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Database: PDB
Entry: 4BCO
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HEADER    TRANSFERASE/CELL CYCLE                  02-OCT-12   4BCO              
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 SYNONYM: CYCLIN-A;                                                   
COMPND  11 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: BOS TAURUS;                                     
SOURCE   9 ORGANISM_COMMON: BOVINE;                                             
SOURCE  10 ORGANISM_TAXID: 9913;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE-CELL CYCLE COMPLEX, CDK-CYCLIN COMPLEX,                   
KEYWDS   2 CYCLIN-INHIBITOR, STRUCTURE-BASED DRUG DESIGN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.HOLE,S.BAUMLI,S.WANG,J.A.ENDICOTT,M.E.M.NOBLE                     
REVDAT   2   27-FEB-13 4BCO    1       JRNL                                     
REVDAT   1   09-JAN-13 4BCO    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) : 2.050                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.599                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.00                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.96                          
REMARK   3   NUMBER OF REFLECTIONS             : 91969                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1906                          
REMARK   3   R VALUE            (WORKING SET) : 0.1887                          
REMARK   3   FREE R VALUE                     : 0.2260                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 4595                            
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 49.6138 -  6.3655    0.97     3082   162  0.1856 0.1985        
REMARK   3     2  6.3655 -  5.0541    0.98     3000   144  0.1932 0.2649        
REMARK   3     3  5.0541 -  4.4157    0.99     2974   161  0.1525 0.1905        
REMARK   3     4  4.4157 -  4.0122    0.99     2964   157  0.1568 0.1948        
REMARK   3     5  4.0122 -  3.7247    0.98     2888   170  0.1675 0.1839        
REMARK   3     6  3.7247 -  3.5051    0.97     2877   145  0.1708 0.2097        
REMARK   3     7  3.5051 -  3.3296    0.99     2899   175  0.1749 0.2054        
REMARK   3     8  3.3296 -  3.1847    0.99     2941   139  0.1821 0.1958        
REMARK   3     9  3.1847 -  3.0621    1.00     2926   160  0.1880 0.2274        
REMARK   3    10  3.0621 -  2.9565    0.99     2902   146  0.1893 0.2349        
REMARK   3    11  2.9565 -  2.8641    0.97     2888   159  0.2080 0.2339        
REMARK   3    12  2.8641 -  2.7822    0.99     2890   130  0.2057 0.2539        
REMARK   3    13  2.7822 -  2.7090    0.99     2929   159  0.2031 0.2370        
REMARK   3    14  2.7090 -  2.6429    0.99     2872   154  0.1935 0.2369        
REMARK   3    15  2.6429 -  2.5828    0.99     2959   144  0.1888 0.2108        
REMARK   3    16  2.5828 -  2.5278    1.00     2865   184  0.1960 0.2156        
REMARK   3    17  2.5278 -  2.4773    1.00     2911   143  0.2079 0.2630        
REMARK   3    18  2.4773 -  2.4305    1.00     2911   162  0.2193 0.3042        
REMARK   3    19  2.4305 -  2.3871    0.99     2868   148  0.2210 0.2653        
REMARK   3    20  2.3871 -  2.3467    0.98     2880   136  0.2171 0.2675        
REMARK   3    21  2.3467 -  2.3088    0.99     2876   174  0.2076 0.2714        
REMARK   3    22  2.3088 -  2.2733    1.00     2945   129  0.2091 0.2342        
REMARK   3    23  2.2733 -  2.2398    0.99     2831   169  0.2173 0.2741        
REMARK   3    24  2.2398 -  2.2083    1.00     2965   144  0.2227 0.2972        
REMARK   3    25  2.2083 -  2.1785    1.00     2888   135  0.2151 0.2345        
REMARK   3    26  2.1785 -  2.1502    1.00     2900   145  0.2210 0.3085        
REMARK   3    27  2.1502 -  2.1233    1.00     2903   145  0.2329 0.2629        
REMARK   3    28  2.1233 -  2.0977    1.00     2930   152  0.2428 0.2930        
REMARK   3    29  2.0977 -  2.0733    1.00     2901   149  0.2431 0.2987        
REMARK   3    30  2.0733 -  2.0500    0.98     2809   175  0.2492 0.2848        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.389                                         
REMARK   3   B_SOL              : 44.553                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.64             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.08            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.61                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.7662                                              
REMARK   3    B22 (A**2) : -0.0647                                              
REMARK   3    B33 (A**2) : 0.8309                                               
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      :  0.005           9050                                  
REMARK   3   ANGLE     :  0.902          12282                                  
REMARK   3   CHIRALITY :  0.061           1388                                  
REMARK   3   PLANARITY :  0.004           1534                                  
REMARK   3   DIHEDRAL  : 14.168           3386                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 1:85)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -10.5758  13.3096 -23.8003              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2267 T22:   0.2697                                     
REMARK   3      T33:   0.2648 T12:   0.0307                                     
REMARK   3      T13:   0.0230 T23:  -0.0355                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5874 L22:   2.0853                                     
REMARK   3      L33:   2.7631 L12:   0.1657                                     
