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Database: PDB
Entry: 4BCN
LinkDB: 4BCN
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HEADER    TRANSFERASE/CELL CYCLE                  02-OCT-12   4BCN              
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;                                                            
COMPND  10 FRAGMENT: RESIDUES 171-432;                                          
COMPND  11 SYNONYM: CYCLIN-A;                                                   
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CYCLIN-A2;                                                 
COMPND  15 CHAIN: D;                                                            
COMPND  16 FRAGMENT: RESIDUES 171-431;                                          
COMPND  17 SYNONYM: CYCLIN-A;                                                   
COMPND  18 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;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 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   1   06-MAR-13 4BCN    0                                                
JRNL        AUTH   A.J.HOLE,S.BAUMLI,H.SHAO,S.SHI,C.PEPPER,P.M.FISCHER,S.WANG,  
JRNL        AUTH 2 J.A.ENDICOTT,M.E.M.NOBLE                                     
JRNL        TITL   COMPARATIVE STRUCTURAL AND FUNCTIONAL STUDIES OF             
JRNL        TITL 2 4-(THIAZOL- 5-YL)-2-(PHENYLAMINO)PYRIMIDINE-5-CARBONITRILE   
JRNL        TITL 3 CDK9 INHIBITORS SUGGEST THE BASIS FOR ISOTYPE SELECTIVITY.   
JRNL        REF    J.MED.CHEM.                   V.  56   660 2013              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23252711                                                     
JRNL        DOI    10.1021/JM301495V                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.915                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.81                          
REMARK   3   NUMBER OF REFLECTIONS             : 87253                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1856                          
REMARK   3   R VALUE            (WORKING SET) : 0.1838                          
REMARK   3   FREE R VALUE                     : 0.2191                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 4376                            
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 49.9289 -  6.5205    0.98     2926   165  0.1795 0.2107        
REMARK   3     2  6.5205 -  5.1773    0.99     2828   149  0.1974 0.2315        
REMARK   3     3  5.1773 -  4.5233    1.00     2796   163  0.1485 0.1760        
REMARK   3     4  4.5233 -  4.1100    1.00     2774   159  0.1389 0.1481        
REMARK   3     5  4.1100 -  3.8155    1.00     2813   152  0.1502 0.1902        
REMARK   3     6  3.8155 -  3.5906    1.00     2789   153  0.1563 0.1934        
REMARK   3     7  3.5906 -  3.4108    1.00     2779   142  0.1675 0.1856        
REMARK   3     8  3.4108 -  3.2624    1.00     2765   166  0.1849 0.2143        
REMARK   3     9  3.2624 -  3.1368    1.00     2750   134  0.1938 0.2511        
REMARK   3    10  3.1368 -  3.0286    1.00     2788   152  0.2009 0.2192        
REMARK   3    11  3.0286 -  2.9339    1.00     2770   127  0.2057 0.2303        
REMARK   3    12  2.9339 -  2.8500    1.00     2720   157  0.2068 0.2596        
REMARK   3    13  2.8500 -  2.7750    1.00     2761   153  0.2051 0.2632        
REMARK   3    14  2.7750 -  2.7073    1.00     2760   130  0.2026 0.2582        
REMARK   3    15  2.7073 -  2.6458    1.00     2738   148  0.1994 0.2104        
REMARK   3    16  2.6458 -  2.5895    1.00     2788   125  0.1959 0.2649        
REMARK   3    17  2.5895 -  2.5377    1.00     2746   147  0.1875 0.2571        
REMARK   3    18  2.5377 -  2.4898    1.00     2753   138  0.1895 0.2075        
REMARK   3    19  2.4898 -  2.4453    1.00     2723   157  0.1922 0.2355        
REMARK   3    20  2.4453 -  2.4039    1.00     2742   141  0.1910 0.2516        
REMARK   3    21  2.4039 -  2.3651    1.00     2754   128  0.1890 0.2391        
REMARK   3    22  2.3651 -  2.3287    1.00     2721   147  0.2047 0.2388        
REMARK   3    23  2.3287 -  2.2945    1.00     2773   135  0.1990 0.2303        
REMARK   3    24  2.2945 -  2.2621    1.00     2732   134  0.2065 0.2460        
REMARK   3    25  2.2621 -  2.2316    1.00     2728   144  0.2246 0.2918        
REMARK   3    26  2.2316 -  2.2026    1.00     2715   148  0.2186 0.2748        
REMARK   3    27  2.2026 -  2.1751    1.00     2757   156  0.2210 0.2725        
REMARK   3    28  2.1751 -  2.1489    1.00     2717   148  0.2337 0.3060        
REMARK   3    29  2.1489 -  2.1239    1.00     2738   133  0.2486 0.3235        
REMARK   3    30  2.1239 -  2.1000    1.00     2733   145  0.2519 0.2826        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.374                                         
REMARK   3   B_SOL              : 47.471                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.62             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.37            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.05                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.8624                                              
REMARK   3    B22 (A**2) : 1.5466                                               
REMARK   3    B33 (A**2) : 0.3157                                               
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      :  0.004           9221                                  
REMARK   3   ANGLE     :  0.774          12528                                  
REMARK   3   CHIRALITY :  0.055           1408                                  
REMARK   3   PLANARITY :  0.003           1569                                  
REMARK   3   DIHEDRAL  : 13.835           3455                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 1:85)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5497  14.3963  24.2879              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1833 T22:   0.2130                                     
