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Database: PDB
Entry: 3NZS
LinkDB: 3NZS
Original site: 3NZS 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       16-JUL-10   3NZS              
TITLE     STRUCTURE-BASED OPTIMIZATION OF PYRAZOLO -PYRIMIDINE AND -PYRIDINE    
TITLE    2 INHIBITORS OF PI3-KINASE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT GAMMA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PTDINS-3-KINASE SUBUNIT GAMMA, PI3-KINASE SUBUNIT GAMMA,    
COMPND   6 PI3K-GAMMA, PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE 110 KDA   
COMPND   7 CATALYTIC SUBUNIT GAMMA, PTDINS-3-KINASE SUBUNIT P110-GAMMA, P120-   
COMPND   8 PI3K;                                                                
COMPND   9 EC: 2.7.1.153;                                                       
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: PIK3CG;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    KINASE P110, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.MURRAY,C.WIESMANN                                                 
REVDAT   1   29-DEC-10 3NZS    0                                                
JRNL        AUTH   S.T.STABEN,T.P.HEFFRON,D.P.SUTHERLIN,S.R.BHAT,G.M.CASTANEDO, 
JRNL        AUTH 2 I.S.CHUCKOWREE,J.DOTSON,A.J.FOLKES,L.S.FRIEDMAN,L.LEE,       
JRNL        AUTH 3 J.LESNICK,C.LEWIS,J.M.MURRAY,J.NONOMIYA,A.G.OLIVERO,E.PLISE, 
JRNL        AUTH 4 J.PANG,W.W.PRIOR,L.SALPHATI,L.ROUGE,D.SAMPATH,V.TSUI,        
JRNL        AUTH 5 N.C.WAN,S.WANG,C.WIESMANN,P.WU,B.Y.ZHU                       
JRNL        TITL   STRUCTURE-BASED OPTIMIZATION OF PYRAZOLO-PYRIMIDINE AND      
JRNL        TITL 2 -PYRIDINE INHIBITORS OF PI3-KINASE.                          
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  20  6048 2010              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   20822905                                                     
JRNL        DOI    10.1016/J.BMCL.2010.08.067                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_392)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 26966                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1363                            
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 19.9734 -  5.8797    1.00     2660   133  0.1955 0.2025        
REMARK   3     2  5.8797 -  4.6867    1.00     2588   144  0.1936 0.2329        
REMARK   3     3  4.6867 -  4.1001    1.00     2563   153  0.1613 0.2049        
REMARK   3     4  4.1001 -  3.7279    1.00     2600   127  0.1944 0.2145        
REMARK   3     5  3.7279 -  3.4622    1.00     2522   155  0.2180 0.2795        
REMARK   3     6  3.4622 -  3.2590    1.00     2597   114  0.2297 0.2610        
REMARK   3     7  3.2590 -  3.0964    1.00     2535   148  0.2571 0.2910        
REMARK   3     8  3.0964 -  2.9620    1.00     2536   134  0.2876 0.3676        
REMARK   3     9  2.9620 -  2.8483    0.99     2574   116  0.3237 0.4105        
REMARK   3    10  2.8483 -  2.7503    0.95     2428   139  0.3485 0.3732        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.06                                          
REMARK   3   K_SOL              : 0.29                                          
REMARK   3   B_SOL              : 59.26                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 98.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.32960                                              
REMARK   3    B22 (A**2) : -4.27030                                             
REMARK   3    B33 (A**2) : -0.05930                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.27020                                              
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      :  0.001           6898                                  
REMARK   3   ANGLE     :  0.499           9340                                  
REMARK   3   CHIRALITY :  0.035           1055                                  
REMARK   3   PLANARITY :  0.002           1179                                  
REMARK   3   DIHEDRAL  : 10.813           2561                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 144:190)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  37.6804 -18.9354  11.6009              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3859 T22:   0.7812                                     
REMARK   3      T33:   0.8566 T12:   0.1965                                     
REMARK   3      T13:  -0.1589 T23:  -0.5481                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8604 L22:   1.4369                                     
REMARK   3      L33:   1.8802 L12:   0.1901                                     
REMARK   3      L13:   2.2672 L23:   0.6008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1105 S12:   1.7519 S13:  -1.7513                       
