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Database: PDB
Entry: 4BCK
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HEADER    TRANSFERASE/CELL CYCLE                  02-OCT-12   4BCK              
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, STRUCTURE-BASED   
KEYWDS   2 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 4BCK    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.    2.05 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) : 2.052                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.863                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.07                          
REMARK   3   NUMBER OF REFLECTIONS             : 101785                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1954                          
REMARK   3   R VALUE            (WORKING SET) : 0.1932                          
REMARK   3   FREE R VALUE                     : 0.2358                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 5083                            
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 29.8666 -  6.3565    0.92     3289   188  0.1855 0.1827        
REMARK   3     2  6.3565 -  5.0533    0.95     3309   165  0.1714 0.2043        
REMARK   3     3  5.0533 -  4.4168    0.96     3295   170  0.1341 0.1820        
REMARK   3     4  4.4168 -  4.0140    0.96     3253   174  0.1495 0.1928        
REMARK   3     5  4.0140 -  3.7269    0.97     3299   173  0.1676 0.2172        
REMARK   3     6  3.7269 -  3.5075    0.98     3311   170  0.1784 0.2262        
REMARK   3     7  3.5075 -  3.3321    0.98     3314   157  0.1942 0.2447        
REMARK   3     8  3.3321 -  3.1872    0.99     3339   188  0.2149 0.2648        
REMARK   3     9  3.1872 -  3.0647    0.99     3307   188  0.2238 0.2590        
REMARK   3    10  3.0647 -  2.9590    0.99     3341   165  0.2226 0.2666        
REMARK   3    11  2.9590 -  2.8666    0.99     3319   166  0.2154 0.2863        
REMARK   3    12  2.8666 -  2.7847    0.99     3344   179  0.2232 0.2583        
REMARK   3    13  2.7847 -  2.7114    1.00     3313   172  0.2225 0.2766        
REMARK   3    14  2.7114 -  2.6453    0.99     3333   174  0.2195 0.2738        
REMARK   3    15  2.6453 -  2.5852    1.00     3319   163  0.2107 0.2473        
REMARK   3    16  2.5852 -  2.5302    1.00     3357   191  0.2004 0.2385        
REMARK   3    17  2.5302 -  2.4796    1.00     3314   156  0.1949 0.2556        
REMARK   3    18  2.4796 -  2.4329    1.00     3312   182  0.1913 0.2273        
REMARK   3    19  2.4329 -  2.3894    1.00     3343   157  0.1991 0.2417        
REMARK   3    20  2.3894 -  2.3489    1.00     3240   212  0.2061 0.2954        
REMARK   3    21  2.3489 -  2.3111    1.00     3332   188  0.2209 0.2966        
REMARK   3    22  2.3111 -  2.2755    1.00     3280   163  0.2184 0.2876        
REMARK   3    23  2.2755 -  2.2421    1.00     3339   184  0.2259 0.2677        
REMARK   3    24  2.2421 -  2.2105    0.99     3293   167  0.2381 0.2942        
REMARK   3    25  2.2105 -  2.1806    0.97     3229   195  0.2487 0.2960        
REMARK   3    26  2.1806 -  2.1523    0.93     3098   152  0.2709 0.3179        
REMARK   3    27  2.1523 -  2.1254    0.90     2984   151  0.2836 0.3477        
REMARK   3    28  2.1254 -  2.0998    0.86     2879   138  0.2965 0.3430        
REMARK   3    29  2.0998 -  2.0754    0.82     2729   145  0.3148 0.3304        
REMARK   3    30  2.0754 -  2.0521    0.69     2288   110  0.3217 0.3747        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.40                                          
REMARK   3   SHRINKAGE RADIUS   : 1.37                                          
REMARK   3   K_SOL              : 0.340                                         
REMARK   3   B_SOL              : 75.842                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.34             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.02            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.86                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.0070                                              
REMARK   3    B22 (A**2) : 2.7655                                               
REMARK   3    B33 (A**2) : -0.7585                                              
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      :  0.023           9368                                  
REMARK   3   ANGLE     :  1.675          12741                                  
REMARK   3   CHIRALITY :  0.113           1403                                  
REMARK   3   PLANARITY :  0.007           1584                                  
REMARK   3   DIHEDRAL  : 18.070           3543                                  
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):  10.6956  14.4442  25.3001              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2314 T22:   0.2578                                     
REMARK   3      T33:   0.2285 T12:  -0.0099                                     
REMARK   3      T13:   0.0075 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1180 L22:   0.2825                                     
REMARK   3      L33:   0.2899 L12:   0.0436                                     
REMARK   3      L13:   0.0609 L23:   0.1867                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0044 S12:  -0.0558 S13:  -0.1060                       
REMARK   3      S21:  -0.0087 S22:  -0.1002 S23:   0.0571                       
REMARK   3      S31:   0.0497 S32:  -0.1556 S33:   0.0379                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 86:298)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9685  32.5291   4.2950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1116 T22:   0.2065                                     
REMARK   3      T33:   0.2573 T12:   0.0064                                     
REMARK   3      T13:   0.0035 T23:   0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1794 L22:   0.1022                                     
REMARK   3      L33:   0.1104 L12:  -0.0836                                     
REMARK   3      L13:   0.1048 L23:  -0.0239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0485 S12:   0.1438 S13:   0.1477                       
REMARK   3      S21:  -0.0007 S22:  -0.0289 S23:   0.0069                       
REMARK   3      S31:  -0.0010 S32:   0.0236 S33:   0.0031                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5138  -0.3827  -3.0910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2324 T22:   0.2098                                     
REMARK   3      T33:   0.2209 T12:  -0.0073                                     
REMARK   3      T13:  -0.0034 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3619 L22:   0.2228                                     