REMARK   3      T33:   0.1719 T12:  -0.0087                                     
REMARK   3      T13:  -0.0003 T23:   0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0651 L22:   1.7601                                     
REMARK   3      L33:   2.2990 L12:  -0.1222                                     
REMARK   3      L13:   0.7164 L23:   0.9061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0670 S12:  -0.2150 S13:  -0.1337                       
REMARK   3      S21:   0.1988 S22:  -0.1778 S23:   0.1911                       
REMARK   3      S31:   0.1892 S32:  -0.4231 S33:   0.0998                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 86:298)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7100  31.3360   4.2277              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0873 T22:   0.1326                                     
REMARK   3      T33:   0.1801 T12:   0.0029                                     
REMARK   3      T13:   0.0248 T23:   0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5450 L22:   0.7168                                     
REMARK   3      L33:   0.8797 L12:  -0.1067                                     
REMARK   3      L13:   0.5749 L23:  -0.3015                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0252 S12:   0.0506 S13:   0.2134                       
REMARK   3      S21:   0.0005 S22:  -0.0136 S23:   0.0423                       
REMARK   3      S31:  -0.0648 S32:  -0.0575 S33:   0.0068                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5052  -0.1863  -2.8189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1646 T22:   0.1398                                     
REMARK   3      T33:   0.1491 T12:   0.0079                                     
REMARK   3      T13:  -0.0195 T23:  -0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4380 L22:   1.7410                                     
REMARK   3      L33:   1.8259 L12:   0.2813                                     
REMARK   3      L13:  -0.3930 L23:  -0.2577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0471 S12:   0.1579 S13:  -0.0862                       
REMARK   3      S21:  -0.1245 S22:   0.0730 S23:  -0.0827                       
REMARK   3      S31:   0.2997 S32:  -0.0033 S33:  -0.0334                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 1:85)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6705  -7.8247  31.6193              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3960 T22:   0.3236                                     
REMARK   3      T33:   0.2250 T12:   0.0466                                     
REMARK   3      T13:  -0.0404 T23:   0.1069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3714 L22:   1.9402                                     
REMARK   3      L33:   0.9745 L12:   0.2715                                     
REMARK   3      L13:   0.7103 L23:   1.1871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2201 S12:  -0.2890 S13:  -0.2217                       
REMARK   3      S21:   0.3397 S22:  -0.1766 S23:  -0.0720                       
REMARK   3      S31:   0.4849 S32:   0.0388 S33:  -0.0224                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 86:298)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  55.1687 -14.1582  34.1373              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3228 T22:   0.7243                                     
REMARK   3      T33:   0.5139 T12:   0.2013                                     
REMARK   3      T13:   0.0643 T23:   0.2908                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3573 L22:   2.5579                                     
REMARK   3      L33:   1.5855 L12:  -0.1770                                     
REMARK   3      L13:   0.4416 L23:  -1.0426                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1394 S12:  -0.0339 S13:  -0.1801                       
REMARK   3      S21:  -0.2143 S22:  -0.4699 S23:  -0.8046                       
REMARK   3      S31:   0.3282 S32:   0.7744 S33:   0.2936                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  44.6071  20.4852  34.3956              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2907 T22:   0.4760                                     
REMARK   3      T33:   0.3195 T12:  -0.1871                                     
REMARK   3      T13:  -0.0648 T23:   0.0993                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2185 L22:   2.4859                                     
REMARK   3      L33:   2.0081 L12:  -0.1894                                     
REMARK   3      L13:  -0.4380 L23:  -0.4556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0863 S12:  -0.2690 S13:   0.3558                       
REMARK   3      S21:   0.0368 S22:  -0.2862 S23:  -0.5521                       
REMARK   3      S31:  -0.2839 S32:   0.7331 S33:   0.1711                       
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 4BCN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-54252.                                       
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                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
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   : 87330                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.07                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.91                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.02                               
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.68                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.05                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.38                               
