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Database: PDB
Entry: 4BCP
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Original site: 4BCP 
HEADER    TRANSFERASE/CELL CYCLE                  02-OCT-12   4BCP              
TITLE     STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2-AMINO-4-           
TITLE    2 HETEROARYL-PYRIMIDINE INHIBITOR                                      
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: RESIDUES 171-432;                                          
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE-CELL CYCLE COMPLEX, CDK-CYCLIN COMPLEX,                   
KEYWDS   2 CYCLIN-INHIBITOR, STRUCTURE-BASED DRUG DESIGN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.HOLE,S.BAUMLI,S.WANG,J.A.ENDICOTT,M.E.M.NOBLE                     
REVDAT   2   07-AUG-13 4BCP    1       REMARK                                   
REVDAT   1   17-APR-13 4BCP    0                                                
JRNL        AUTH   H.SHAO,S.SHI,S.HUANG,A.HOLE,A.Y.ABBAS,S.BAUMLI,X.LIU,F.LAM,  
JRNL        AUTH 2 D.W.FOLEY,P.M.FISCHER,M.NOBLE,J.A.ENDICOTT,C.PEPPER,S.WANG   
JRNL        TITL   SUBSTITUTED 4-(THIAZOL-5-YL)-2-(PHENYLAMINO)PYRIMIDINES ARE  
JRNL        TITL 2 HIGHLY ACTIVE CDK9 INHIBITORS: SYNTHESIS, X-RAY CRYSTAL      
JRNL        TITL 3 STRUCTURE, SAR AND ANTI-CANCER ACTIVITIES.                   
JRNL        REF    J.MED.CHEM.                   V.  56   640 2013              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23301767                                                     
JRNL        DOI    10.1021/JM301475F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.26 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.684                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.00                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.07                          
REMARK   3   NUMBER OF REFLECTIONS             : 69591                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1828                          
REMARK   3   R VALUE            (WORKING SET) : 0.1810                          
REMARK   3   FREE R VALUE                     : 0.2171                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3512                            
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 29.6860 -  6.5859    0.98     2817   147  0.1722 0.1770        
REMARK   3     2  6.5859 -  5.2368    0.98     2685   158  0.1880 0.2415        
REMARK   3     3  5.2368 -  4.5775    0.99     2701   140  0.1458 0.1573        
REMARK   3     4  4.5775 -  4.1602    0.99     2670   142  0.1378 0.1742        
REMARK   3     5  4.1602 -  3.8627    0.99     2661   152  0.1571 0.1882        
REMARK   3     6  3.8627 -  3.6354    0.99     2666   135  0.1570 0.1944        
REMARK   3     7  3.6354 -  3.4536    1.00     2678   136  0.1621 0.2079        
REMARK   3     8  3.4536 -  3.3035    1.00     2660   165  0.1690 0.1806        
REMARK   3     9  3.3035 -  3.1765    1.00     2642   142  0.1848 0.2416        
REMARK   3    10  3.1765 -  3.0670    1.00     2624   155  0.1965 0.2664        
REMARK   3    11  3.0670 -  2.9712    1.00     2664   136  0.1964 0.2148        
REMARK   3    12  2.9712 -  2.8863    1.00     2665   145  0.2169 0.2704        
REMARK   3    13  2.8863 -  2.8104    1.00     2628   151  0.2165 0.2785        
REMARK   3    14  2.8104 -  2.7419    1.00     2598   150  0.2256 0.2841        
REMARK   3    15  2.7419 -  2.6796    1.00     2657   137  0.2244 0.2406        
REMARK   3    16  2.6796 -  2.6226    1.00     2630   138  0.2111 0.2602        
REMARK   3    17  2.6226 -  2.5702    1.00     2663   128  0.2150 0.2590        
REMARK   3    18  2.5702 -  2.5217    1.00     2648   122  0.2141 0.2971        
REMARK   3    19  2.5217 -  2.4767    1.00     2638   132  0.2187 0.2705        
REMARK   3    20  2.4767 -  2.4347    1.00     2651   136  0.2273 0.2725        
REMARK   3    21  2.4347 -  2.3955    1.00     2604   147  0.2243 0.2769        
REMARK   3    22  2.3955 -  2.3586    1.00     2649   129  0.2139 0.2709        
REMARK   3    23  2.3586 -  2.3239    1.00     2626   140  0.2152 0.2491        
REMARK   3    24  2.3239 -  2.2912    1.00     2658   117  0.2083 0.2462        
REMARK   3    25  2.2912 -  2.2603    0.88     2296   132  0.2309 0.2866        
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              : 0.370                                         
REMARK   3   B_SOL              : 48.057                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.53             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.50            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.1006                                              
REMARK   3    B22 (A**2) : 3.0220                                               
REMARK   3    B33 (A**2) : 1.0786                                               
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
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      :  0.003           9091                                  
REMARK   3   ANGLE     :  0.702          12336                                  
REMARK   3   CHIRALITY :  0.050           1384                                  
REMARK   3   PLANARITY :  0.003           1534                                  
REMARK   3   DIHEDRAL  : 15.712           3404                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 1:85)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5479  13.5108  23.9945              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2489 T22:   0.3468                                     
REMARK   3      T33:   0.2798 T12:  -0.0390                                     
REMARK   3      T13:   0.0303 T23:   0.0563                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0257 L22:   1.7507                                     
REMARK   3      L33:   2.1838 L12:  -0.3952                                     
REMARK   3      L13:   0.8872 L23:   1.1366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0811 S12:  -0.3542 S13:  -0.2281                       
REMARK   3      S21:   0.2203 S22:  -0.1349 S23:   0.2427                       