REMARK   3      L33:   0.3808 L12:   0.1036                                     
REMARK   3      L13:  -0.1518 L23:  -0.0091                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0749 S12:   0.0970 S13:  -0.0299                       
REMARK   3      S21:  -0.0371 S22:   0.0821 S23:  -0.0607                       
REMARK   3      S31:   0.1838 S32:  -0.0483 S33:   0.0022                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 1:85)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  29.6221  -8.3647  32.7060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3856 T22:   0.3992                                     
REMARK   3      T33:   0.2531 T12:   0.0845                                     
REMARK   3      T13:   0.0032 T23:   0.0875                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3105 L22:   0.2207                                     
REMARK   3      L33:   0.0152 L12:   0.0903                                     
REMARK   3      L13:  -0.0376 L23:  -0.0504                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0671 S12:  -0.2477 S13:  -0.0407                       
REMARK   3      S21:   0.1350 S22:  -0.0620 S23:   0.0122                       
REMARK   3      S31:   0.0750 S32:   0.0849 S33:   0.0067                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 86:298)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  57.5115 -15.0446  35.5111              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2085 T22:   0.9729                                     
REMARK   3      T33:   0.3908 T12:   0.5761                                     
REMARK   3      T13:  -0.0425 T23:   0.4572                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0647 L22:   0.2559                                     
REMARK   3      L33:   0.0538 L12:  -0.0291                                     
REMARK   3      L13:  -0.0317 L23:  -0.0297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0009 S12:  -0.3145 S13:  -0.1296                       
REMARK   3      S21:   0.0598 S22:  -0.0874 S23:  -0.4510                       
REMARK   3      S31:   0.1629 S32:   0.5211 S33:   0.0516                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  46.2620  21.0356  36.1863              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3778 T22:   0.7139                                     
REMARK   3      T33:   0.3889 T12:  -0.2732                                     
REMARK   3      T13:   0.0327 T23:  -0.0372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1038 L22:   0.2133                                     
REMARK   3      L33:   0.2356 L12:  -0.0302                                     
REMARK   3      L13:  -0.0592 L23:   0.0243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0264 S12:  -0.3768 S13:   0.2164                       
REMARK   3      S21:  -0.0544 S22:   0.0161 S23:  -0.3189                       
REMARK   3      S31:  -0.1382 S32:   0.6435 S33:  -0.0523                       
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 4BCK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-54253.                                       
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                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
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   : 101828                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.05                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.86                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 3.74                               
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.55                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.94                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.45                               
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): 3                        
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       38.60100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.58450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.18450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.58450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.60100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.18450            
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: 3220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.9 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.9 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     LEU A   298                                                      
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    13                                                      
REMARK 465     THR C    14                                                      
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     ASP D   177                                                      
REMARK 465     ASN D   431                                                      
REMARK 465     LEU D   432                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    TYR B   178     O    HOH B  2040              2.01            
REMARK 500   OE1A GLU B   277     O    HOH B  2124              2.02            
REMARK 500   O    HOH A  2078     O    HOH A  2081              2.17            
REMARK 500   O    HOH B  2011     O    HOH B  2079              2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 177   CB    CYS A 177   SG      0.096                       
REMARK 500    TRP A 187   CB    TRP A 187   CG      0.118                       
REMARK 500    TRP A 243   CB    TRP A 243   CG      0.136                       
REMARK 500    GLU B 180   CB    GLU B 180   CG      0.116                       
REMARK 500    TYR B 318   CD1   TYR B 318   CE1     0.099                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 122   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP A 127   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG A 150   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A 150   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASP A 270   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    LEU C  32   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    PRO C 284   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  14      -82.84    -52.82                                   
REMARK 500    GLU A  73     -129.81     64.25                                   
REMARK 500    ASP A 127       44.62   -148.96                                   
REMARK 500    ASP A 145       83.60     58.44                                   
REMARK 500    VAL A 164      130.96     76.02                                   
REMARK 500    SER A 181     -148.82   -145.34                                   
REMARK 500    THR A 290     -166.20   -126.01                                   
