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Database: PDB
Entry: 4BCM
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Original site: 4BCM 
HEADER    TRANSFERASE/CELL CYCLE                  02-OCT-12   4BCM              
TITLE     STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2-AMINO-4-           
TITLE    2 HETEROARYL-PYRIMIDINE INHIBITOR                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;         
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: RESIDUES 171-432;                                          
COMPND  11 SYNONYM: CYCLIN-A;                                                   
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CYCLIN-A2;                                                 
COMPND  15 CHAIN: D;                                                            
COMPND  16 FRAGMENT: RESIDUES 171-432;                                          
COMPND  17 SYNONYM: CYCLIN-A;                                                   
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE-CELL CYCLE COMPLEX, CDK-CYCLIN COMPLEX, 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 4BCM    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.    2.45 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) : 2.450                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.462                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.99                          
REMARK   3   NUMBER OF REFLECTIONS             : 55144                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1981                          
REMARK   3   R VALUE            (WORKING SET) : 0.1959                          
REMARK   3   FREE R VALUE                     : 0.2580                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.6                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1999                            
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 52.4738 -  5.9023    0.96     3933   147  0.1954 0.2493        
REMARK   3     2  5.9023 -  4.6858    0.98     3823   144  0.1706 0.2276        
REMARK   3     3  4.6858 -  4.0937    0.98     3808   143  0.1458 0.1945        
REMARK   3     4  4.0937 -  3.7196    0.99     3817   144  0.1554 0.2230        
REMARK   3     5  3.7196 -  3.4530    1.00     3821   144  0.1760 0.2209        
REMARK   3     6  3.4530 -  3.2495    1.00     3806   143  0.1846 0.2645        
REMARK   3     7  3.2495 -  3.0867    0.99     3754   141  0.1995 0.2577        
REMARK   3     8  3.0867 -  2.9524    0.99     3813   144  0.2200 0.3105        
REMARK   3     9  2.9524 -  2.8387    0.99     3759   141  0.2290 0.3110        
REMARK   3    10  2.8387 -  2.7408    0.99     3770   142  0.2409 0.3194        
REMARK   3    11  2.7408 -  2.6551    0.99     3745   141  0.2534 0.3138        
REMARK   3    12  2.6551 -  2.5792    0.99     3782   142  0.2825 0.3578        
REMARK   3    13  2.5792 -  2.5113    0.99     3772   143  0.3093 0.3846        
REMARK   3    14  2.5113 -  2.4500    1.00     3742   140  0.3207 0.3714        
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              : 0.380                                         
REMARK   3   B_SOL              : 49.742                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.85             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.48            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.12                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.0055                                              
REMARK   3    B22 (A**2) : 2.8361                                               
REMARK   3    B33 (A**2) : 2.1693                                               
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      :  0.006           9049                                  
REMARK   3   ANGLE     :  0.964          12285                                  
REMARK   3   CHIRALITY :  0.063           1378                                  
REMARK   3   PLANARITY :  0.004           1532                                  
REMARK   3   DIHEDRAL  : 15.134           3396                                  
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):  10.6777  14.3532  24.3445              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2078 T22:   0.2961                                     
REMARK   3      T33:   0.2063 T12:  -0.0350                                     
REMARK   3      T13:   0.0115 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3242 L22:   1.8671                                     
REMARK   3      L33:   1.8461 L12:   0.1744                                     
REMARK   3      L13:   0.0594 L23:   0.9211                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0841 S12:  -0.2439 S13:  -0.1462                       
REMARK   3      S21:   0.1444 S22:  -0.3148 S23:   0.1673                       
REMARK   3      S31:   0.1669 S32:  -0.3376 S33:   0.1353                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 86:298)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8776  31.4373   3.9811              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0793 T22:   0.1819                                     
REMARK   3      T33:   0.1939 T12:   0.0039                                     
REMARK   3      T13:   0.0257 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5250 L22:   0.5945                                     
REMARK   3      L33:   0.5703 L12:  -0.2515                                     
REMARK   3      L13:   0.5859 L23:  -0.3675                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0460 S12:   0.0089 S13:   0.1384                       