REMARK   3      S21:  -0.3054 S22:   0.1965 S23:  -0.2968                       
REMARK   3      S31:   0.3723 S32:   0.6192 S33:  -0.3856                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 191:321)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  10.4620 -11.8498  36.3181              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3533 T22:   0.9544                                     
REMARK   3      T33:   0.9901 T12:   0.0383                                     
REMARK   3      T13:   0.2204 T23:   0.5555                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0430 L22:   1.3852                                     
REMARK   3      L33:   2.6952 L12:  -1.3026                                     
REMARK   3      L13:   0.6153 L23:   0.4522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1451 S12:  -0.8303 S13:  -1.3368                       
REMARK   3      S21:   0.3122 S22:   0.2729 S23:   0.8197                       
REMARK   3      S31:   0.1464 S32:  -1.3994 S33:  -0.5340                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 350:488)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  63.9138  -5.2603  13.9273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2172 T22:   1.6802                                     
REMARK   3      T33:   0.2140 T12:   0.0514                                     
REMARK   3      T13:   0.0431 T23:  -0.2023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6895 L22:   1.9788                                     
REMARK   3      L33:   6.0994 L12:   0.2329                                     
REMARK   3      L13:   2.5005 L23:  -1.7153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0607 S12:   1.6959 S13:  -0.4960                       
REMARK   3      S21:  -0.1309 S22:  -0.2794 S23:  -0.3850                       
REMARK   3      S31:  -0.1629 S32:   2.8796 S33:   0.0529                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 495:533)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  55.4018  -6.4034  12.4076              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4488 T22:   1.1706                                     
REMARK   3      T33:   0.1668 T12:   0.2543                                     
REMARK   3      T13:   0.0956 T23:  -0.2866                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6810 L22:   0.9360                                     
REMARK   3      L33:   0.9089 L12:   0.3938                                     
REMARK   3      L13:   1.3598 L23:  -0.0229                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1952 S12:   1.7722 S13:  -0.2247                       
REMARK   3      S21:  -0.3704 S22:  -0.2346 S23:  -0.0790                       
REMARK   3      S31:  -0.0348 S32:   1.3717 S33:  -0.2292                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 544:725)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  46.1045 -10.4599  34.1653              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2502 T22:   0.1267                                     
REMARK   3      T33:   0.2712 T12:   0.0116                                     
REMARK   3      T13:  -0.0021 T23:   0.0290                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2653 L22:   0.8449                                     
REMARK   3      L33:   4.2047 L12:  -1.1050                                     
REMARK   3      L13:   2.8878 L23:  -0.1560                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2165 S12:  -0.1708 S13:  -0.9280                       
REMARK   3      S21:   0.1001 S22:   0.1927 S23:   0.2059                       
REMARK   3      S31:   0.0100 S32:   0.2191 S33:  -0.3225                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 726:836)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6179   4.4422  11.7125              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4309 T22:   0.8153                                     
REMARK   3      T33:   0.4120 T12:   0.2921                                     
REMARK   3      T13:  -0.0764 T23:   0.1556                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5168 L22:   2.5684                                     
REMARK   3      L33:   0.6833 L12:  -2.0481                                     
REMARK   3      L13:   0.1426 L23:   0.4162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3927 S12:   1.4114 S13:  -0.4824                       
REMARK   3      S21:  -0.5575 S22:  -0.3280 S23:   0.7484                       
REMARK   3      S31:  -0.2094 S32:  -0.7569 S33:  -0.2230                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 837:866)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1981   4.7346  34.7520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9813 T22:   0.3501                                     
