.8563              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5164 T22:   0.1580                                     
REMARK   3      T33:   0.2181 T12:  -0.0038                                     
REMARK   3      T13:   0.0898 T23:  -0.0290                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1304 L22:   1.0069                                     
REMARK   3      L33:   0.4554 L12:   0.1499                                     
REMARK   3      L13:   0.3265 L23:   0.2720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0040 S12:   0.0096 S13:  -0.1731                       
REMARK   3      S21:  -0.3791 S22:   0.0580 S23:   0.0644                       
REMARK   3      S31:   0.0027 S32:   0.0714 S33:   0.1608                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain 'D' and (resseq 175:192)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6515 -23.9643  22.3664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2019 T22:   0.1902                                     
REMARK   3      T33:   0.1790 T12:  -0.0227                                     
REMARK   3      T13:   0.0847 T23:  -0.0529                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3780 L22:   1.3814                                     
REMARK   3      L33:   1.1341 L12:  -0.5164                                     
REMARK   3      L13:  -0.1338 L23:   0.9474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0772 S12:   0.3502 S13:  -0.0169                       
REMARK   3      S21:  -0.4635 S22:  -0.0788 S23:  -0.1849                       
REMARK   3      S31:  -0.2705 S32:   0.0414 S33:   0.0037                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain 'D' and (resseq 193:268)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1129 -19.9089  36.1809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2901 T22:   0.1541                                     
REMARK   3      T33:   0.1762 T12:   0.0033                                     
REMARK   3      T13:   0.0432 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3067 L22:   0.6736                                     
REMARK   3      L33:   0.1968 L12:  -0.0765                                     
REMARK   3      L13:  -0.4577 L23:   0.3236                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0852 S12:  -0.0518 S13:   0.0079                       
REMARK   3      S21:   0.3213 S22:   0.1261 S23:   0.1286                       
REMARK   3      S31:   0.0174 S32:   0.1351 S33:  -0.0103                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain 'D' and (resseq 269:310)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2695 -21.9879  28.1527              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2727 T22:   0.1690                                     
REMARK   3      T33:   0.2802 T12:  -0.0202                                     
REMARK   3      T13:   0.0297 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2347 L22:   0.5643                                     
REMARK   3      L33:   0.1230 L12:  -0.2945                                     
REMARK   3      L13:  -0.1475 L23:   0.2060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1243 S12:   0.1269 S13:   0.0738                       
REMARK   3      S21:   0.0505 S22:   0.0269 S23:   0.0735                       
REMARK   3      S31:   0.0832 S32:  -0.0281 S33:   0.0732                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: chain 'D' and (resseq 311:399)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  20.8746 -29.5277  39.4148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2567 T22:   0.2049                                     
REMARK   3      T33:   0.1958 T12:   0.0838                                     
REMARK   3      T13:   0.0008 T23:  -0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5780 L22:   0.6308                                     
REMARK   3      L33:   0.4874 L12:   0.3377                                     
REMARK   3      L13:  -0.2015 L23:  -0.5515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2215 S12:  -0.2297 S13:  -0.1190                       
REMARK   3      S21:   0.1493 S22:   0.1455 S23:  -0.1079                       
REMARK   3      S31:   0.0591 S32:   0.0222 S33:   0.0492                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: chain 'D' and (resseq 400:431)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6897 -35.7801  47.8875              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5204 T22:   0.2751                                     
REMARK   3      T33:   0.2301 T12:   0.1162                                     
REMARK   3      T13:   0.1024 T23:   0.0636                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5113 L22:   0.4103                                     
REMARK   3      L33:   0.2872 L12:  -0.1934                                     
REMARK   3      L13:  -0.1874 L23:  -0.3741                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2781 S12:  -0.3193 S13:  -0.5098                       
REMARK   3      S21:   0.2196 S22:   0.3160 S23:   0.0957                       
REMARK   3      S31:  -0.0356 S32:  -0.0453 S33:   0.0344                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 1:296 )                 
REMARK   3     SELECTION          : chain C and (resseq 1:296 )                 
REMARK   3     ATOM PAIRS NUMBER  : 2382                                        
REMARK   3     RMSD               : 0.078                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 175:430 )               
REMARK   3     SELECTION          : chain D and (resseq 175:430 )               
REMARK   3     ATOM PAIRS NUMBER  : 2068                                        
