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Database: PDB
Entry: 6ATH
LinkDB: 6ATH
Original site: 6ATH 
HEADER    TRANSFERASE                             29-AUG-17   6ATH              
TITLE     CDK2/CYCLIN A/P27-KID-DELTAC                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2,P33 PROTEIN KINASE;          
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: PHOSPHORYLATED;                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CYCLIN-A2;                                                 
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 173-432;                                      
COMPND  12 SYNONYM: CYCLIN-A,CYCLIN A;                                          
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: CYCLIN-DEPENDENT KINASE INHIBITOR 1B;                      
COMPND  16 CHAIN: C;                                                            
COMPND  17 FRAGMENT: UNP RESIDUES 22-85;                                        
COMPND  18 SYNONYM: CYCLIN-DEPENDENT KINASE INHIBITOR P27,P27KIP1;              
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX4T1;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: CDKN1B, KIP1;                                                  
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    INHIBITOR, COMPLEX, IDP, CDK, CYCLIN, KINASE, PHOSPHORTLATION,        
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.W.WHITE,M.YUN                                                       
REVDAT   4   24-APR-19 6ATH    1       JRNL                                     
REVDAT   3   10-APR-19 6ATH    1       JRNL                                     
REVDAT   2   20-FEB-19 6ATH    1       REMARK                                   
REVDAT   1   12-SEP-18 6ATH    0                                                
JRNL        AUTH   M.TSYTLONOK,H.SANABRIA,Y.WANG,S.FELEKYAN,K.HEMMEN,           
JRNL        AUTH 2 A.H.PHILLIPS,M.K.YUN,M.B.WADDELL,C.G.PARK,S.VAITHIYALINGAM,  
JRNL        AUTH 3 L.ICONARU,S.W.WHITE,P.TOMPA,C.A.M.SEIDEL,R.KRIWACKI          
JRNL        TITL   DYNAMIC ANTICIPATION BY CDK2/CYCLIN A-BOUND P27 MEDIATES     
JRNL        TITL 2 SIGNAL INTEGRATION IN CELL CYCLE REGULATION.                 
JRNL        REF    NAT COMMUN                    V.  10  1676 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30976006                                                     
JRNL        DOI    10.1038/S41467-019-09446-W                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.3_928                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 71378                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3582                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.6286 -  5.3689    1.00     2848   147  0.2001 0.2011        
REMARK   3     2  5.3689 -  4.2656    1.00     2728   146  0.1581 0.1690        
REMARK   3     3  4.2656 -  3.7275    1.00     2681   148  0.1509 0.1525        
REMARK   3     4  3.7275 -  3.3873    1.00     2681   144  0.1585 0.1766        
REMARK   3     5  3.3873 -  3.1448    1.00     2657   146  0.1772 0.1903        
REMARK   3     6  3.1448 -  2.9595    1.00     2684   131  0.1827 0.2112        
REMARK   3     7  2.9595 -  2.8114    1.00     2670   119  0.1808 0.1770        
REMARK   3     8  2.8114 -  2.6891    1.00     2623   146  0.1698 0.1722        
REMARK   3     9  2.6891 -  2.5857    1.00     2663   145  0.1683 0.1781        
REMARK   3    10  2.5857 -  2.4965    1.00     2638   111  0.1615 0.2378        
REMARK   3    11  2.4965 -  2.4185    1.00     2644   135  0.1610 0.1666        
REMARK   3    12  2.4185 -  2.3494    1.00     2662   128  0.1609 0.1916        
REMARK   3    13  2.3494 -  2.2876    1.00     2610   129  0.1613 0.1938        
REMARK   3    14  2.2876 -  2.2318    1.00     2641   132  0.1586 0.1749        
REMARK   3    15  2.2318 -  2.1810    1.00     2618   124  0.1531 0.1668        
REMARK   3    16  2.1810 -  2.1346    1.00     2629   170  0.1484 0.1679        
REMARK   3    17  2.1346 -  2.0920    1.00     2603   135  0.1531 0.1779        
REMARK   3    18  2.0920 -  2.0525    1.00     2587   139  0.1546 0.1772        
REMARK   3    19  2.0525 -  2.0158    1.00     2652   138  0.1573 0.1836        
REMARK   3    20  2.0158 -  1.9817    1.00     2579   139  0.1621 0.2051        
REMARK   3    21  1.9817 -  1.9497    0.98     2541   139  0.1787 0.2214        
REMARK   3    22  1.9497 -  1.9197    0.97     2533   151  0.1915 0.2581        
REMARK   3    23  1.9197 -  1.8915    0.97     2509   152  0.2170 0.2225        
REMARK   3    24  1.8915 -  1.8649    0.98     2560   121  0.2286 0.2399        
REMARK   3    25  1.8649 -  1.8397    0.96     2484   147  0.2596 0.2892        