REMARK   3      T33:   0.3993 T12:   0.2554                                     
REMARK   3      T13:   0.2433 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6322 L22:   0.9982                                     
REMARK   3      L33:   0.4195 L12:  -0.4412                                     
REMARK   3      L13:   0.7194 L23:   0.0124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4090 S12:   0.1828 S13:   0.5641                       
REMARK   3      S21:   1.2807 S22:   0.2210 S23:   0.1954                       
REMARK   3      S31:  -0.6299 S32:  -0.6412 S33:   0.1287                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 867:881)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5466   5.0082  18.4762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4830 T22:   0.6596                                     
REMARK   3      T33:   0.4015 T12:   0.1911                                     
REMARK   3      T13:   0.0368 T23:   0.1086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0107 L22:   3.5163                                     
REMARK   3      L33:   0.2122 L12:  -0.9573                                     
REMARK   3      L13:   0.6103 L23:  -0.7234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0986 S12:   1.2253 S13:   1.1494                       
REMARK   3      S21:   0.9512 S22:  -0.1367 S23:  -0.3456                       
REMARK   3      S31:  -0.4321 S32:   0.2890 S33:   0.1189                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 882:1090)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1894  18.8819  36.8850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0139 T22:   0.2175                                     
REMARK   3      T33:   0.6814 T12:   0.2584                                     
REMARK   3      T13:  -0.0752 T23:  -0.1211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8240 L22:   2.5785                                     
REMARK   3      L33:   1.3345 L12:  -0.7488                                     
REMARK   3      L13:   0.8783 L23:  -0.6350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7816 S12:  -0.4755 S13:   2.0755                       
REMARK   3      S21:   1.3076 S22:   0.2509 S23:  -0.0503                       
REMARK   3      S31:  -0.7780 S32:  -0.1737 S33:   0.3378                       
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 3NZS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060484.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUL-07; 10-APR-08               
REMARK 200  TEMPERATURE           (KELVIN) : NULL; NULL                         
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ALS; ALS                           
REMARK 200  BEAMLINE                       : 5.0.1; 5.0.1                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL; NULL                         
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0; 1.0                           
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC QUANTUM     
REMARK 200                                   315                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27142                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.660                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE; SINGLE                                 
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, 0.2M NH4SO4, 0.1M TRIS-HCL     
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       72.48300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.98250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       72.48300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.98250            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     LYS A   251                                                      
REMARK 465     MET A   252                                                      
REMARK 465     ALA A   253                                                      
REMARK 465     LYS A   254                                                      
REMARK 465     LYS A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     SER A   257                                                      
REMARK 465     LEU A   258                                                      
REMARK 465     MET A   259                                                      
REMARK 465     ASP A   260                                                      
REMARK 465     ILE A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     GLU A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     GLN A   265                                                      
REMARK 465     SER A   266                                                      
REMARK 465     GLU A   267                                                      