REMARK   3      L13:   1.0085 L23:  -1.0155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1154 S12:   0.2671 S13:  -0.2469                       
REMARK   3      S21:  -0.3076 S22:  -0.1502 S23:  -0.3229                       
REMARK   3      S31:   0.3443 S32:   0.5067 S33:   0.0281                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 86:298)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.4534  31.0799  -4.1780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1396 T22:   0.2112                                     
REMARK   3      T33:   0.2154 T12:   0.0026                                     
REMARK   3      T13:   0.0259 T23:  -0.0457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7842 L22:   0.7660                                     
REMARK   3      L33:   1.0665 L12:   0.1904                                     
REMARK   3      L13:   0.9682 L23:   0.0018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0015 S12:  -0.1087 S13:   0.1820                       
REMARK   3      S21:   0.0164 S22:  -0.0031 S23:  -0.0670                       
REMARK   3      S31:  -0.0485 S32:   0.0697 S33:   0.0164                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0153  -0.3932   3.5941              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1770 T22:   0.1943                                     
REMARK   3      T33:   0.1590 T12:  -0.0102                                     
REMARK   3      T13:  -0.0386 T23:   0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5180 L22:   1.7044                                     
REMARK   3      L33:   1.7085 L12:  -0.6213                                     
REMARK   3      L13:  -0.6254 L23:   0.3756                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0695 S12:  -0.2279 S13:  -0.1054                       
REMARK   3      S21:   0.1347 S22:   0.0984 S23:   0.0383                       
REMARK   3      S31:   0.2495 S32:   0.0315 S33:  -0.0375                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 1:85)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -28.3432  -9.3700 -30.6746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3789 T22:   0.2819                                     
REMARK   3      T33:   0.2747 T12:   0.0075                                     
REMARK   3      T13:  -0.0168 T23:  -0.0573                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2945 L22:   2.0480                                     
REMARK   3      L33:   1.6454 L12:  -0.1215                                     
REMARK   3      L13:   0.8956 L23:  -1.5021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2710 S12:   0.2399 S13:  -0.0705                       
REMARK   3      S21:  -0.1289 S22:  -0.1476 S23:  -0.0567                       
REMARK   3      S31:   0.2784 S32:   0.2594 S33:  -0.1204                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 86:298)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -52.3670 -16.9444 -31.7441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2974 T22:   0.3398                                     
REMARK   3      T33:   0.2717 T12:  -0.0992                                     
REMARK   3      T13:   0.0478 T23:  -0.0582                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3538 L22:   2.4140                                     
REMARK   3      L33:   1.6378 L12:  -0.0401                                     
REMARK   3      L13:   0.3049 L23:   0.1004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0861 S12:   0.0267 S13:  -0.1624                       
REMARK   3      S21:   0.1422 S22:  -0.0714 S23:   0.3677                       
REMARK   3      S31:   0.2885 S32:  -0.3942 S33:  -0.0021                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -45.0284  18.7255 -34.8806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2821 T22:   0.2182                                     
REMARK   3      T33:   0.3530 T12:   0.0923                                     
REMARK   3      T13:   0.0515 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9322 L22:   1.9124                                     
REMARK   3      L33:   1.4614 L12:   0.7387                                     
REMARK   3      L13:  -0.1429 L23:  -0.0959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0133 S12:   0.0129 S13:   0.3956                       
REMARK   3      S21:   0.2064 S22:   0.0080 S23:   0.5594                       
REMARK   3      S31:  -0.1538 S32:  -0.2832 S33:  -0.0043                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN A (RESSEQ 1299)                                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1615  23.1920 -24.5163              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3564 T22:   0.2615                                     
REMARK   3      T33:   0.2867 T12:   0.0410                                     
REMARK   3      T13:   0.0180 T23:  -0.0602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0036 L22:   9.2018                                     
REMARK   3      L33:   2.0897 L12:   1.1472                                     
REMARK   3      L13:   3.2706 L23:  -0.5678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2619 S12:   0.4381 S13:  -0.1002                       
REMARK   3      S21:  -1.0921 S22:  -0.0963 S23:  -0.1211                       
REMARK   3      S31:  -0.1197 S32:   0.2353 S33:   0.3637                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN C (RESSEQ 1298)                                  
REMARK   3    ORIGIN FOR THE GROUP (A): -32.4647 -19.4808 -30.2711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5134 T22:   0.8134                                     