REMARK   3      S31:   0.2954 S32:  -0.5254 S33:   0.0474                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 86:298)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4035  31.2876   4.2184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1435 T22:   0.2617                                     
REMARK   3      T33:   0.2475 T12:  -0.0079                                     
REMARK   3      T13:   0.0350 T23:   0.0698                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6391 L22:   0.8537                                     
REMARK   3      L33:   0.9359 L12:  -0.3062                                     
REMARK   3      L13:   0.7011 L23:  -0.0145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0074 S12:   0.0899 S13:   0.1827                       
REMARK   3      S21:  -0.0030 S22:   0.0198 S23:   0.0656                       
REMARK   3      S31:  -0.0535 S32:  -0.0952 S33:   0.0052                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9699  -0.3881  -3.4230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1928 T22:   0.2025                                     
REMARK   3      T33:   0.1673 T12:   0.0008                                     
REMARK   3      T13:  -0.0403 T23:  -0.0518                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7058 L22:   1.8685                                     
REMARK   3      L33:   1.8815 L12:   0.6273                                     
REMARK   3      L13:  -0.3757 L23:  -0.4377                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0732 S12:   0.2778 S13:  -0.1093                       
REMARK   3      S21:  -0.1338 S22:   0.1280 S23:  -0.0870                       
REMARK   3      S31:   0.3054 S32:  -0.0222 S33:  -0.0541                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 1:85)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  27.9620  -8.9202  30.8532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4400 T22:   0.3403                                     
REMARK   3      T33:   0.2842 T12:   0.0086                                     
REMARK   3      T13:  -0.0314 T23:   0.0827                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8270 L22:   2.2515                                     
REMARK   3      L33:   1.5126 L12:   0.3336                                     
REMARK   3      L13:   1.0700 L23:   0.4699                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2375 S12:  -0.3405 S13:  -0.1530                       
REMARK   3      S21:   0.0276 S22:  -0.1148 S23:   0.1592                       
REMARK   3      S31:   0.3626 S32:  -0.2229 S33:  -0.0795                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 86:298)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  52.3691 -17.0875  31.9287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3649 T22:   0.4989                                     
REMARK   3      T33:   0.3325 T12:   0.1556                                     
REMARK   3      T13:   0.0666 T23:   0.0878                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6591 L22:   2.3506                                     
REMARK   3      L33:   1.5002 L12:  -0.2455                                     
REMARK   3      L13:   0.4545 L23:  -0.5495                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0735 S12:  -0.0794 S13:  -0.1360                       
REMARK   3      S21:  -0.1091 S22:  -0.1139 S23:  -0.4077                       
REMARK   3      S31:   0.3245 S32:   0.4958 S33:   0.0451                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN D  AND (RESSEQ 176:432)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.0493  18.7415  35.0566              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3149 T22:   0.2888                                     
REMARK   3      T33:   0.4265 T12:  -0.1341                                     
REMARK   3      T13:   0.0581 T23:   0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9462 L22:   2.0779                                     
REMARK   3      L33:   1.5313 L12:  -0.7176                                     
REMARK   3      L13:   0.1156 L23:  -0.1375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0263 S12:  -0.0555 S13:   0.4456                       
REMARK   3      S21:  -0.1714 S22:  -0.0496 S23:  -0.6613                       
REMARK   3      S31:  -0.1155 S32:   0.3764 S33:   0.0682                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 1299)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9848  22.9119  23.2201              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7130 T22:   0.6940                                     
REMARK   3      T33:   0.5245 T12:  -0.1748                                     
REMARK   3      T13:  -0.1258 T23:   0.1957                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6379 L22:   1.0429                                     
REMARK   3      L33:   1.3364 L12:   0.5826                                     
REMARK   3      L13:   1.2098 L23:  -0.4748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2870 S12:  -0.1144 S13:   0.0062                       
REMARK   3      S21:   0.1628 S22:  -0.2941 S23:  -0.1908                       
REMARK   3      S31:  -0.0140 S32:  -0.0060 S33:   0.3796                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN D AND (RESSEQ 1433:1434)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  28.0066   6.3912  19.9396              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9011 T22:   1.3782                                     
REMARK   3      T33:   1.1580 T12:   0.0282                                     
REMARK   3      T13:  -0.1969 T23:   0.1772                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5164 L22:   5.8864                                     
REMARK   3      L33:   6.0486 L12:  -4.4528                                     
REMARK   3      L13:  -2.5183 L23:   3.1123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0838 S12:   0.2819 S13:  -0.1007                       
REMARK   3      S21:   0.2331 S22:   0.0308 S23:   0.0259                       
REMARK   3      S31:  -0.2486 S32:   0.1136 S33:   0.0193                       