REMARK 465     GLN A   268                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     TRP A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     LEU A   325                                                      
REMARK 465     VAL A   326                                                      
REMARK 465     ASP A   327                                                      
REMARK 465     ASP A   328                                                      
REMARK 465     CYS A   329                                                      
REMARK 465     THR A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     VAL A   332                                                      
REMARK 465     THR A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     TYR A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     GLN A   338                                                      
REMARK 465     LEU A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     ASP A   345                                                      
REMARK 465     HIS A   346                                                      
REMARK 465     GLU A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     VAL A   349                                                      
REMARK 465     PHE A   350                                                      
REMARK 465     THR A   351                                                      
REMARK 465     VAL A   352                                                      
REMARK 465     GLY A   436                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     ALA A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 465     ALA A   440                                                      
REMARK 465     LEU A   441                                                      
REMARK 465     SER A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     ALA A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     ALA A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     SER A   449                                                      
REMARK 465     PRO A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     SER A   452                                                      
REMARK 465     GLU A   453                                                      
REMARK 465     SER A   454                                                      
REMARK 465     LYS A   455                                                      
REMARK 465     GLY A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     VAL A   458                                                      
REMARK 465     SER A   488                                                      
REMARK 465     GLY A   489                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     GLY A   491                                                      
REMARK 465     GLU A   492                                                      
REMARK 465     ASP A   493                                                      
REMARK 465     GLN A   494                                                      
REMARK 465     GLY A   495                                                      
REMARK 465     ASN A   522                                                      
REMARK 465     TYR A   523                                                      
REMARK 465     CYS A   524                                                      
REMARK 465     HIS A   525                                                      
REMARK 465     PRO A   526                                                      
REMARK 465     ILE A   527                                                      
REMARK 465     HIS A   532                                                      
REMARK 465     GLN A   533                                                      
REMARK 465     PRO A   534                                                      
REMARK 465     THR A   535                                                      
REMARK 465     PRO A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     PRO A   538                                                      
REMARK 465     GLU A   539                                                      
REMARK 465     GLY A   540                                                      
REMARK 465     ASP A   541                                                      
REMARK 465     ARG A   542                                                      
REMARK 465     VAL A   543                                                      
REMARK 465     ARG A   544                                                      
REMARK 465     ALA A   545                                                      
REMARK 465     SER A   753                                                      
REMARK 465     ALA A   754                                                      