REMARK   3      S21:  -0.0327 S22:  -0.0318 S23:   0.0156                       
REMARK   3      S31:  -0.0501 S32:  -0.0562 S33:   0.0025                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6305  -0.1252  -2.9672              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1503 T22:   0.1066                                     
REMARK   3      T33:   0.1433 T12:   0.0070                                     
REMARK   3      T13:  -0.0071 T23:  -0.0159                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0054 L22:   1.0011                                     
REMARK   3      L33:   1.3369 L12:   0.3431                                     
REMARK   3      L13:  -0.1706 L23:  -0.0880                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0411 S12:   0.0876 S13:  -0.0513                       
REMARK   3      S21:  -0.0335 S22:   0.0375 S23:  -0.0201                       
REMARK   3      S31:   0.2300 S32:  -0.0018 S33:   0.0094                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 1:85)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3980  -8.1867  31.6681              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2756 T22:   0.3965                                     
REMARK   3      T33:   0.1638 T12:   0.0643                                     
REMARK   3      T13:  -0.0189 T23:   0.1126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6208 L22:   0.9854                                     
REMARK   3      L33:   0.8112 L12:   0.1777                                     
REMARK   3      L13:   0.1885 L23:   0.6388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0555 S12:  -0.3283 S13:  -0.1301                       
REMARK   3      S21:   0.1623 S22:  -0.1152 S23:   0.0146                       
REMARK   3      S31:   0.1755 S32:   0.1321 S33:   0.0399                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN C AND (RESSEQ 86:298)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  55.1021 -14.5707  34.1527              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2981 T22:   0.9365                                     
REMARK   3      T33:   0.3792 T12:   0.2744                                     
REMARK   3      T13:   0.0469 T23:   0.3038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3191 L22:   1.0351                                     
REMARK   3      L33:   0.2982 L12:  -0.2873                                     
REMARK   3      L13:  -0.1533 L23:  -0.2797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0198 S12:  -0.3514 S13:  -0.0950                       
REMARK   3      S21:   0.0340 S22:  -0.1654 S23:  -0.4226                       
REMARK   3      S31:   0.2033 S32:   0.6222 S33:   0.1510                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  43.0768  19.6267  34.7201              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3435 T22:   0.6892                                     
REMARK   3      T33:   0.2521 T12:  -0.4054                                     
REMARK   3      T13:   0.0258 T23:   0.0096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8113 L22:   0.8617                                     
REMARK   3      L33:   0.5118 L12:  -0.0057                                     
REMARK   3      L13:  -0.1387 L23:  -0.0734                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0476 S12:  -0.1908 S13:   0.2340                       
REMARK   3      S21:  -0.0790 S22:  -0.0639 S23:  -0.3498                       
REMARK   3      S31:  -0.3129 S32:   0.6883 S33:  -0.0249                       
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 4BCM 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-54251.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55186                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.39                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.54                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.47                               
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.25                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.52                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.42                               
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, IN THE PRESENCE OF          
REMARK 280  100MM HEPES, PH 7.0, 5MM DTT AND COMPOUND                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.03500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.31500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.70500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.31500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.03500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.70500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.4 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     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     ARG A   297                                                      
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     PRO C    -2                                                      
REMARK 465     GLY C    -1                                                      
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     GLN D   322                                                      
REMARK 465     GLN D   323                                                      
REMARK 465     PRO D   324                                                      
REMARK 465     ALA D   325                                                      
REMARK 465     ASN D   326                                                      