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       37.02500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.09500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.54000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.09500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.02500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.54000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.1 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.4 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 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     THR A    39                                                      
REMARK 465     GLU A    40                                                      
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     HIS C   295                                                      
REMARK 465     LEU C   296                                                      
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 465     PRO D   176                                                      
REMARK 465     VAL D   432                                                      
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     ALA B 357    CB                                                  
REMARK 470     ALA D 357    CB                                                  
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   O    GLN D   203     O    HOH D  2016              2.14            
REMARK 500   O    HOH A  2136     O    HOH A  2286              2.12            
REMARK 500   O    HOH B  2008     O    HOH B  2111              1.93            
REMARK 500   O    HOH B  2040     O    HOH A  2120              2.16            
REMARK 500   O    HOH D  2032     O    HOH D  2054              1.92            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  37       57.08   -102.28                                   
REMARK 500    LEU A  58       67.26   -112.83                                   
REMARK 500    ASP A 127       46.31   -153.17                                   
REMARK 500    ASP A 145       82.60     59.42                                   
REMARK 500    VAL A 164      127.37     74.21                                   
REMARK 500    SER A 181     -144.60   -147.23                                   
REMARK 500    THR A 290     -159.29   -126.39                                   
REMARK 500    TYR B 178      -18.02     76.51                                   
REMARK 500    TRP B 372      109.74    -28.73                                   
REMARK 500    THR C  14      -44.52    117.96                                   
REMARK 500    THR C  41      -78.33   -134.93                                   
REMARK 500    ASP C 127       38.97   -153.72                                   
REMARK 500    ASP C 145       85.38     52.91                                   
REMARK 500    VAL C 164      129.38     72.05                                   
REMARK 500    SER C 181     -148.51   -153.47                                   
REMARK 500    ASP C 256     -169.63    -79.87                                   
REMARK 500    TYR D 178       -6.62     63.61                                   
REMARK 500    HIS D 321       40.58    -94.92                                   
REMARK 500    GLN D 323       88.20   -152.87                                   
REMARK 500    PRO D 324     -156.15    -84.46                                   
REMARK 500    TRP D 372      105.24    -32.78                                   
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 T9N A1299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T9N C1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1433                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1432                 
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: 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: 4BCP   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  4BCN A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4BCN B  171   432  UNP    P20248   CCNA2_HUMAN    171    432             
DBREF  4BCN C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4BCN D  171   431  UNP    P20248   CCNA2_HUMAN    171    431             
SEQADV 4BCN GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCN SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCN ALA B  357  UNP  P20248    GLY   357 CONFLICT                       
SEQADV 4BCN LEU B  392  UNP  P20248    MET   392 CONFLICT                       
SEQADV 4BCN ARG B  400  UNP  P20248    LYS   400 CONFLICT                       
SEQADV 4BCN LYS B  403  UNP  P20248    GLN   403 CONFLICT                       
SEQADV 4BCN GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCN SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCN VAL D  432  UNP  P20248              EXPRESSION TAG                 
SEQADV 4BCN ALA D  357  UNP  P20248    GLY   357 CONFLICT                       
SEQADV 4BCN LEU D  392  UNP  P20248    MET   392 CONFLICT                       
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 ALA 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  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO LYS 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 ALA 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  LEU 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 VAL                                                      
MODRES 4BCN TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4BCN TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    T9N  A1299      24                                                       
HET    T9N  C1296      24                                                       
HET    SO4  B1433       5                                                       
HET    SO4  D1432       5                                                       
HETNAM     T9N 2-[(3-HYDROXYPHENYL)AMINO]-4-[4-METHYL-2-                        
HETNAM   2 T9N  (METHYLAMINO)-1,3-THIAZOL-5-YL]PYRIMIDINE-5-                    
HETNAM   3 T9N  CARBONITRILE                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   5  T9N    2(C16 H14 N6 O S)                                            