REMARK 465     GLU A   755                                                      
REMARK 465     LYS A   756                                                      
REMARK 465     LEU A   969                                                      
REMARK 465     GLY A   970                                                      
REMARK 465     ASN A   971                                                      
REMARK 465     TYR A   972                                                      
REMARK 465     LYS A   973                                                      
REMARK 465     SER A   974                                                      
REMARK 465     PHE A   975                                                      
REMARK 465     LEU A   976                                                      
REMARK 465     GLY A   977                                                      
REMARK 465     ILE A   978                                                      
REMARK 465     ASN A   979                                                      
REMARK 465     LYS A   980                                                      
REMARK 465     GLU A   981                                                      
REMARK 465     GLY A  1093                                                      
REMARK 465     ILE A  1094                                                      
REMARK 465     HIS A  1095                                                      
REMARK 465     HIS A  1096                                                      
REMARK 465     HIS A  1097                                                      
REMARK 465     HIS A  1098                                                      
REMARK 465     HIS A  1099                                                      
REMARK 465     HIS A  1100                                                      
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     SER A 496    OG                                                  
REMARK 470     TYR A 757    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A1000    CG   CD   CE   NZ                                   
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ARG A  375                                                       
REMARK 475     ASN A  376                                                       
REMARK 475     THR A  377                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  602   CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 916   C   -  N   -  CD  ANGL. DEV. = -28.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 167       56.14   -112.88                                   
REMARK 500    HIS A 199       58.69     38.99                                   
REMARK 500    ALA A 216      -76.51    -88.09                                   
REMARK 500    SER A 227      -79.04   -148.76                                   
REMARK 500    SER A 230      145.81   -176.26                                   
REMARK 500    ASP A 278       56.27    -90.90                                   
REMARK 500    PRO A 374      152.31    -48.52                                   
REMARK 500    ARG A 375       20.94    -74.99                                   
REMARK 500    HIS A 389       94.47   -161.52                                   
REMARK 500    GLN A 391       16.64     56.29                                   
REMARK 500    ASP A 509       92.60    -67.73                                   
REMARK 500    PRO A 530     -172.56    -63.87                                   
REMARK 500    ARG A 613       45.81   -107.25                                   
REMARK 500    SER A 760      179.61    -59.10                                   
REMARK 500    ASP A 788       80.03   -161.22                                   
REMARK 500    ALA A 797       75.97   -106.85                                   
REMARK 500    LEU A 823      -74.85    -77.15                                   
REMARK 500    PRO A 916      -77.06    -85.39                                   
REMARK 500    ASN A 949        8.91    -67.95                                   
REMARK 500    PHE A 961      143.19   -170.22                                   
REMARK 500    LEU A1042       76.35   -115.28                                   
REMARK 500    THR A1043       49.62   -140.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NZS A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3NZU   RELATED DB: PDB                                   
DBREF  3NZS A  147  1094  UNP    P48736   PK3CG_HUMAN    147   1094             
SEQADV 3NZS HIS A 1095  UNP  P48736              EXPRESSION TAG                 
SEQADV 3NZS HIS A 1096  UNP  P48736              EXPRESSION TAG                 
SEQADV 3NZS HIS A 1097  UNP  P48736              EXPRESSION TAG                 