REMARK 465     CYS D   327                                                      
REMARK 465     LYS D   328                                                      
REMARK 465     VAL D   329                                                      
REMARK 465     GLU D   330                                                      
REMARK 465     LEU D   364                                                      
REMARK 465     TYR D   365                                                      
REMARK 465     THR D   366                                                      
REMARK 465     VAL D   367                                                      
REMARK 465     THR D   368                                                      
REMARK 465     GLY D   369                                                      
REMARK 465     GLN D   370                                                      
REMARK 465     SER D   371                                                      
REMARK 465     THR D   429                                                      
REMARK 465     LEU D   430                                                      
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   OE2  GLU A    51     O    HOH A  2016              2.16            
REMARK 500   NH2  ARG A   150     O    GLU B   268              2.20            
REMARK 500   O    ASP A   235     O    HOH A  2099              2.20            
REMARK 500   O    GLN B   203     O    HOH B  2025              2.12            
REMARK 500   OE1  GLN B   317     O    HOH B  2016              2.06            
REMARK 500   O    ARG C   157     O    HOH C  2024              2.11            
REMARK 500   O    PRO C   204     O    HOH C  2034              2.12            
REMARK 500   O    GLN D   203     O    HOH D  2002              2.17            
REMARK 500   O    HOH A  2036     O    HOH A  2116              2.11            
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    GLU A   8      160.91    177.32                                   
REMARK 500    THR A  72     -160.04   -123.45                                   
REMARK 500    SER A  94       31.89    -82.85                                   
REMARK 500    ASP A 127       40.91   -159.40                                   
REMARK 500    ASP A 145       79.02     58.72                                   
REMARK 500    VAL A 164      129.96     79.09                                   
REMARK 500    SER A 181     -155.91   -145.56                                   
REMARK 500    TRP B 372      108.21    -47.28                                   
REMARK 500    ASN B 431       82.15     64.48                                   
REMARK 500    THR C  41      -85.37   -127.00                                   
REMARK 500    LEU C  96      -70.28    -81.40                                   
REMARK 500    ASP C 127       38.17   -157.59                                   
REMARK 500    LYS C 129      153.93    175.20                                   
REMARK 500    ASP C 145       79.88     58.31                                   
REMARK 500    VAL C 164      132.37     70.08                                   
REMARK 500    LEU C 166      -73.96    -11.16                                   
REMARK 500    SER C 181     -156.64   -152.24                                   
REMARK 500    PRO C 204       63.72    -66.04                                   
REMARK 500    THR C 218      -37.78   -130.12                                   
REMARK 500    ASP C 256     -172.92    -59.91                                   
REMARK 500    THR C 290     -165.77   -127.46                                   
REMARK 500    PRO D 373      156.46    -47.87                                   
REMARK 500    LEU D 387       32.73    -94.04                                   
REMARK 500    TYR D 413       30.99    -90.24                                   
REMARK 500    PRO D 427       39.50    -66.47                                   
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 SGM D1429                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B1433                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T7Z C1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T7Z A1297                 
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: 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  4BCM A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4BCM B  171   432  UNP    P20248   CCNA2_HUMAN    171    432             
DBREF  4BCM C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4BCM D  171   432  UNP    P20248   CCNA2_HUMAN    171    432             
SEQADV 4BCM PRO A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCM GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCM SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCM PRO C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCM GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCM SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4BCM LEU D  331  UNP  P20248    SER   331 CONFLICT                       
SEQRES   1 A  301  PRO GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE          
SEQRES   2 A  301  GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN          
SEQRES   3 A  301  LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG          
SEQRES   4 A  301  LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE          
SEQRES   5 A  301  ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN          
SEQRES   6 A  301  ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS          
SEQRES   7 A  301  LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS          