REMARK   3     RMSD               : 0.082                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4II5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB076781.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : DIAMOND LAUE                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83087                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.560                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% W/V POLYACRYLIC ACID SODIUM SALT     
REMARK 280  5100, 20MM MGCL2, 100MM HEPES PH 7.5, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 293.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       82.07000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     SER B   431                                                      
REMARK 465     VAL B   432                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     VAL D   432                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG D   202     O    HOH D   690              1.38            
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    HIS A  60      143.05   -170.28                                   
REMARK 500    ASP A 127       36.99   -141.08                                   
REMARK 500    ASP A 145       75.69     48.15                                   
REMARK 500    VAL A 164      130.64     74.72                                   
REMARK 500    SER A 181     -147.15   -145.32                                   
REMARK 500    ASP C 127       40.66   -140.82                                   
REMARK 500    ASP C 145       79.89     44.93                                   
REMARK 500    VAL C 164      133.69     85.57                                   
REMARK 500    SER C 181     -147.40   -149.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 513   O                                                      
REMARK 620 2 HOH A 512   O   103.1                                              
REMARK 620 3 ASP A 145   OD2  84.3 172.4                                        
REMARK 620 4 ASN A 132   OD1  91.1  90.5  87.3                                  
REMARK 620 5 ADP A 301   O1A 162.7  92.5  80.4  96.2                            
REMARK 620 6 ADP A 301   O3B  94.8  92.5  88.8 172.5  76.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 500   O                                                      
REMARK 620 2 HOH C 501   O   102.8                                              
REMARK 620 3 ADP C 301   O1A  88.9 165.7                                        
REMARK 620 4 ASN C 132   OD1  95.1  97.9  89.3                                  
REMARK 620 5 ASP C 145   OD2 159.5  96.6  71.1  88.8                            
REMARK 620 6 ADP C 301   O3B  89.0  99.3  72.3 161.1  81.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4I3Z   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF PCDK2/CYCLINA BOUND TO ADP AND 2 MAGNESIUM IONS         
DBREF  4II5 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4II5 B  175   432  UNP    P51943   CCNA2_MOUSE    165    422             
DBREF  4II5 C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4II5 D  175   432  UNP    P51943   CCNA2_MOUSE    165    422             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 B  258  VAL PRO ASP TYR GLN GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 B  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 B  258  LYS ARG GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 B  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 B  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 B  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 B  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 B  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 B  258  VAL TYR ILE THR ASP ASP THR TYR SER LYS LYS GLN VAL          
SEQRES  10 B  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU ALA PHE          
SEQRES  11 B  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 B  258  TYR PHE LEU HIS LEU GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 B  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 B  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER LEU ILE ALA          
SEQRES  15 B  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 B  258  GLN SER TRP PRO GLU SER LEU ALA GLN GLN THR GLY TYR          
SEQRES  17 B  258  THR LEU GLU SER LEU LYS PRO CYS LEU VAL ASP LEU HIS          
SEQRES  18 B  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 B  258  ILE ARG GLU LYS TYR LYS HIS SER LYS TYR HIS SER VAL          
SEQRES  20 B  258  SER LEU LEU ASN PRO PRO GLU THR LEU SER VAL                  
SEQRES   1 C  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 C  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 C  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 C  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 C  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 C  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 C  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 C  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 C  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 C  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 C  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 C  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 C  298  ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 C  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 C  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 C  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 C  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 C  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 C  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 C  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 C  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 C  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 C  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 D  258  VAL PRO ASP TYR GLN GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 D  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 D  258  LYS ARG GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 D  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 D  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 D  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 D  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 D  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 D  258  VAL TYR ILE THR ASP ASP THR TYR SER LYS LYS GLN VAL          