SEQADV 3NZS HIS A 1098  UNP  P48736              EXPRESSION TAG                 
SEQADV 3NZS HIS A 1099  UNP  P48736              EXPRESSION TAG                 
SEQADV 3NZS HIS A 1100  UNP  P48736              EXPRESSION TAG                 
SEQRES   1 A  954  SER GLN ALA PHE GLN ARG GLN LEU THR ALA LEU ILE GLY          
SEQRES   2 A  954  TYR ASP VAL THR ASP VAL SER ASN VAL HIS ASP ASP GLU          
SEQRES   3 A  954  LEU GLU PHE THR ARG ARG GLY LEU VAL THR PRO ARG MET          
SEQRES   4 A  954  ALA GLU VAL ALA SER ARG ASP PRO LYS LEU TYR ALA MET          
SEQRES   5 A  954  HIS PRO TRP VAL THR SER LYS PRO LEU PRO GLU TYR LEU          
SEQRES   6 A  954  TRP LYS LYS ILE ALA ASN ASN CYS ILE PHE ILE VAL ILE          
SEQRES   7 A  954  HIS ARG SER THR THR SER GLN THR ILE LYS VAL SER PRO          
SEQRES   8 A  954  ASP ASP THR PRO GLY ALA ILE LEU GLN SER PHE PHE THR          
SEQRES   9 A  954  LYS MET ALA LYS LYS LYS SER LEU MET ASP ILE PRO GLU          
SEQRES  10 A  954  SER GLN SER GLU GLN ASP PHE VAL LEU ARG VAL CYS GLY          
SEQRES  11 A  954  ARG ASP GLU TYR LEU VAL GLY GLU THR PRO ILE LYS ASN          
SEQRES  12 A  954  PHE GLN TRP VAL ARG HIS CYS LEU LYS ASN GLY GLU GLU          
SEQRES  13 A  954  ILE HIS VAL VAL LEU ASP THR PRO PRO ASP PRO ALA LEU          
SEQRES  14 A  954  ASP GLU VAL ARG LYS GLU GLU TRP PRO LEU VAL ASP ASP          
SEQRES  15 A  954  CYS THR GLY VAL THR GLY TYR HIS GLU GLN LEU THR ILE          
SEQRES  16 A  954  HIS GLY LYS ASP HIS GLU SER VAL PHE THR VAL SER LEU          
SEQRES  17 A  954  TRP ASP CYS ASP ARG LYS PHE ARG VAL LYS ILE ARG GLY          
SEQRES  18 A  954  ILE ASP ILE PRO VAL LEU PRO ARG ASN THR ASP LEU THR          
SEQRES  19 A  954  VAL PHE VAL GLU ALA ASN ILE GLN HIS GLY GLN GLN VAL          
SEQRES  20 A  954  LEU CYS GLN ARG ARG THR SER PRO LYS PRO PHE THR GLU          
SEQRES  21 A  954  GLU VAL LEU TRP ASN VAL TRP LEU GLU PHE SER ILE LYS          
SEQRES  22 A  954  ILE LYS ASP LEU PRO LYS GLY ALA LEU LEU ASN LEU GLN          
SEQRES  23 A  954  ILE TYR CYS GLY LYS ALA PRO ALA LEU SER SER LYS ALA          
SEQRES  24 A  954  SER ALA GLU SER PRO SER SER GLU SER LYS GLY LYS VAL          
SEQRES  25 A  954  GLN LEU LEU TYR TYR VAL ASN LEU LEU LEU ILE ASP HIS          
SEQRES  26 A  954  ARG PHE LEU LEU ARG ARG GLY GLU TYR VAL LEU HIS MET          
SEQRES  27 A  954  TRP GLN ILE SER GLY LYS GLY GLU ASP GLN GLY SER PHE          
SEQRES  28 A  954  ASN ALA ASP LYS LEU THR SER ALA THR ASN PRO ASP LYS          
SEQRES  29 A  954  GLU ASN SER MET SER ILE SER ILE LEU LEU ASP ASN TYR          
SEQRES  30 A  954  CYS HIS PRO ILE ALA LEU PRO LYS HIS GLN PRO THR PRO          
SEQRES  31 A  954  ASP PRO GLU GLY ASP ARG VAL ARG ALA GLU MET PRO ASN          
SEQRES  32 A  954  GLN LEU ARG LYS GLN LEU GLU ALA ILE ILE ALA THR ASP          
SEQRES  33 A  954  PRO LEU ASN PRO LEU THR ALA GLU ASP LYS GLU LEU LEU          
SEQRES  34 A  954  TRP HIS PHE ARG TYR GLU SER LEU LYS HIS PRO LYS ALA          
SEQRES  35 A  954  TYR PRO LYS LEU PHE SER SER VAL LYS TRP GLY GLN GLN          
SEQRES  36 A  954  GLU ILE VAL ALA LYS THR TYR GLN LEU LEU ALA ARG ARG          
SEQRES  37 A  954  GLU VAL TRP ASP GLN SER ALA LEU ASP VAL GLY LEU THR          
SEQRES  38 A  954  MET GLN LEU LEU ASP CYS ASN PHE SER ASP GLU ASN VAL          
SEQRES  39 A  954  ARG ALA ILE ALA VAL GLN LYS LEU GLU SER LEU GLU ASP          
SEQRES  40 A  954  ASP ASP VAL LEU HIS TYR LEU LEU GLN LEU VAL GLN ALA          
SEQRES  41 A  954  VAL LYS PHE GLU PRO TYR HIS ASP SER ALA LEU ALA ARG          
SEQRES  42 A  954  PHE LEU LEU LYS ARG GLY LEU ARG ASN LYS ARG ILE GLY          
SEQRES  43 A  954  HIS PHE LEU PHE TRP PHE LEU ARG SER GLU ILE ALA GLN          
SEQRES  44 A  954  SER ARG HIS TYR GLN GLN ARG PHE ALA VAL ILE LEU GLU          
SEQRES  45 A  954  ALA TYR LEU ARG GLY CYS GLY THR ALA MET LEU HIS ASP          
SEQRES  46 A  954  PHE THR GLN GLN VAL GLN VAL ILE GLU MET LEU GLN LYS          
SEQRES  47 A  954  VAL THR LEU ASP ILE LYS SER LEU SER ALA GLU LYS TYR          
SEQRES  48 A  954  ASP VAL SER SER GLN VAL ILE SER GLN LEU LYS GLN LYS          
SEQRES  49 A  954  LEU GLU ASN LEU GLN ASN SER GLN LEU PRO GLU SER PHE          
SEQRES  50 A  954  ARG VAL PRO TYR ASP PRO GLY LEU LYS ALA GLY ALA LEU          
SEQRES  51 A  954  ALA ILE GLU LYS CYS LYS VAL MET ALA SER LYS LYS LYS          
SEQRES  52 A  954  PRO LEU TRP LEU GLU PHE LYS CYS ALA ASP PRO THR ALA          
SEQRES  53 A  954  LEU SER ASN GLU THR ILE GLY ILE ILE PHE LYS HIS GLY          
SEQRES  54 A  954  ASP ASP LEU ARG GLN ASP MET LEU ILE LEU GLN ILE LEU          
SEQRES  55 A  954  ARG ILE MET GLU SER ILE TRP GLU THR GLU SER LEU ASP          
SEQRES  56 A  954  LEU CYS LEU LEU PRO TYR GLY CYS ILE SER THR GLY ASP          
SEQRES  57 A  954  LYS ILE GLY MET ILE GLU ILE VAL LYS ASP ALA THR THR          