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 4BCP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-54255.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69656                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.26                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.83                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.42                               
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.91                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.41                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.58                               
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: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: COCRYSTALS WERE GROWN IN                 
REMARK 280  1-1.25M AMMONIUM SULFATE, 0.5-0.9M KCL, 100MM HEPES, PH             
REMARK 280  7.0, 5MM DTT AND IN THE PRESENCE OF COMPOUND.                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       36.90500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.58400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.27650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.58400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.90500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.27650            
REMARK 290   SMTRY3   4  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: 3670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.8 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: 3650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.9 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     GLY A    -1                                                      
REMARK 465     SER B   171                                                      
REMARK 465     VAL B   172                                                      
REMARK 465     ASN B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     VAL B   175                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     GLY C    13                                                      
REMARK 465     THR C    14                                                      
REMARK 465     TYR C    15                                                      
REMARK 465     PRO C   222                                                      
REMARK 465     ASP C   223                                                      
REMARK 465     GLU C   224                                                      
REMARK 465     VAL C   225                                                      
REMARK 465     VAL C   226                                                      
REMARK 465     TRP C   227                                                      
REMARK 465     PRO C   228                                                      
REMARK 465     GLY C   229                                                      
REMARK 465     VAL C   230                                                      
REMARK 465     THR C   231                                                      
REMARK 465     SER C   232                                                      
REMARK 465     MET C   233                                                      
REMARK 465     PRO C   234                                                      
REMARK 465     ASP C   235                                                      
REMARK 465     TYR C   236                                                      
REMARK 465     LYS C   237                                                      
REMARK 465     PRO C   238                                                      
REMARK 465     SER C   239                                                      
REMARK 465     PHE C   240                                                      
REMARK 465     PRO C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     TRP C   243                                                      
REMARK 465     ALA C   244                                                      
REMARK 465     ARG C   245                                                      
REMARK 465     GLN C   246                                                      
REMARK 465     ASP C   247                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     SER D   171                                                      
REMARK 465     VAL D   172                                                      
REMARK 465     ASN D   173                                                      
REMARK 465     GLU D   174                                                      
REMARK 465     VAL D   175                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A   0    OG                                                  
REMARK 470     SER C   0    OG                                                  
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   OH   TYR A    15     OE1  GLU A    51              2.18            
REMARK 500   O    HOH C  2004     O    HOH C  2024              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 127       43.13   -156.19                                   
REMARK 500    ASP A 145       82.45     58.95                                   
REMARK 500    VAL A 164      128.19     72.11                                   
REMARK 500    SER A 181     -151.08   -146.04                                   
REMARK 500    TRP B 372      106.25    -30.36                                   
REMARK 500    THR C  41      -81.90   -131.98                                   
REMARK 500    ASP C 127       45.01   -152.95                                   
REMARK 500    ASP C 145       79.54     55.78                                   
REMARK 500    PHE C 146       33.05    -94.55                                   
REMARK 500    VAL C 164      126.48     70.90                                   
REMARK 500    SER C 181     -146.20   -149.05                                   
REMARK 500    ASP D 284       15.59     55.86                                   
REMARK 500    TRP D 372      107.81    -26.03                                   
REMARK 500    ASN D 431       78.32     55.31                                   