REMARK   3      T33:   0.3175 T12:  -0.1591                                     
REMARK   3      T13:  -0.0252 T23:  -0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6057 L22:   5.1814                                     
REMARK   3      L33:   7.7081 L12:   2.1148                                     
REMARK   3      L13:   0.3328 L23:   1.3086                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1383 S12:   0.1352 S13:  -0.3754                       
REMARK   3      S21:  -0.2981 S22:  -0.0282 S23:  -0.3578                       
REMARK   3      S31:  -0.1976 S32:   0.2996 S33:   0.1724                       
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 4BCO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-54254.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92057                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.58                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.36                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NAN                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.22                               
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.16                               
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     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.29                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.41                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: COCRYSTALS WERE GROWN IN                 
REMARK 280  1-1.25M AMMONIUM SULFATE, 0.5-0.9M KCL, 100MM HEPES, PH             
REMARK 280  7.0, 5MM DTT AND IN THE PRESENCE OF COMPOUND.                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.95100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.19100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.90650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.19100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.95100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.90650            
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: 3720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.9 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: 3860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     SER B   171                                                      
REMARK 465     VAL B   172                                                      
REMARK 465     ASN B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     PRO C   222                                                      
REMARK 465     ASP C   223                                                      
REMARK 465     GLU C   224                                                      
REMARK 465     VAL C   225                                                      
REMARK 465     VAL C   226                                                      
REMARK 465     TRP C   227                                                      
REMARK 465     PRO C   228                                                      
REMARK 465     GLY C   229                                                      
REMARK 465     VAL C   230                                                      
REMARK 465     THR C   231                                                      
REMARK 465     SER C   232                                                      
REMARK 465     MET C   233                                                      
REMARK 465     PRO C   234                                                      
REMARK 465     ASP C   235                                                      
REMARK 465     TYR C   236                                                      
REMARK 465     LYS C   237                                                      
REMARK 465     PRO C   238                                                      
REMARK 465     SER C   239                                                      
REMARK 465     PHE C   240                                                      
REMARK 465     PRO C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     TRP C   243                                                      
REMARK 465     ALA C   244                                                      
REMARK 465     ARG C   245                                                      
REMARK 465     GLN C   246                                                      
REMARK 465     ASP C   247                                                      
REMARK 465     PHE C   248                                                      
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 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   OH   TYR C    15     OE1  GLU C    51              1.97            
REMARK 500   O    GLN D   203     O    HOH D  2022              2.14            
REMARK 500   O    HOH B  2017     O    HOH A  2182              2.18            
REMARK 500   O    HOH B  2030     O    HOH B  2031              2.17            
REMARK 500   O    HOH B  2066     O    HOH B  2067              2.19            
REMARK 500   O    HOH D  2006     O    HOH D  2048              2.19            
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  41      -53.16     89.56                                   
REMARK 500    GLU A  73      -67.34    -29.64                                   
REMARK 500    ASP A 127       42.35   -154.02                                   
REMARK 500    ASP A 145       82.69     56.93                                   
REMARK 500    VAL A 164      126.90     75.41                                   
REMARK 500    SER A 181     -148.93   -144.97                                   
REMARK 500    THR A 290     -168.98   -128.37                                   