SEQRES   8 A  301  LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU          
SEQRES   9 A  301  PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY          
SEQRES  10 A  301  LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP          
SEQRES  11 A  301  LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA          
SEQRES  12 A  301  ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY          
SEQRES  13 A  301  VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU          
SEQRES  14 A  301  TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR          
SEQRES  15 A  301  TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE          
SEQRES  16 A  301  PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY          
SEQRES  17 A  301  ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR          
SEQRES  18 A  301  LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR          
SEQRES  19 A  301  SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA          
SEQRES  20 A  301  ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU          
SEQRES  21 A  301  ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP          
SEQRES  22 A  301  PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS          
SEQRES  23 A  301  PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU          
SEQRES  24 A  301  ARG 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  301  PRO GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE          
SEQRES   2 C  301  GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN          
SEQRES   3 C  301  LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG          
SEQRES   4 C  301  LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE          
SEQRES   5 C  301  ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN          
SEQRES   6 C  301  ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS          
SEQRES   7 C  301  LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS          
SEQRES   8 C  301  LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU          
SEQRES   9 C  301  PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY          
SEQRES  10 C  301  LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP          
SEQRES  11 C  301  LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA          
SEQRES  12 C  301  ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY          
SEQRES  13 C  301  VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU          
SEQRES  14 C  301  TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR          
SEQRES  15 C  301  TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE          
SEQRES  16 C  301  PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY          
SEQRES  17 C  301  ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR          
SEQRES  18 C  301  LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR          
SEQRES  19 C  301  SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA          
SEQRES  20 C  301  ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU          
SEQRES  21 C  301  ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP          
SEQRES  22 C  301  PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS          
SEQRES  23 C  301  PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU          
SEQRES  24 C  301  ARG 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 LEU 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 4BCM TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4BCM TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    SGM  D1429       6                                                       
HET    SGM  B1433       6                                                       
HET    T7Z  C1295      33                                                       
HET    T7Z  A1297      33                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETNAM     T7Z 4-(4-METHYL-2-METHYLIMINO-3H-1,3-THIAZOL-5-                      
HETNAM   2 T7Z  YL)-2-[(4-METHYL-3-MORPHOLIN-4-YLSULFONYL-                      
HETNAM   3 T7Z  PHENYL)AMINO]PYRIMIDINE-5-CARBONITRILE                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   5  TPO    2(C4 H10 N O6 P)                                             
FORMUL   6  SGM    2(C3 H8 O2 S)                                                
FORMUL   7  T7Z    2(C21 H23 N7 O3 S2)                                          
FORMUL   8  HOH   *287(H2 O)                                                    
HELIX    1   1 SER A    0  GLU A    2  5                                   3    
HELIX    2   2 PRO A   45  LEU A   58  1                                  14    
HELIX    3   3 LEU A   87  SER A   94  1                                   8    
HELIX    4   4 PRO A  100  HIS A  121  1                                  22    
HELIX    5   5 LYS A  129  GLN A  131  5                                   3    
HELIX    6   6 THR A  165  ARG A  169  5                                   5    
HELIX    7   7 ALA A  170  LEU A  175  1                                   6    
HELIX    8   8 THR A  182  ARG A  199  1                                  18    
HELIX    9   9 SER A  207  GLY A  220  1                                  14    
HELIX   10  10 GLY A  229  MET A  233  5                                   5    
HELIX   11  11 ASP A  247  VAL A  252  1                                   6    
HELIX   12  12 ASP A  256  LEU A  267  1                                  12    
HELIX   13  13 SER A  276  LEU A  281  1                                   6    
HELIX   14  14 ALA A  282  GLN A  287  5                                   6    
