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Database: PDB
Entry: 4WB5
LinkDB: 4WB5
Original site: 4WB5 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       02-SEP-14   4WB5              
TITLE     CRYSTAL STRUCTURE OF HUMAN CAMP-DEPENDENT PROTEIN KINASE A (CATALYTIC 
TITLE    2 ALPHA SUBUNIT)                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PKI (5-24);                                                
COMPND   9 CHAIN: I;                                                            
COMPND  10 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: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PLATE11;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    CATALYSIS, PROTEIN KINASE, ADENOSINE TRIPHOSPHATE, PHOSPHORYLATION,   
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.CHEUNG,C.GINTER,M.CASSIDY,M.C.FRANKLIN,M.J.RUDOLPH,W.A.HENDRICKSON  
REVDAT   5   22-NOV-17 4WB5    1       SOURCE KEYWDS JRNL   REMARK              
REVDAT   4   25-FEB-15 4WB5    1       REMARK                                   
REVDAT   3   11-FEB-15 4WB5    1       JRNL                                     
REVDAT   2   04-FEB-15 4WB5    1       JRNL                                     
REVDAT   1   21-JAN-15 4WB5    0                                                
JRNL        AUTH   J.CHEUNG,C.GINTER,M.CASSIDY,M.C.FRANKLIN,M.J.RUDOLPH,        
JRNL        AUTH 2 N.ROBINE,R.B.DARNELL,W.A.HENDRICKSON                         
JRNL        TITL   STRUCTURAL INSIGHTS INTO MIS-REGULATION OF PROTEIN KINASE A  
JRNL        TITL 2 IN HUMAN TUMORS.                                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 112  1374 2015              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   25605907                                                     
JRNL        DOI    10.1073/PNAS.1424206112                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.59                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 54455                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2641                            
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 36.5981 -  4.3765    0.98     2895   151  0.1469 0.1483        
REMARK   3     2  4.3765 -  3.4746    0.99     2796   153  0.1362 0.1714        
REMARK   3     3  3.4746 -  3.0356    1.00     2784   152  0.1630 0.1871        
REMARK   3     4  3.0356 -  2.7582    1.00     2756   150  0.1703 0.2277        
REMARK   3     5  2.7582 -  2.5605    1.00     2763   163  0.1729 0.2263        
REMARK   3     6  2.5605 -  2.4096    1.00     2712   170  0.1682 0.2149        
REMARK   3     7  2.4096 -  2.2889    1.00     2743   141  0.1648 0.1947        
REMARK   3     8  2.2889 -  2.1893    1.00     2741   153  0.1656 0.2076        
REMARK   3     9  2.1893 -  2.1050    1.00     2756   125  0.1614 0.1977        
REMARK   3    10  2.1050 -  2.0324    1.00     2729   119  0.1620 0.1811        
REMARK   3    11  2.0324 -  1.9689    1.00     2767   111  0.1709 0.2082        
REMARK   3    12  1.9689 -  1.9126    1.00     2752   142  0.1846 0.2131        
REMARK   3    13  1.9126 -  1.8622    1.00     2747   130  0.1984 0.2731        
REMARK   3    14  1.8622 -  1.8168    1.00     2706   145  0.1920 0.2335        
REMARK   3    15  1.8168 -  1.7755    1.00     2733   134  0.1869 0.2390        
REMARK   3    16  1.7755 -  1.7377    1.00     2714   135  0.1970 0.2394        
REMARK   3    17  1.7377 -  1.7030    1.00     2739   125  0.2060 0.2039        
REMARK   3    18  1.7030 -  1.6708    1.00     2714   134  0.2316 0.2879        
REMARK   3    19  1.6708 -  1.6410    0.83     2267   108  0.2485 0.3354        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.740           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.24                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.012           3162                                  
REMARK   3   ANGLE     :  1.372           4295                                  
REMARK   3   CHIRALITY :  0.073            449                                  
REMARK   3   PLANARITY :  0.007            548                                  
REMARK   3   DIHEDRAL  : 14.174           1187                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 13 THROUGH 31 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -40.1574   1.3557  18.0822              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3270 T22:   0.3562                                     
REMARK   3      T33:   0.3154 T12:   0.0670                                     
REMARK   3      T13:   0.0848 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9450 L22:   3.7200                                     
REMARK   3      L33:   3.4917 L12:  -4.6879                                     
REMARK   3      L13:   0.9980 L23:  -1.7184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0135 S12:  -0.2965 S13:   0.2966                       
REMARK   3      S21:   0.7186 S22:   0.1031 S23:   0.5797                       
REMARK   3      S31:  -0.6046 S32:  -0.8347 S33:  -0.0630                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 54 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -32.0330 -20.1675   1.2502              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2343 T22:   0.2610                                     
REMARK   3      T33:   0.2849 T12:  -0.0993                                     
REMARK   3      T13:   0.0028 T23:  -0.0387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4493 L22:   1.0902                                     
REMARK   3      L33:   4.5148 L12:  -0.5108                                     
REMARK   3      L13:  -1.6105 L23:  -0.9250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0496 S12:  -0.0649 S13:  -0.0554                       