REMARK   3    26  1.8397 -  1.8158    0.80     2071   120  0.2914 0.2772        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 42.91                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.440           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.19490                                             
REMARK   3    B22 (A**2) : 1.69790                                              
REMARK   3    B33 (A**2) : -1.50300                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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           4903                                  
REMARK   3   ANGLE     :  0.940           6661                                  
REMARK   3   CHIRALITY :  0.068            746                                  
REMARK   3   PLANARITY :  0.005            840                                  
REMARK   3   DIHEDRAL  : 14.082           1830                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  17.1938   9.2721  71.8809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0761 T22:   0.1253                                     
REMARK   3      T33:   0.0963 T12:  -0.0195                                     
REMARK   3      T13:   0.0379 T23:  -0.0349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2434 L22:   0.9592                                     
REMARK   3      L33:   1.1998 L12:  -0.4186                                     
REMARK   3      L13:  -0.1776 L23:   0.4075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0896 S12:  -0.1458 S13:   0.0112                       
REMARK   3      S21:   0.1193 S22:   0.0057 S23:   0.0630                       
REMARK   3      S31:   0.2019 S32:  -0.0512 S33:   0.0314                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  31.8965  -5.5514  45.7430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0861 T22:   0.0636                                     
REMARK   3      T33:   0.0708 T12:   0.0018                                     
REMARK   3      T13:   0.0139 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9857 L22:   1.4135                                     
REMARK   3      L33:   1.1638 L12:   0.1627                                     
REMARK   3      L13:  -0.2098 L23:   0.3742                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0401 S12:   0.0205 S13:   0.0272                       
REMARK   3      S21:  -0.0243 S22:  -0.0016 S23:   0.0753                       
REMARK   3      S31:   0.1071 S32:  -0.0280 S33:   0.0254                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0649 -23.9802  67.1630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9315 T22:   0.2307                                     
REMARK   3      T33:   0.2607 T12:  -0.0711                                     
REMARK   3      T13:   0.1370 T23:   0.1762                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1466 L22:   0.1956                                     
REMARK   3      L33:   1.4249 L12:  -0.1567                                     
REMARK   3      L13:  -0.0979 L23:  -0.0710                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2282 S12:  -0.3142 S13:  -0.5608                       
REMARK   3      S21:   0.7855 S22:   0.0352 S23:   0.1470                       
REMARK   3      S31:   0.4297 S32:  -0.0250 S33:  -0.1744                       
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 6ATH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229789.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71452                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 10.70                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP V9.2.10                                        
REMARK 200 STARTING MODEL: 1JSU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, LITHIUM SULFATE, PH 7.2, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291.15K                        
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       37.09550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.75550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.82250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.75550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.09550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.82250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     TYR A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     SER B   171                                                      
REMARK 465     MET B   172                                                      
REMARK 465     GLY C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     HIS C    20                                                      
REMARK 465     MET C    21                                                      
REMARK 465     GLU C    22                                                      