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 SO4 B1433                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B1434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B1435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3C C1297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1433                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM D1434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3C A1299                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4BCF   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2                  
REMARK 900  -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR                            
REMARK 900 RELATED ID: 4BCG   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2                  
REMARK 900  -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR                            
REMARK 900 RELATED ID: 4BCH   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2                  
REMARK 900  -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR                            
REMARK 900 RELATED ID: 4BCI   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2                  
REMARK 900  -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR                            
REMARK 900 RELATED ID: 4BCJ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2                  
REMARK 900  -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR                            
REMARK 900 RELATED ID: 4BCK   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2                  
REMARK 900  -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR                            
REMARK 900 RELATED ID: 4BCM   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2                  
REMARK 900  -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR                            
REMARK 900 RELATED ID: 4BCN   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2                  
REMARK 900  -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR                            
REMARK 900 RELATED ID: 4BCO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2                  
REMARK 900  -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR                            
REMARK 900 RELATED ID: 4BCQ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2                  
REMARK 900  -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR                            
DBREF  4BCP A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4BCP B  171   432  UNP    P20248   CCNA2_HUMAN    171    432             
DBREF  4BCP C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4BCP D  171   432  UNP    P20248   CCNA2_HUMAN    171    432             
SEQADV 4BCP GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCP SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCP GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCP SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQRES   1 A  300  GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 A  300  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 A  300  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 A  300  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 A  300  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 A  300  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 A  300  TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS          
SEQRES   8 A  300  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 A  300  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 A  300  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 A  300  LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 A  300  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 A  300  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 A  300  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 A  300  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 A  300  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 A  300  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 A  300  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 A  300  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 A  300  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 A  300  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 A  300  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 A  300  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG          
SEQRES  24 A  300  LEU                                                          
SEQRES   1 B  262  SER VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 B  262  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 B  262  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 B  262  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 B  262  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 B  262  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 B  262  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 B  262  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 B  262  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 B  262  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 B  262  VAL LEU THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN          
SEQRES  12 B  262  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 B  262  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 B  262  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 B  262  SER VAL ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 B  262  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG          
SEQRES  17 B  262  LYS THR GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU          
SEQRES  18 B  262  MET ASP LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS          
SEQRES  19 B  262  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 B  262  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 B  262  ASN LEU                                                      
SEQRES   1 C  300  GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 C  300  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 C  300  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 C  300  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 C  300  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 C  300  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 C  300  TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS          