REMARK   3      S21:  -0.1106 S22:  -0.0035 S23:   0.0365                       
REMARK   3      S31:   0.4784 S32:   0.0974 S33:   0.0283                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 55 THROUGH 81 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -30.3750 -19.4487   0.0881              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1752 T22:   0.1896                                     
REMARK   3      T33:   0.1830 T12:  -0.0448                                     
REMARK   3      T13:   0.0258 T23:  -0.0344                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1748 L22:   2.2450                                     
REMARK   3      L33:   4.6404 L12:   0.0141                                     
REMARK   3      L13:   2.8799 L23:  -0.0411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0340 S12:   0.2152 S13:  -0.2331                       
REMARK   3      S21:  -0.1454 S22:   0.0693 S23:   0.1406                       
REMARK   3      S31:   0.3476 S32:  -0.1017 S33:  -0.0239                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 160 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6238  -4.3353   1.9636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1181 T22:   0.1955                                     
REMARK   3      T33:   0.1764 T12:  -0.0054                                     
REMARK   3      T13:  -0.0122 T23:  -0.0247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7242 L22:   1.5446                                     
REMARK   3      L33:   2.0876 L12:   0.1534                                     
REMARK   3      L13:  -0.0396 L23:  -0.5762                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0482 S12:   0.0862 S13:  -0.0045                       
REMARK   3      S21:  -0.0741 S22:   0.0710 S23:   0.1836                       
REMARK   3      S31:  -0.0353 S32:  -0.2902 S33:  -0.0492                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 252 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.6020   3.1810   3.7593              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1381 T22:   0.1496                                     
REMARK   3      T33:   0.1372 T12:   0.0074                                     
REMARK   3      T13:  -0.0060 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0332 L22:   2.0481                                     
REMARK   3      L33:   3.4687 L12:   0.4809                                     
REMARK   3      L13:  -0.4022 L23:  -1.1029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0072 S12:  -0.0843 S13:   0.0214                       
REMARK   3      S21:   0.0122 S22:  -0.1332 S23:  -0.1173                       
REMARK   3      S31:  -0.1753 S32:   0.2502 S33:   0.1289                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 253 THROUGH 297 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -23.0673  18.2442   2.8453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4654 T22:   0.1498                                     
REMARK   3      T33:   0.2700 T12:   0.0034                                     
REMARK   3      T13:  -0.0132 T23:  -0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7110 L22:   2.6766                                     
REMARK   3      L33:   4.1480 L12:   0.4257                                     
REMARK   3      L13:   0.3946 L23:  -0.9003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0254 S12:  -0.1078 S13:   0.4257                       
REMARK   3      S21:   0.2416 S22:  -0.0327 S23:  -0.0216                       
REMARK   3      S31:  -0.8948 S32:   0.0511 S33:   0.0344                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 298 THROUGH 316 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.4288   8.9881  -3.4718              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3161 T22:   0.4584                                     
REMARK   3      T33:   0.3992 T12:   0.1598                                     
REMARK   3      T13:  -0.0940 T23:   0.0370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6537 L22:   3.7999                                     
REMARK   3      L33:   2.3302 L12:   0.5658                                     
REMARK   3      L13:  -0.4887 L23:   1.5259                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0360 S12:   0.3050 S13:   0.1586                       
REMARK   3      S21:  -0.4321 S22:  -0.1082 S23:   0.7188                       
REMARK   3      S31:  -0.2927 S32:  -0.5961 S33:   0.0653                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 350 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.9659 -19.8060  -1.4227              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1852 T22:   0.2226                                     
REMARK   3      T33:   0.2447 T12:  -0.0589                                     
REMARK   3      T13:   0.0416 T23:  -0.0412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5497 L22:   4.2686                                     
REMARK   3      L33:   6.5301 L12:   0.0760                                     
REMARK   3      L13:   0.5981 L23:  -2.9106                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0011 S12:   0.1205 S13:  -0.1858                       
REMARK   3      S21:  -0.4654 S22:   0.0273 S23:  -0.0994                       
REMARK   3      S31:   0.7220 S32:  -0.0488 S33:  -0.1097                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 5 THROUGH 11 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -13.0525   8.1080 -16.0968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2188 T22:   0.2615                                     