REMARK 465     HIS C    23                                                      
REMARK 465     PRO C    24                                                      
REMARK 465     CYS C    49                                                      
REMARK 465     ARG C    50                                                      
REMARK 465     ASP C    51                                                      
REMARK 465     MET C    52                                                      
REMARK 465     GLU C    53                                                      
REMARK 465     GLU C    80                                                      
REMARK 465     LYS C    81                                                      
REMARK 465     GLY C    82                                                      
REMARK 465     SER C    83                                                      
REMARK 465     LEU C    84                                                      
REMARK 465     PRO C    85                                                      
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     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 323    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  54    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  71    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  58       62.00   -111.79                                   
REMARK 500    ASP A 127       48.53   -151.02                                   
REMARK 500    ASP A 145       77.46     60.00                                   
REMARK 500    VAL A 164      132.44     76.92                                   
REMARK 500    SER A 181     -137.01   -151.92                                   
REMARK 500    THR A 290     -167.41   -129.71                                   
REMARK 500    PHE B 304       15.71     59.28                                   
REMARK 500    PRO B 324     -166.84   -100.65                                   
REMARK 500    TRP B 372      112.54    -28.70                                   
REMARK 500    ASN C  61       56.58     37.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 684        DISTANCE =  6.51 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301                 
DBREF  6ATH A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  6ATH B  173   432  UNP    P20248   CCNA2_HUMAN    173    432             
DBREF  6ATH C   22    85  UNP    P46527   CDN1B_HUMAN     22     85             
SEQADV 6ATH GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 6ATH SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 6ATH GLY B  170  UNP  P20248              EXPRESSION TAG                 
SEQADV 6ATH SER B  171  UNP  P20248              EXPRESSION TAG                 
SEQADV 6ATH MET B  172  UNP  P20248              EXPRESSION TAG                 
SEQADV 6ATH GLY C   18  UNP  P46527              EXPRESSION TAG                 
SEQADV 6ATH SER C   19  UNP  P46527              EXPRESSION TAG                 
SEQADV 6ATH HIS C   20  UNP  P46527              EXPRESSION TAG                 
SEQADV 6ATH MET C   21  UNP  P46527              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  263  GLY SER MET ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE          
SEQRES   2 B  263  HIS THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO          
SEQRES   3 B  263  LYS VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN          
SEQRES   4 B  263  SER MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL          
SEQRES   5 B  263  GLY GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU          
SEQRES   6 B  263  ALA VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER          
SEQRES   7 B  263  VAL LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA          
SEQRES   8 B  263  MET LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO          
SEQRES   9 B  263  GLU VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR          
SEQRES  10 B  263  THR LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU          
SEQRES  11 B  263  LYS VAL LEU THR PHE ASP LEU ALA ALA PRO THR VAL ASN          
SEQRES  12 B  263  GLN PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA          
SEQRES  13 B  263  ASN CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU          
SEQRES  14 B  263  LEU SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU          
SEQRES  15 B  263  PRO SER VAL ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU          
SEQRES  16 B  263  TYR THR VAL THR GLY GLN SER TRP PRO GLU SER LEU ILE          
SEQRES  17 B  263  ARG LYS THR GLY TYR THR LEU GLU SER LEU LYS PRO CYS          
SEQRES  18 B  263  LEU MET ASP LEU HIS GLN THR TYR LEU LYS ALA PRO GLN          
SEQRES  19 B  263  HIS ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER          