SEQRES  10 D  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU ALA PHE          
SEQRES  11 D  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 D  258  TYR PHE LEU HIS LEU GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 D  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 D  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER LEU ILE ALA          
SEQRES  15 D  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 D  258  GLN SER TRP PRO GLU SER LEU ALA GLN GLN THR GLY TYR          
SEQRES  17 D  258  THR LEU GLU SER LEU LYS PRO CYS LEU VAL ASP LEU HIS          
SEQRES  18 D  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 D  258  ILE ARG GLU LYS TYR LYS HIS SER LYS TYR HIS SER VAL          
SEQRES  20 D  258  SER LEU LEU ASN PRO PRO GLU THR LEU SER VAL                  
MODRES 4II5 TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4II5 TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    ADP  A 301      27                                                       
HET     MG  A 302       1                                                       
HET    GOL  A 303       6                                                       
HET    GOL  B 501       6                                                       
HET    GOL  B 502       6                                                       
HET    ADP  C 301      27                                                       
HET     MG  C 302       1                                                       
HET    GOL  C 303       6                                                       
HET    GOL  C 304       6                                                       
HET    GOL  D 501       6                                                       
HET    GOL  D 502       6                                                       
HET    GOL  D 503       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL   7  GOL    8(C3 H8 O3)                                                  
FORMUL  17  HOH   *517(H2 O)                                                    
HELIX    1   1 PRO A   45  LEU A   58  1                                  14    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 THR A  165  ARG A  169  5                                   5    
HELIX    6   6 ALA A  170  LEU A  175  1                                   6    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  252  1                                   6    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  ALA A  282  1                                   7    
HELIX   13  13 HIS A  283  GLN A  287  5                                   5    
HELIX   14  14 TYR B  178  CYS B  193  1                                  16    
HELIX   15  15 THR B  207  TYR B  225  1                                  19    
HELIX   16  16 GLN B  228  MET B  246  1                                  19    
HELIX   17  17 LYS B  252  GLU B  269  1                                  18    
HELIX   18  18 GLU B  274  THR B  282  1                                   9    
HELIX   19  19 SER B  287  ALA B  303  1                                  17    
HELIX   20  20 THR B  310  LEU B  320  1                                  11    
HELIX   21  21 ASN B  326  LEU B  341  1                                  16    
HELIX   22  22 ASP B  343  LEU B  348  1                                   6    
HELIX   23  23 LEU B  351  GLY B  369  1                                  19    
HELIX   24  24 PRO B  373  GLY B  381  1                                   9    
HELIX   25  25 THR B  383  LYS B  400  1                                  18    
HELIX   26  26 GLN B  407  TYR B  413  1                                   7    
HELIX   27  27 LYS B  414  HIS B  419  5                                   6    
HELIX   28  28 SER B  420  LEU B  424  5                                   5    
HELIX   29  29 PRO C   45  LEU C   58  1                                  14    
HELIX   30  30 LEU C   87  SER C   94  1                                   8    
HELIX   31  31 PRO C  100  HIS C  121  1                                  22    
HELIX   32  32 LYS C  129  GLN C  131  5                                   3    
HELIX   33  33 THR C  165  ARG C  169  5                                   5    
HELIX   34  34 ALA C  170  LEU C  175  1                                   6    
HELIX   35  35 THR C  182  ARG C  199  1                                  18    
HELIX   36  36 SER C  207  GLY C  220  1                                  14    
HELIX   37  37 GLY C  229  MET C  233  5                                   5    
HELIX   38  38 ASP C  247  VAL C  252  1                                   6    
HELIX   39  39 ASP C  256  LEU C  267  1                                  12    
HELIX   40  40 SER C  276  ALA C  282  1                                   7    
HELIX   41  41 HIS C  283  GLN C  287  5                                   5    
HELIX   42  42 TYR D  178  CYS D  193  1                                  16    
HELIX   43  43 GLY D  198  GLN D  203  5                                   6    
HELIX   44  44 THR D  207  TYR D  225  1                                  19    
HELIX   45  45 GLN D  228  MET D  246  1                                  19    
HELIX   46  46 LEU D  249  GLY D  251  5                                   3    
HELIX   47  47 LYS D  252  GLU D  269  1                                  18    
HELIX   48  48 GLU D  274  THR D  282  1                                   9    
HELIX   49  49 SER D  287  ALA D  303  1                                  17    