REMARK   3      T33:   0.1840 T12:  -0.0273                                     
REMARK   3      T13:  -0.0140 T23:  -0.0255                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1304 L22:   8.2252                                     
REMARK   3      L33:   8.1515 L12:  -1.2933                                     
REMARK   3      L13:  -3.3026 L23:  -5.5255                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0446 S12:   0.0771 S13:  -0.0239                       
REMARK   3      S21:   0.0094 S22:  -0.2125 S23:   0.4215                       
REMARK   3      S31:  -0.3441 S32:   0.0914 S33:   0.2041                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 12 THROUGH 24 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0108  -3.8996  -4.1142              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3985 T22:   0.2366                                     
REMARK   3      T33:   0.2048 T12:   0.0574                                     
REMARK   3      T13:   0.0575 T23:   0.0397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9697 L22:   4.1866                                     
REMARK   3      L33:   0.9133 L12:   2.2219                                     
REMARK   3      L13:   0.3995 L23:  -0.0275                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3103 S12:  -0.6103 S13:  -0.5851                       
REMARK   3      S21:   0.5864 S22:  -0.0363 S23:  -0.3455                       
REMARK   3      S31:   0.9666 S32:   0.0174 S33:   0.2447                       
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 4WB5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203249.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54512                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.641                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.84600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 4WB8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 6000, 0.1M HEPES PH 7.5, VAPOR   
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.58900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.35800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.54550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.35800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.58900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.54550            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I                                  
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     ASN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLN A    12                                                      
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    ASP A 166       44.17   -149.32                                   
REMARK 500    ASP A 184       80.02     68.94                                   
REMARK 500    ASN A 216     -157.96   -140.93                                   
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 A 774        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH A 839        DISTANCE =  6.96 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 171   OD1                                                    
REMARK 620 2 ASP A 184   OD2  94.5                                              
REMARK 620 3 ATP A 401   O2G 107.1  87.6                                        
REMARK 620 4 ATP A 401   O3B 176.7  86.3  69.7                                  
REMARK 620 5 ATP A 401   O1A  93.3  91.8 159.6  89.9                            
REMARK 620 6 HOH A 691   O    87.8 177.3  90.3  91.3  89.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 184   OD1                                                    
REMARK 620 2 ASP A 184   OD2  58.5                                              
REMARK 620 3 ATP A 401   O3G 150.2  91.8                                        
REMARK 620 4 ATP A 401   O2B  87.1  87.2  94.6                                  
REMARK 620 5 HOH A 577   O    82.7  90.2  95.9 169.3                            
REMARK 620 6 HOH A 580   O   101.6 160.1 108.0  91.0  87.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WB6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WB7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WB8   RELATED DB: PDB                                   
DBREF  4WB5 A    1   350  UNP    P17612   KAPCA_HUMAN      2    351             
DBREF  4WB5 I    5    24  PDB    4WB5     4WB5             5     24             
SEQRES   1 A  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 A  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 A  350  LEU LYS LYS TRP GLU SER PRO ALA GLN ASN THR ALA HIS          
SEQRES   4 A  350  LEU ASP GLN PHE GLU ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 A  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU THR          
SEQRES   6 A  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 A  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 A  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 A  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 A  350  MET VAL MET GLU TYR VAL PRO GLY GLY GLU MET PHE SER          
SEQRES  11 A  350  HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA          
SEQRES  12 A  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 A  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 A  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 A  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 A  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 A  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 A  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 A  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 A  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 A  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 A  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 A  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 A  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 A  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 A  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 A  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE SER GLU PHE              