SEQRES   8 C  300  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 C  300  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 C  300  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 C  300  LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 C  300  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 C  300  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 C  300  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 C  300  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 C  300  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 C  300  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 C  300  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 C  300  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 C  300  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 C  300  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 C  300  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 C  300  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG          
SEQRES  24 C  300  LEU                                                          
SEQRES   1 D  262  SER VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 D  262  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 D  262  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 D  262  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 D  262  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 D  262  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 D  262  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 D  262  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 D  262  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 D  262  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 D  262  VAL LEU THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN          
SEQRES  12 D  262  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 D  262  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 D  262  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 D  262  SER VAL ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 D  262  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG          
SEQRES  17 D  262  LYS THR GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU          
SEQRES  18 D  262  MET ASP LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS          
SEQRES  19 D  262  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 D  262  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 D  262  ASN LEU                                                      
MODRES 4BCP TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4BCP TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    SO4  B1433       5                                                       
HET    SGM  B1434       6                                                       
HET    SGM  B1435       6                                                       
HET    TPO  C 160      11                                                       
HET    T3C  C1297      60                                                       
HET    SO4  D1433       5                                                       
HET    SGM  D1434       6                                                       
HET    T3C  A1299      60                                                       
HETNAM     T3C 2-[[3-(1,4-DIAZEPAN-1-YL)PHENYL]AMINO]-4-[4-                     
HETNAM   2 T3C  METHYL-2-(METHYLAMINO)-1,3-THIAZOL-5-YL]                        
HETNAM   3 T3C  PYRIMIDINE-5-CARBONITRILE                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   5  T3C    2(C21 H24 N8 S)                                              
FORMUL   6  SO4    2(O4 S 2-)                                                   
FORMUL   7  SGM    3(C3 H8 O2 S)                                                
FORMUL   8  TPO    2(C4 H10 N O6 P)                                             
FORMUL   9  HOH   *363(H2 O)                                                    
HELIX    1   1 SER A    0  GLU A    2  5                                   3    
HELIX    2   2 PRO A   45  LEU A   58  1                                  14    
HELIX    3   3 LEU A   87  SER A   94  1                                   8    
HELIX    4   4 PRO A  100  HIS A  121  1                                  22    
HELIX    5   5 LYS A  129  GLN A  131  5                                   3    
HELIX    6   6 THR A  165  ARG A  169  5                                   5    
HELIX    7   7 ALA A  170  LEU A  175  1                                   6    
HELIX    8   8 THR A  182  ARG A  199  1                                  18    
HELIX    9   9 SER A  207  GLY A  220  1                                  14    
HELIX   10  10 GLY A  229  MET A  233  5                                   5    
HELIX   11  11 ASP A  247  VAL A  252  1                                   6    
HELIX   12  12 ASP A  256  LEU A  267  1                                  12    
HELIX   13  13 SER A  276  LEU A  281  1                                   6    
HELIX   14  14 ALA A  282  GLN A  287  5                                   6    
HELIX   15  15 TYR B  178  CYS B  193  1                                  16    
HELIX   16  16 GLY B  198  GLN B  203  1                                   6    
HELIX   17  17 THR B  207  TYR B  225  1                                  19    
HELIX   18  18 GLN B  228  SER B  244  1                                  17    
HELIX   19  19 LEU B  249  GLY B  251  5                                   3    
HELIX   20  20 LYS B  252  GLU B  269  1                                  18    
HELIX   21  21 GLU B  274  THR B  282  1                                   9    
HELIX   22  22 THR B  287  LEU B  302  1                                  16    
HELIX   23  23 THR B  310  LEU B  320  1                                  11    
HELIX   24  24 ASN B  326  ASP B  343  1                                  18    
HELIX   25  25 ASP B  343  LEU B  348  1                                   6    
HELIX   26  26 LEU B  351  THR B  368  1                                  18    
HELIX   27  27 PRO B  373  GLY B  381  1                                   9    