SEQRES  20 B  263  LYS TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR          
SEQRES  21 B  263  LEU ASN LEU                                                  
SEQRES   1 C   68  GLY SER HIS MET GLU HIS PRO LYS PRO SER ALA CYS ARG          
SEQRES   2 C   68  ASN LEU PHE GLY PRO VAL ASP HIS GLU GLU LEU THR ARG          
SEQRES   3 C   68  ASP LEU GLU LYS HIS CYS ARG ASP MET GLU GLU ALA SER          
SEQRES   4 C   68  GLN ARG LYS TRP ASN PHE ASP PHE GLN ASN HIS LYS PRO          
SEQRES   5 C   68  LEU GLU GLY LYS TYR GLU TRP GLN GLU VAL GLU LYS GLY          
SEQRES   6 C   68  SER LEU PRO                                                  
MODRES 6ATH TPO A  160  THR  MODIFIED RESIDUE                                   
HET    TPO  A 160      11                                                       
HET    SO4  A 301       5                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *399(H2 O)                                                    
HELIX    1 AA1 PRO A   45  LYS A   56  1                                  12    
HELIX    2 AA2 LEU A   87  SER A   94  1                                   8    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 THR A  165  ARG A  169  5                                   5    
HELIX    6 AA6 ALA A  170  LEU A  175  1                                   6    
HELIX    7 AA7 THR A  182  ARG A  199  1                                  18    
HELIX    8 AA8 SER A  207  GLY A  220  1                                  14    
HELIX    9 AA9 GLY A  229  MET A  233  5                                   5    
HELIX   10 AB1 ASP A  247  VAL A  252  1                                   6    
HELIX   11 AB2 ASP A  256  LEU A  267  1                                  12    
HELIX   12 AB3 SER A  276  LEU A  281  1                                   6    
HELIX   13 AB4 ALA A  282  GLN A  287  5                                   6    
HELIX   14 AB5 TYR B  178  CYS B  193  1                                  16    
HELIX   15 AB6 GLY B  198  GLN B  203  5                                   6    
HELIX   16 AB7 THR B  207  TYR B  225  1                                  19    
HELIX   17 AB8 GLN B  228  MET B  246  1                                  19    
HELIX   18 AB9 LEU B  249  GLU B  269  1                                  21    
HELIX   19 AC1 GLU B  274  THR B  282  1                                   9    
HELIX   20 AC2 THR B  287  LEU B  302  1                                  16    
HELIX   21 AC3 THR B  310  LEU B  320  1                                  11    
HELIX   22 AC4 ASN B  326  ASP B  343  1                                  18    
HELIX   23 AC5 ASP B  343  LEU B  348  1                                   6    
HELIX   24 AC6 LEU B  351  GLY B  369  1                                  19    
HELIX   25 AC7 PRO B  373  GLY B  381  1                                   9    
HELIX   26 AC8 THR B  383  ALA B  401  1                                  19    
HELIX   27 AC9 PRO B  402  HIS B  404  5                                   3    
HELIX   28 AD1 GLN B  407  TYR B  413  1                                   7    
HELIX   29 AD2 LYS B  414  HIS B  419  5                                   6    
HELIX   30 AD3 GLY B  420  LEU B  424  5                                   5    
HELIX   31 AD4 ASP C   37  HIS C   48  1                                  12    
HELIX   32 AD5 ALA C   55  ASN C   61  1                                   7    
SHEET    1 AA1 5 LEU A  66  HIS A  71  0                                        
SHEET    2 AA1 5 LYS A  75  GLU A  81 -1  O  TYR A  77   N  ILE A  70           
SHEET    3 AA1 5 VAL A  29  ARG A  36 -1  N  LYS A  33   O  LEU A  78           
SHEET    4 AA1 5 TYR A  19  ASN A  23 -1  N  TYR A  19   O  LEU A  32           
SHEET    5 AA1 5 TYR C  74  GLU C  78 -1  O  GLN C  77   N  LYS A  20           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1 AA4 2 PHE C  62  ASP C  63  0                                        
SHEET    2 AA4 2 LYS C  68  PRO C  69 -1  O  LYS C  68   N  ASP C  63           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0        -5.67                     
CISPEP   2 GLN B  323    PRO B  324          0        -8.31                     
CISPEP   3 ASP B  345    PRO B  346          0        12.02                     
SITE     1 AC1  7 ARG A 214  ARG A 217  LYS A 278  HOH A 405                    
SITE     2 AC1  7 HOH A 414  HOH A 552  HOH B 531                               
CRYST1   74.191   77.645  137.511  90.00  90.00  90.00 P 21 21 21    4          
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      0.013479  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012879  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007272        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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