SEQRES   1 I   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 I   20  ARG ARG ASN ALA ILE HIS ASP                                  
MODRES 4WB5 SEP A  139  SER  MODIFIED RESIDUE                                   
MODRES 4WB5 TPO A  197  THR  MODIFIED RESIDUE                                   
MODRES 4WB5 SEP A  338  SER  MODIFIED RESIDUE                                   
HET    SEP  A 139      10                                                       
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    ATP  A 401      31                                                       
HET     MG  A 402       1                                                       
HET     MG  A 403       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  ATP    C10 H16 N5 O13 P3                                            
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  HOH   *405(H2 O)                                                    
HELIX    1 AA1 GLU A   13  SER A   32  1                                  20    
HELIX    2 AA2 HIS A   39  ASP A   41  5                                   3    
HELIX    3 AA3 LYS A   76  LEU A   82  1                                   7    
HELIX    4 AA4 GLN A   84  GLN A   96  1                                  13    
HELIX    5 AA5 GLU A  127  GLY A  136  1                                  10    
HELIX    6 AA6 SEP A  139  LEU A  160  1                                  22    
HELIX    7 AA7 LYS A  168  GLU A  170  5                                   3    
HELIX    8 AA8 THR A  201  LEU A  205  5                                   5    
HELIX    9 AA9 ALA A  206  LEU A  211  1                                   6    
HELIX   10 AB1 LYS A  217  GLY A  234  1                                  18    
HELIX   11 AB2 GLN A  242  GLY A  253  1                                  12    
HELIX   12 AB3 SER A  262  LEU A  273  1                                  12    
HELIX   13 AB4 VAL A  288  ASN A  293  1                                   6    
HELIX   14 AB5 HIS A  294  ALA A  298  5                                   5    
HELIX   15 AB6 ASP A  301  GLN A  307  1                                   7    
HELIX   16 AB7 THR I    6  ALA I   12  1                                   7    
SHEET    1 AA1 5 PHE A  43  THR A  51  0                                        
SHEET    2 AA1 5 ARG A  56  HIS A  62 -1  O  LEU A  59   N  LYS A  47           
SHEET    3 AA1 5 HIS A  68  ASP A  75 -1  O  MET A  71   N  MET A  58           
SHEET    4 AA1 5 ASN A 115  GLU A 121 -1  O  MET A 120   N  ALA A  70           
SHEET    5 AA1 5 LEU A 106  LYS A 111 -1  N  PHE A 108   O  VAL A 119           
SHEET    1 AA2 2 LEU A 162  ILE A 163  0                                        
SHEET    2 AA2 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1 AA3 2 LEU A 172  ILE A 174  0                                        
SHEET    2 AA3 2 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
LINK         C   PHE A 138                 N   SEP A 139     1555   1555  1.34  
LINK         C   SEP A 139                 N   GLU A 140     1555   1555  1.33  
LINK         OD1 ASN A 171                MG    MG A 402     1555   1555  2.09  
LINK         OD1 ASP A 184                MG    MG A 403     1555   1555  2.27  
LINK         OD2 ASP A 184                MG    MG A 402     1555   1555  2.07  
LINK         OD2 ASP A 184                MG    MG A 403     1555   1555  2.25  
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.34  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.33  
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.33  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
LINK         O2G ATP A 401                MG    MG A 402     1555   1555  2.05  
LINK         O3G ATP A 401                MG    MG A 403     1555   1555  1.93  
LINK         O2B ATP A 401                MG    MG A 403     1555   1555  2.12  
LINK         O3B ATP A 401                MG    MG A 402     1555   1555  2.31  
LINK         O1A ATP A 401                MG    MG A 402     1555   1555  1.95  
LINK        MG    MG A 402                 O   HOH A 691     1555   1555  2.12  
LINK        MG    MG A 403                 O   HOH A 577     1555   1555  2.19  
LINK        MG    MG A 403                 O   HOH A 580     1555   1555  1.99  
SITE     1 AC1 29 GLY A  52  SER A  53  PHE A  54  GLY A  55                    
SITE     2 AC1 29 VAL A  57  ALA A  70  LYS A  72  VAL A 104                    
SITE     3 AC1 29 MET A 120  GLU A 121  VAL A 123  GLU A 127                    
SITE     4 AC1 29 ASP A 166  LYS A 168  GLU A 170  ASN A 171                    
SITE     5 AC1 29 LEU A 173  THR A 183  ASP A 184  PHE A 327                    
SITE     6 AC1 29  MG A 402   MG A 403  HOH A 577  HOH A 580                    
SITE     7 AC1 29 HOH A 653  HOH A 691  HOH A 843  ARG I  18                    
SITE     8 AC1 29 ALA I  21                                                     
SITE     1 AC2  4 ASN A 171  ASP A 184  ATP A 401  HOH A 691                    
SITE     1 AC3  4 ASP A 184  ATP A 401  HOH A 577  HOH A 580                    
CRYST1   73.178   75.091   80.716  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      0.013665  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013317  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012389        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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