HELIX   28  28 THR B  383  ALA B  401  1                                  19    
HELIX   29  29 PRO B  402  HIS B  404  5                                   3    
HELIX   30  30 GLN B  407  TYR B  413  1                                   7    
HELIX   31  31 LYS B  414  HIS B  419  5                                   6    
HELIX   32  32 GLY B  420  LEU B  424  5                                   5    
HELIX   33  33 PRO C   45  LEU C   58  1                                  14    
HELIX   34  34 LEU C   87  SER C   94  1                                   8    
HELIX   35  35 PRO C  100  HIS C  121  1                                  22    
HELIX   36  36 LYS C  129  GLN C  131  5                                   3    
HELIX   37  37 THR C  165  ARG C  169  5                                   5    
HELIX   38  38 ALA C  170  LEU C  175  1                                   6    
HELIX   39  39 THR C  182  ARG C  199  1                                  18    
HELIX   40  40 SER C  207  GLY C  220  1                                  14    
HELIX   41  41 ASP C  256  LEU C  267  1                                  12    
HELIX   42  42 SER C  276  LEU C  281  1                                   6    
HELIX   43  43 ALA C  282  GLN C  287  5                                   6    
HELIX   44  44 TYR D  178  CYS D  193  1                                  16    
HELIX   45  45 TYR D  199  GLN D  203  5                                   5    
HELIX   46  46 THR D  207  TYR D  225  1                                  19    
HELIX   47  47 GLN D  228  LEU D  243  1                                  16    
HELIX   48  48 LEU D  249  GLY D  251  5                                   3    
HELIX   49  49 LYS D  252  GLU D  269  1                                  18    
HELIX   50  50 GLU D  274  ILE D  281  1                                   8    
HELIX   51  51 THR D  287  LEU D  302  1                                  16    
HELIX   52  52 THR D  310  PHE D  319  1                                  10    
HELIX   53  53 LEU D  320  GLN D  322  5                                   3    
HELIX   54  54 ASN D  326  ASP D  343  1                                  18    
HELIX   55  55 ASP D  343  LEU D  348  1                                   6    
HELIX   56  56 LEU D  351  THR D  368  1                                  18    
HELIX   57  57 PRO D  373  GLY D  381  1                                   9    
HELIX   58  58 LEU D  387  ALA D  401  1                                  15    
HELIX   59  59 PRO D  402  HIS D  404  5                                   3    
HELIX   60  60 GLN D  407  TYR D  413  1                                   7    
HELIX   61  61 LYS D  414  HIS D  419  5                                   6    
HELIX   62  62 GLY D  420  LEU D  424  5                                   5    
SHEET    1  AA 5 PHE A   4  GLU A  12  0                                        
SHEET    2  AA 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3  AA 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 LEU A  66  THR A  72 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1  AC 2 VAL A 123  LEU A 124  0                                        
SHEET    2  AC 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1  CA 5 PHE C   4  GLY C  11  0                                        
SHEET    2  CA 5 VAL C  17  ASN C  23 -1  O  VAL C  18   N  ILE C  10           
SHEET    3  CA 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4  CA 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5  CA 5 LEU C  66  ILE C  70 -1  N  LEU C  67   O  VAL C  79           
SHEET    1  CB 3 GLN C  85  ASP C  86  0                                        
SHEET    2  CB 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3  CB 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1  CC 2 VAL C 123  LEU C 124  0                                        
SHEET    2  CC 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         N   TPO A 160                 C   TYR A 159     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
LINK         N   TPO C 160                 C   TYR C 159     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0        -5.74                     
CISPEP   2 GLN B  323    PRO B  324          0        -3.56                     
CISPEP   3 ASP B  345    PRO B  346          0         9.61                     
CISPEP   4 VAL C  154    PRO C  155          0        -2.35                     
CISPEP   5 GLN D  323    PRO D  324          0        -0.55                     
CISPEP   6 ASP D  345    PRO D  346          0         8.61                     
SITE     1 AC1  7 TYR B 199  LYS B 202  GLN B 203  LEU B 243                    
SITE     2 AC1  7 SER B 245  MET B 246  SER B 247                               
SITE     1 AC2  7 HOH A2031  MET B 189  LYS B 192  CYS B 193                    
SITE     2 AC2  7 ARG B 241  ASP B 305  HOH B2105                               
SITE     1 AC3  2 CYS B 327  GLU B 330                                          
SITE     1 AC4 12 ILE C  10  VAL C  64  PHE C  80  GLU C  81                    
SITE     2 AC4 12 PHE C  82  LEU C  83  ASP C  86  LYS C  89                    
SITE     3 AC4 12 GLN C 131  ASN C 132  LEU C 134  ASP C 145                    
SITE     1 AC5  6 LYS D 202  GLN D 203  SER D 244  SER D 245                    
SITE     2 AC5  6 MET D 246  SER D 247                                          
SITE     1 AC6  4 LYS D 192  CYS D 193  ARG D 241  ASP D 305                    
SITE     1 AC7 17 ILE A  10  GLY A  13  ALA A  31  VAL A  64                    
SITE     2 AC7 17 PHE A  80  GLU A  81  PHE A  82  LEU A  83                    
SITE     3 AC7 17 HIS A  84  GLN A  85  ASP A  86  LYS A  89                    
SITE     4 AC7 17 GLN A 131  ASN A 132  LEU A 134  ASP A 145                    
SITE     5 AC7 17 HOH A2026                                                     
CRYST1   73.810  134.553  149.168  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013548  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007432  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006704        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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