HELIX   15  15 TYR B  178  CYS B  193  1                                  16    
HELIX   16  16 THR B  207  TYR B  225  1                                  19    
HELIX   17  17 GLN B  228  SER B  244  1                                  17    
HELIX   18  18 LEU B  249  GLU B  269  1                                  21    
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  LEU B  320  1                                  11    
HELIX   22  22 ASN B  326  ASP B  343  1                                  18    
HELIX   23  23 ASP B  343  LEU B  348  1                                   6    
HELIX   24  24 LEU B  351  GLY B  369  1                                  19    
HELIX   25  25 PRO B  373  GLY B  381  1                                   9    
HELIX   26  26 THR B  383  ALA B  401  1                                  19    
HELIX   27  27 PRO B  402  HIS B  404  5                                   3    
HELIX   28  28 GLN B  407  TYR B  413  1                                   7    
HELIX   29  29 LYS B  414  HIS B  419  5                                   6    
HELIX   30  30 GLY B  420  LEU B  424  5                                   5    
HELIX   31  31 PRO C   45  LYS C   56  1                                  12    
HELIX   32  32 LEU C   87  SER C   94  1                                   8    
HELIX   33  33 PRO C  100  SER C  120  1                                  21    
HELIX   34  34 LYS C  129  GLN C  131  5                                   3    
HELIX   35  35 ASP C  145  ALA C  149  5                                   5    
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  247  VAL C  252  1                                   6    
HELIX   41  41 ASP C  256  LEU C  267  1                                  12    
HELIX   42  42 SER C  276  HIS C  283  1                                   8    
HELIX   43  43 PRO C  284  GLN C  287  5                                   4    
HELIX   44  44 TYR D  178  CYS D  193  1                                  16    
HELIX   45  45 THR D  207  LYS D  226  1                                  20    
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  THR D  282  1                                   9    
HELIX   50  50 THR D  287  LEU D  302  1                                  16    
HELIX   51  51 THR D  310  PHE D  319  1                                  10    
HELIX   52  52 LEU D  331  ASP D  343  1                                  13    
HELIX   53  53 ASP D  343  LEU D  348  1                                   6    
HELIX   54  54 LEU D  351  ALA D  363  1                                  13    
HELIX   55  55 PRO D  373  GLY D  381  1                                   9    
HELIX   56  56 LEU D  387  LYS D  400  1                                  14    
HELIX   57  57 ALA D  401  HIS D  404  5                                   4    
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 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  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1  AC 2 VAL A 123  LEU A 124  0                                        
SHEET    2  AC 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1  CA 5 PHE C   4  GLU C  12  0                                        
SHEET    2  CA 5 GLY C  16  ASN C  23 -1  O  VAL C  18   N  ILE C  10           
SHEET    3  CA 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4  CA 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5  CA 5 LEU C  66  ILE C  70 -1  N  LEU C  67   O  VAL C  79           
SHEET    1  CB 3 GLN C  85  ASP C  86  0                                        
SHEET    2  CB 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3  CB 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1  CC 2 VAL C 123  LEU C 124  0                                        
SHEET    2  CC 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         N   TPO A 160                 C   TYR A 159     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
LINK         N   TPO C 160                 C   TYR C 159     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0       -11.17                     
CISPEP   2 GLN B  323    PRO B  324          0        -6.50                     
CISPEP   3 ASP B  345    PRO B  346          0        11.04                     
CISPEP   4 VAL C  154    PRO C  155          0        -0.44                     
CISPEP   5 ASP D  345    PRO D  346          0         7.13                     
SITE     1 AC1  6 MET D 189  LYS D 192  CYS D 193  ARG D 241                    
SITE     2 AC1  6 ASP D 305  HOH D2017                                          
SITE     1 AC2  5 MET B 189  CYS B 193  ARG B 241  ASP B 305                    
SITE     2 AC2  5 HOH B2106                                                     
SITE     1 AC3 13 ILE C  10  GLU C  12  VAL C  18  PHE C  80                    
SITE     2 AC3 13 GLU C  81  PHE C  82  LEU C  83  HIS C  84                    
SITE     3 AC3 13 ASP C  86  LYS C  89  LEU C 134  HOH C2018                    
SITE     4 AC3 13 HOH C2022                                                     
SITE     1 AC4 16 ILE A  10  GLY A  11  GLU A  12  VAL A  18                    
SITE     2 AC4 16 VAL A  64  PHE A  80  GLU A  81  PHE A  82                    
SITE     3 AC4 16 LEU A  83  HIS A  84  ASP A  86  LYS A  89                    
SITE     4 AC4 16 LEU A 134  HOH A2035  HOH A2056  HOH A2057                    
CRYST1   74.070  135.410  148.630  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      0.013501  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007385  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006728        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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