REMARK 500    TRP B 372      108.48    -32.29                                   
REMARK 500    ASN B 431       77.00     58.45                                   
REMARK 500    VAL C   7      -61.22   -104.32                                   
REMARK 500    THR C  41      -88.21   -131.86                                   
REMARK 500    ASP C 127       32.79   -154.36                                   
REMARK 500    ASP C 145       81.47     54.28                                   
REMARK 500    ARG C 157     -169.18   -121.69                                   
REMARK 500    VAL C 164      130.65     73.06                                   
REMARK 500    CYS C 177      140.28    -35.67                                   
REMARK 500    SER C 181     -152.61   -165.11                                   
REMARK 500    ARG C 199        6.84     81.79                                   
REMARK 500    PRO C 228      105.04    -45.86                                   
REMARK 500    ASP C 235       11.76     49.02                                   
REMARK 500    LYS C 291       78.42   -119.43                                   
REMARK 500    GLN D 323     -134.20    -62.79                                   
REMARK 500    PRO D 324       91.00    -43.16                                   
REMARK 500    THR D 368       21.34   -148.35                                   
REMARK 500    TRP D 372      102.80    -29.49                                   
REMARK 500    PRO D 427     -177.34    -62.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG A 122        23.0      L          L   OUTSIDE RANGE           
REMARK 500    TYR D 347        24.9      L          L   OUTSIDE RANGE           
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 T3E A1298                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T3E C1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM 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: 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: 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  4BCK A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4BCK B  171   432  UNP    P20248   CCNA2_HUMAN    171    432             
DBREF  4BCK C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4BCK D  171   432  UNP    P20248   CCNA2_HUMAN    171    432             
SEQADV 4BCK GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCK SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCK GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCK 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 4BCK TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4BCK TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    T3E  A1298     168                                                       
HET    T3E  C1295     168                                                       
HET    SGM  A1299       6                                                       
HETNAM     T3E 3-[[5-CYANO-4-[4-METHYL-2-(METHYLAMINO)-1,3-                     
HETNAM   2 T3E  THIAZOL-5-YL]PYRIMIDIN-2-YL]AMINO]                              
HETNAM   3 T3E  BENZENESULFONAMIDE                                              
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   5  T3E    2(C16 H15 N7 O2 S2)                                          
FORMUL   6  SGM    C3 H8 O2 S                                                   
FORMUL   7  TPO    2(C4 H10 N O6 P)                                             
FORMUL   8  HOH   *629(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 TYR B  199  GLN B  203  5                                   5    
HELIX   16  16 THR B  207  TYR B  225  1                                  19    
HELIX   17  17 GLN B  228  SER B  244  1                                  17    
HELIX   18  18 LYS B  252  GLU B  269  1                                  18    
HELIX   19  19 GLU B  274  THR B  282  1                                   9    
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  SER B  340  1                                  15    
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  LYS B  400  1                                  18    
HELIX   28  28 ALA B  401  HIS B  404  5                                   4    
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  MET C  266  1                                  11    
HELIX   43  43 SER C  276  LEU C  281  1                                   6    
HELIX   44  44 ALA C  282  GLN C  287  5                                   6    
HELIX   45  45 TYR D  178  GLU D  190  1                                  13    
HELIX   46  46 GLY D  198  GLN D  203  5                                   6    
HELIX   47  47 THR D  207  TYR D  225  1                                  19    
HELIX   48  48 GLN D  228  SER D  244  1                                  17    
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  PHE D  319  1                                  10    
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  LYS D  400  1                                  14    
HELIX   59  59 ALA D  401  HIS D  404  5                                   4    
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 GLY A  16  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  ILE A  70 -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 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  1.35  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.35  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
LINK         N   TPO C 160                 C   TYR C 159     1555   1555  1.34  
CISPEP   1 VAL A  154    PRO A  155          0        -7.25                     
CISPEP   2 GLN B  323    PRO B  324          0        -9.07                     
CISPEP   3 ASP B  345    PRO B  346          0        10.57                     
CISPEP   4 VAL C  154    PRO C  155          0        -4.52                     
CISPEP   5 ASP D  345    PRO D  346          0        10.56                     
SITE     1 AC1 11 ILE A  10  VAL A  18  PHE A  80  PHE A  82                    
SITE     2 AC1 11 LEU A  83  HIS A  84  GLN A  85  ASP A  86                    
SITE     3 AC1 11 LYS A  89  LEU A 134  HOH A2133                               
SITE     1 AC2 11 ILE C  10  VAL C  18  PHE C  80  GLU C  81                    
SITE     2 AC2 11 PHE C  82  LEU C  83  HIS C  84  GLN C  85                    
SITE     3 AC2 11 ASP C  86  LYS C  89  LEU C 134                               
SITE     1 AC3  3 CYS A 177  LYS A 178  MET A 233                               
CRYST1   77.202  140.369  155.169  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      0.012953  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007124  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006445        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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