REMARK 500    TYR B 178       -1.00     72.15                                   
REMARK 500    TRP B 372      113.02    -29.37                                   
REMARK 500    THR C  41      -77.36   -129.01                                   
REMARK 500    ASP C 127       39.17   -146.45                                   
REMARK 500    ASP C 145       82.31     55.78                                   
REMARK 500    PHE C 146       30.30    -98.44                                   
REMARK 500    VAL C 164      127.33     71.04                                   
REMARK 500    SER C 181     -148.23   -155.09                                   
REMARK 500    TYR D 178       -3.52     68.08                                   
REMARK 500    TRP D 372      105.90    -24.03                                   
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 T6Q A1299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T6Q C1298                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B1433                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B1434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM D1433                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM D1434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1435                 
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: 4BCL   RELATED DB: PDB                                   
REMARK 900  BACTERIOCHLOROPHYLL CONTAINING PROTEIN                              
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: 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                            
REMARK 900 RELATED ID: 4BCR   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF PPARALPHA IN COMPLEX WITH WY14643                      
REMARK 900 RELATED ID: 4ACM   RELATED DB: PDB                                   
REMARK 900  CDK2 IN COMPLEX WITH 3-AMINO-6-(4-{[2-(DIMETHYLAMINO                
REMARK 900  )ETHYL]SULFAMOYL}-PHENYL)-N-PYRIDIN-3-YLPYRAZINE-2-                 
REMARK 900  CARBOXAMIDE                                                         
DBREF  4BCO A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4BCO B  171   432  UNP    P30274   CCNA2_BOVIN    169    430             
DBREF  4BCO C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4BCO D  171   432  UNP    P30274   CCNA2_BOVIN    169    430             
SEQADV 4BCO GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCO SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCO GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCO 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 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  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 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  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 4BCO TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4BCO TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    T6Q  A1299      33                                                       
HET    T6Q  C1298      33                                                       
HET    SGM  B1433       6                                                       
HET    SGM  B1434       6                                                       
HET    SGM  D1433       6                                                       
HET    SGM  D1434       6                                                       
HET    SO4  B1435       5                                                       
HET    SO4  D1435       5                                                       
HETNAM     T6Q 2-[[3-(4-ETHANOYL-1,4-DIAZEPAN-1-YL)PHENYL]                      
HETNAM   2 T6Q  AMINO]-4-[4-METHYL-2-(METHYLAMINO)-1,3-THIAZOL-                 
HETNAM   3 T6Q  5-YL]PYRIMIDINE-5-CARBONITRILE                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   5  T6Q    2(C23 H26 N8 O S)                                            
FORMUL   6  SO4    2(O4 S 2-)                                                   
FORMUL   7  SGM    4(C3 H8 O2 S)                                                
FORMUL   8  TPO    2(C4 H10 N O6 P)                                             
HELIX    1   1 SER A    0  GLU A    2  5                                   3    
HELIX    2   2 PRO A   45  LEU A   58  1                                  14    
HELIX    3   3 LEU A   87  SER A   94  1                                   8    
HELIX    4   4 PRO A  100  HIS A  121  1                                  22    
HELIX    5   5 LYS A  129  GLN A  131  5                                   3    
HELIX    6   6 THR A  165  ARG A  169  5                                   5    
HELIX    7   7 ALA A  170  LEU A  175  1                                   6    
HELIX    8   8 THR A  182  ARG A  199  1                                  18    
HELIX    9   9 SER A  207  GLY A  220  1                                  14    
HELIX   10  10 GLY A  229  MET A  233  5                                   5    
HELIX   11  11 ASP A  247  VAL A  252  1                                   6    
HELIX   12  12 ASP A  256  LEU A  267  1                                  12    
HELIX   13  13 SER A  276  LEU A  281  1                                   6    
HELIX   14  14 ALA A  282  GLN A  287  5                                   6    
HELIX   15  15 TYR B  178  CYS B  193  1                                  16    
HELIX   16  16 TYR B  199  GLN B  203  5                                   5    
HELIX   17  17 THR B  207  TYR B  225  1                                  19    
HELIX   18  18 GLN B  228  MET B  246  1                                  19    
HELIX   19  19 LEU B  249  GLU B  269  1                                  21    
HELIX   20  20 GLU B  274  THR B  282  1                                   9    