HELIX   50  50 THR D  310  LEU D  320  1                                  11    
HELIX   51  51 ASN D  326  LEU D  341  1                                  16    
HELIX   52  52 ASP D  343  LEU D  348  1                                   6    
HELIX   53  53 LEU D  351  GLY D  369  1                                  19    
HELIX   54  54 PRO D  373  GLY D  381  1                                   9    
HELIX   55  55 THR D  383  LYS D  400  1                                  18    
HELIX   56  56 GLN D  407  TYR D  413  1                                   7    
HELIX   57  57 LYS D  414  HIS D  419  5                                   6    
HELIX   58  58 SER D  420  LEU D  424  5                                   5    
SHEET    1   A 5 PHE A   4  GLU A  12  0                                        
SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  ARG A  22   N  GLN A   5           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  LEU A  32   N  TYR A  19           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1   C 2 VAL A 123  LEU A 124  0                                        
SHEET    2   C 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1   D 5 PHE C   4  GLU C  12  0                                        
SHEET    2   D 5 VAL C  17  ASN C  23 -1  O  LYS C  20   N  VAL C   7           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  LEU C  32   N  TYR C  19           
SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  LEU C  78   N  LYS C  33           
SHEET    5   D 5 LEU C  66  HIS C  71 -1  N  ASP C  68   O  VAL C  79           
SHEET    1   E 3 GLN C  85  ASP C  86  0                                        
SHEET    2   E 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3   E 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1   F 2 VAL C 123  LEU C 124  0                                        
SHEET    2   F 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.33  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
LINK        MG    MG A 302                 O   HOH A 513     1555   1555  2.06  
LINK        MG    MG C 302                 O   HOH C 500     1555   1555  2.08  
LINK        MG    MG C 302                 O   HOH C 501     1555   1555  2.10  
LINK        MG    MG A 302                 O   HOH A 512     1555   1555  2.10  
LINK         OD2 ASP A 145                MG    MG A 302     1555   1555  2.11  
LINK         OD1 ASN A 132                MG    MG A 302     1555   1555  2.12  
LINK         O1A ADP C 301                MG    MG C 302     1555   1555  2.13  
LINK         O1A ADP A 301                MG    MG A 302     1555   1555  2.17  
LINK         OD1 ASN C 132                MG    MG C 302     1555   1555  2.17  
LINK         OD2 ASP C 145                MG    MG C 302     1555   1555  2.24  
LINK         O3B ADP C 301                MG    MG C 302     1555   1555  2.26  
LINK         O3B ADP A 301                MG    MG A 302     1555   1555  2.28  
CISPEP   1 VAL A  154    PRO A  155          0        -1.43                     
CISPEP   2 GLN B  323    PRO B  324          0        -4.99                     
CISPEP   3 ASP B  345    PRO B  346          0        -3.96                     
CISPEP   4 VAL C  154    PRO C  155          0        -1.53                     
CISPEP   5 GLN D  323    PRO D  324          0        -4.98                     
CISPEP   6 ASP D  345    PRO D  346          0        -4.71                     
SITE     1 AC1 20 ILE A  10  VAL A  18  ALA A  31  LYS A  33                    
SITE     2 AC1 20 GLU A  81  LEU A  83  ASP A  86  LYS A  89                    
SITE     3 AC1 20 GLN A 131  ASN A 132  LEU A 134  ASP A 145                    
SITE     4 AC1 20  MG A 302  HOH A 401  HOH A 416  HOH A 439                    
SITE     5 AC1 20 HOH A 443  HOH A 509  HOH A 512  HOH A 543                    
SITE     1 AC2  5 ASN A 132  ASP A 145  ADP A 301  HOH A 512                    
SITE     2 AC2  5 HOH A 513                                                     
SITE     1 AC3  6 PHE A   4  ASN A  23  GLU A  28  LEU A  67                    
SITE     2 AC3  6 HOH A 402  HOH A 475                                          
SITE     1 AC4  4 SER B 209  ASP B 343  HIS B 404  GLN B 406                    
SITE     1 AC5  4 ILE B 213  LEU B 214  GLN B 254  HOH B 679                    
SITE     1 AC6 19 ILE C  10  GLU C  12  ALA C  31  LYS C  33                    
SITE     2 AC6 19 GLU C  81  LEU C  83  ASP C  86  LYS C  89                    
SITE     3 AC6 19 GLN C 131  ASN C 132  LEU C 134  ASP C 145                    
SITE     4 AC6 19  MG C 302  HOH C 401  HOH C 443  HOH C 446                    
SITE     5 AC6 19 HOH C 500  HOH C 515  HOH C 533                               
SITE     1 AC7  5 ASN C 132  ASP C 145  ADP C 301  HOH C 500                    
SITE     2 AC7  5 HOH C 501                                                     
SITE     1 AC8  5 PHE C   4  ASN C  23  GLU C  28  ASP C  68                    
SITE     2 AC8  5 HOH C 486                                                     
SITE     1 AC9  6 GLU B 224  ILE C 209  ASP C 210  PHE C 213                    
SITE     2 AC9  6 ARG C 217  HOH C 498                                          
SITE     1 BC1  5 SER D 209  ASP D 343  HIS D 404  GLN D 406                    
SITE     2 BC1  5 HOH D 710                                                     
SITE     1 BC2  2 ILE D 213  HOH D 636                                          
SITE     1 BC3  4 ASP A 210  PHE A 213  ARG A 217  GLU D 224                    
CRYST1   71.140  164.140   73.450  90.00 107.04  90.00 P 1 21 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      0.014057  0.000000  0.004308        0.00000                         
SCALE2      0.000000  0.006092  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014240        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system