FORMUL   6  SO4    2(O4 S 2-)                                                   
FORMUL   7  TPO    2(C4 H10 N O6 P)                                             
FORMUL   8  HOH   *687(H2 O)                                                    
HELIX    1   1 PRO A   45  LYS A   56  1                                  12    
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  LEU A  281  1                                   6    
HELIX   13  13 ALA A  282  GLN A  287  5                                   6    
HELIX   14  14 TYR B  178  CYS B  193  1                                  16    
HELIX   15  15 GLY B  198  GLN B  203  1                                   6    
HELIX   16  16 THR B  207  TYR B  225  1                                  19    
HELIX   17  17 GLN B  228  MET B  246  1                                  19    
HELIX   18  18 LEU B  249  GLU B  269  1                                  21    
HELIX   19  19 GLU B  274  ILE B  281  1                                   8    
HELIX   20  20 THR B  287  LEU B  302  1                                  16    
HELIX   21  21 THR B  310  PHE B  319  1                                  10    
HELIX   22  22 LEU B  320  GLN B  322  5                                   3    
HELIX   23  23 ASN B  326  ASP B  343  1                                  18    
HELIX   24  24 ASP B  343  LEU B  348  1                                   6    
HELIX   25  25 LEU B  351  GLY B  369  1                                  19    
HELIX   26  26 PRO B  373  GLY B  381  1                                   9    
HELIX   27  27 THR B  383  ALA B  401  1                                  19    
HELIX   28  28 PRO B  402  HIS B  404  5                                   3    
HELIX   29  29 GLN B  407  TYR B  413  1                                   7    
HELIX   30  30 LYS B  414  HIS B  419  5                                   6    
HELIX   31  31 GLY B  420  LEU B  424  5                                   5    
HELIX   32  32 PRO C   45  LEU C   58  1                                  14    
HELIX   33  33 LEU C   87  SER C   94  1                                   8    
HELIX   34  34 PRO C  100  HIS C  121  1                                  22    
HELIX   35  35 LYS C  129  GLN C  131  5                                   3    
HELIX   36  36 THR C  165  ARG C  169  5                                   5    
HELIX   37  37 ALA C  170  LEU C  175  1                                   6    
HELIX   38  38 THR C  182  ARG C  199  1                                  18    
HELIX   39  39 SER C  207  GLY C  220  1                                  14    
HELIX   40  40 GLY C  229  MET C  233  5                                   5    
HELIX   41  41 ASP C  247  VAL C  252  1                                   6    
HELIX   42  42 ASP C  256  LEU C  267  1                                  12    
HELIX   43  43 SER C  276  ALA C  282  1                                   7    
HELIX   44  44 HIS C  283  GLN C  287  5                                   5    
HELIX   45  45 TYR D  178  CYS D  193  1                                  16    
HELIX   46  46 TYR D  199  GLN D  203  5                                   5    
HELIX   47  47 THR D  207  TYR D  225  1                                  19    
HELIX   48  48 GLN D  228  MET D  246  1                                  19    
HELIX   49  49 LEU D  249  GLY D  251  5                                   3    
HELIX   50  50 LYS D  252  GLU D  269  1                                  18    
HELIX   51  51 GLU D  274  THR D  282  1                                   9    
HELIX   52  52 THR D  287  LEU D  302  1                                  16    
HELIX   53  53 THR D  310  LEU D  320  1                                  11    
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  GLY D  369  1                                  19    
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  GLY A  11  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  HIS A  71 -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  GLU C  12  0                                        
SHEET    2  CA 5 GLY C  16  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  HIS C  71 -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        -4.93                     
CISPEP   2 GLN B  323    PRO B  324          0        -6.00                     
CISPEP   3 ASP B  345    PRO B  346          0        12.59                     
CISPEP   4 VAL C  154    PRO C  155          0        -4.19                     
CISPEP   5 GLN D  323    PRO D  324          0        -5.79                     
CISPEP   6 ASP D  345    PRO D  346          0         9.82                     
SITE     1 AC1 16 ILE A  10  VAL A  18  VAL A  64  PHE A  80                    
SITE     2 AC1 16 GLU A  81  PHE A  82  LEU A  83  HIS A  84                    
SITE     3 AC1 16 GLN A  85  ASP A  86  LYS A  89  ASN A 132                    
SITE     4 AC1 16 LEU A 134  ASP A 145  HOH A2133  HOH A2139                    
SITE     1 AC2 12 ILE C  10  VAL C  64  PHE C  80  GLU C  81                    
SITE     2 AC2 12 PHE C  82  LEU C  83  HIS C  84  ASP C  86                    
SITE     3 AC2 12 LYS C  89  ASN C 132  LEU C 134  ASP C 145                    
SITE     1 AC3  8 TYR B 199  LYS B 202  GLN B 203  LEU B 243                    
SITE     2 AC3  8 SER B 245  MET B 246  SER B 247  HOH B2101                    
SITE     1 AC4  8 TYR D 199  LYS D 202  GLN D 203  LEU D 243                    
SITE     2 AC4  8 SER D 244  SER D 245  MET D 246  SER D 247                    
CRYST1   74.050  135.080  148.190  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      0.013504  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007403  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006748        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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