HELIX   21  21 THR B  287  LEU B  302  1                                  16    
HELIX   22  22 THR B  310  LEU B  320  1                                  11    
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  THR B  368  1                                  18    
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 ASP C  256  LEU C  267  1                                  12    
HELIX   41  41 SER C  276  LEU C  281  1                                   6    
HELIX   42  42 ALA C  282  GLN C  287  5                                   6    
HELIX   43  43 TYR D  178  LYS D  194  1                                  17    
HELIX   44  44 TYR D  199  GLN D  203  5                                   5    
HELIX   45  45 THR D  207  TYR D  225  1                                  19    
HELIX   46  46 GLN D  228  MET D  246  1                                  19    
HELIX   47  47 LEU D  249  GLY D  251  5                                   3    
HELIX   48  48 LYS D  252  GLU D  269  1                                  18    
HELIX   49  49 GLU D  274  ILE D  281  1                                   8    
HELIX   50  50 THR D  287  LEU D  302  1                                  16    
HELIX   51  51 THR D  310  LEU D  320  1                                  11    
HELIX   52  52 ASN D  326  ASP D  343  1                                  18    
HELIX   53  53 ASP D  343  LEU D  348  1                                   6    
HELIX   54  54 LEU D  351  GLY D  369  1                                  19    
HELIX   55  55 PRO D  373  GLY D  381  1                                   9    
HELIX   56  56 LEU D  387  ALA D  401  1                                  15    
HELIX   57  57 PRO D  402  HIS D  404  5                                   3    
HELIX   58  58 GLN D  407  TYR D  413  1                                   7    
HELIX   59  59 LYS D  414  HIS D  419  5                                   6    
HELIX   60  60 GLY D  420  LEU D  424  5                                   5    
SHEET    1  AA 5 PHE A   4  GLU A  12  0                                        
SHEET    2  AA 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3  AA 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 LEU A  66  THR A  72 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1  AC 2 VAL A 123  LEU A 124  0                                        
SHEET    2  AC 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1  CA 5 PHE C   4  GLY C  11  0                                        
SHEET    2  CA 5 VAL C  17  ASN C  23 -1  O  VAL C  18   N  ILE C  10           
SHEET    3  CA 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4  CA 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5  CA 5 LEU C  66  ILE C  70 -1  N  LEU C  67   O  VAL C  79           
SHEET    1  CB 3 GLN C  85  ASP C  86  0                                        
SHEET    2  CB 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3  CB 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1  CC 2 VAL C 123  LEU C 124  0                                        
SHEET    2  CC 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         N   TPO A 160                 C   TYR A 159     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         S1  SGM B1434                 SG  CYS B 193     1555   1555  1.94  
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 GLU A   40    THR A   41          0         9.30                     
CISPEP   2 VAL A  154    PRO A  155          0        -5.65                     
CISPEP   3 GLN B  323    PRO B  324          0        -4.99                     
CISPEP   4 ASP B  345    PRO B  346          0         9.75                     
CISPEP   5 VAL C  154    PRO C  155          0         0.23                     
CISPEP   6 GLN D  323    PRO D  324          0        -1.56                     
CISPEP   7 ASP D  345    PRO D  346          0        10.01                     
SITE     1 AC1 16 GLU A   8  GLY A  13  LYS A  20  ALA A  31                    
SITE     2 AC1 16 VAL A  64  PHE A  80  GLU A  81  PHE A  82                    
SITE     3 AC1 16 LEU A  83  HIS A  84  GLN A  85  LYS A  89                    
SITE     4 AC1 16 ASN A 132  LEU A 134  ASP A 145  HOH A2039                    
SITE     1 AC2 15 GLU C   8  GLY C  13  VAL C  18  VAL C  64                    
SITE     2 AC2 15 PHE C  80  GLU C  81  PHE C  82  LEU C  83                    
SITE     3 AC2 15 HIS C  84  ASP C  86  ASN C 132  LEU C 134                    
SITE     4 AC2 15 ASP C 145  HOH C2056  GLN D 403                               
SITE     1 AC3  2 CYS B 327  GLU B 330                                          
SITE     1 AC4  7 HOH A2048  MET B 189  LYS B 192  CYS B 193                    
SITE     2 AC4  7 ARG B 241  ASP B 305  HOH B2092                               
SITE     1 AC5  6 MET D 189  LYS D 192  CYS D 193  ARG D 241                    
SITE     2 AC5  6 ASP D 305  ALA D 308                                          
SITE     1 AC6  3 ASN D 326  CYS D 327  GLU D 330                               
SITE     1 AC7  8 LYS B 202  GLN B 203  LEU B 243  SER B 244                    
SITE     2 AC7  8 SER B 245  MET B 246  SER B 247  HOH B2072                    
SITE     1 AC8  6 LYS A  65  LYS D 202  LEU D 243  SER D 245                    
SITE     2 AC8  6 MET D 246  SER D 247                                          
CRYST1   73.902  133.813  148.382  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      0.013531  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007473  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006739        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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