SEQRES  58 A  954  ILE ALA LYS ILE GLN GLN SER THR VAL GLY ASN THR GLY          
SEQRES  59 A  954  ALA PHE LYS ASP GLU VAL LEU ASN HIS TRP LEU LYS GLU          
SEQRES  60 A  954  LYS SER PRO THR GLU GLU LYS PHE GLN ALA ALA VAL GLU          
SEQRES  61 A  954  ARG PHE VAL TYR SER CYS ALA GLY TYR CYS VAL ALA THR          
SEQRES  62 A  954  PHE VAL LEU GLY ILE GLY ASP ARG HIS ASN ASP ASN ILE          
SEQRES  63 A  954  MET ILE THR GLU THR GLY ASN LEU PHE HIS ILE ASP PHE          
SEQRES  64 A  954  GLY HIS ILE LEU GLY ASN TYR LYS SER PHE LEU GLY ILE          
SEQRES  65 A  954  ASN LYS GLU ARG VAL PRO PHE VAL LEU THR PRO ASP PHE          
SEQRES  66 A  954  LEU PHE VAL MET GLY THR SER GLY LYS LYS THR SER PRO          
SEQRES  67 A  954  HIS PHE GLN LYS PHE GLN ASP ILE CYS VAL LYS ALA TYR          
SEQRES  68 A  954  LEU ALA LEU ARG HIS HIS THR ASN LEU LEU ILE ILE LEU          
SEQRES  69 A  954  PHE SER MET MET LEU MET THR GLY MET PRO GLN LEU THR          
SEQRES  70 A  954  SER LYS GLU ASP ILE GLU TYR ILE ARG ASP ALA LEU THR          
SEQRES  71 A  954  VAL GLY LYS ASN GLU GLU ASP ALA LYS LYS TYR PHE LEU          
SEQRES  72 A  954  ASP GLN ILE GLU VAL CYS ARG ASP LYS GLY TRP THR VAL          
SEQRES  73 A  954  GLN PHE ASN TRP PHE LEU HIS LEU VAL LEU GLY ILE HIS          
SEQRES  74 A  954  HIS HIS HIS HIS HIS                                          
HET    NZS  A   1      27                                                       
HETNAM     NZS 6-(1,1-DIOXIDOTHIOMORPHOLIN-4-YL)-N-(3-METHOXYPHENYL)-           
HETNAM   2 NZS  1-METHYL-1H-PYRAZOLO[3,4-D]PYRIMIDIN-4-AMINE                    
FORMUL   2  NZS    C17 H20 N6 O3 S                                              
HELIX    1   1 SER A  147  GLY A  159  1                                  13    
HELIX    2   2 ASP A  171  LEU A  180  1                                  10    
HELIX    3   3 LEU A  180  ALA A  189  1                                  10    
HELIX    4   4 ASP A  192  HIS A  199  1                                   8    
HELIX    5   5 PRO A  208  LYS A  213  1                                   6    
HELIX    6   6 THR A  240  THR A  250  1                                  11    
HELIX    7   7 PRO A  286  ASN A  289  5                                   4    
HELIX    8   8 PHE A  290  ASN A  299  1                                  10    
HELIX    9   9 ASP A  312  GLU A  317  5                                   6    
HELIX   10  10 SER A  353  CYS A  357  5                                   5    
HELIX   11  11 ASN A  498  THR A  503  5                                   6    
HELIX   12  12 PRO A  548  THR A  561  1                                  14    
HELIX   13  13 THR A  568  PHE A  578  1                                  11    
HELIX   14  14 PHE A  578  LEU A  583  1                                   6    
HELIX   15  15 LYS A  584  LYS A  587  5                                   4    
HELIX   16  16 ALA A  588  PHE A  593  1                                   6    
HELIX   17  17 GLN A  600  ALA A  612  1                                  13    
HELIX   18  18 GLU A  615  SER A  620  1                                   6    
HELIX   19  19 ASP A  623  LEU A  630  1                                   8    
HELIX   20  20 ASP A  637  GLU A  649  1                                  13    
HELIX   21  21 GLU A  652  ALA A  666  1                                  15    
HELIX   22  22 VAL A  667  GLU A  670  5                                   4    
HELIX   23  23 SER A  675  ASN A  688  1                                  14    
HELIX   24  24 ASN A  688  SER A  706  1                                  19    
HELIX   25  25 TYR A  709  ARG A  722  1                                  14    
HELIX   26  26 GLY A  725  LEU A  752  1                                  28    
HELIX   27  27 SER A  760  ASN A  776  1                                  17    
HELIX   28  28 ASP A  837  GLU A  858  1                                  22    
HELIX   29  29 ILE A  888  VAL A  896  1                                   9    
HELIX   30  30 GLU A  905  SER A  915  1                                  11    
HELIX   31  31 THR A  917  LEU A  942  1                                  26    
HELIX   32  32 THR A  988  MET A  995  1                                   8    
HELIX   33  33 HIS A 1005  ARG A 1021  1                                  17    
HELIX   34  34 HIS A 1023  MET A 1039  1                                  17    
HELIX   35  35 SER A 1044  GLU A 1049  1                                   6    
HELIX   36  36 GLU A 1049  LEU A 1055  1                                   7    
HELIX   37  37 ASN A 1060  GLY A 1079  1                                  20    
HELIX   38  38 TRP A 1080  LEU A 1090  1                                  11    
SHEET    1   A 3 SER A 230  GLN A 231  0                                        
SHEET    2   A 3 ILE A 220  HIS A 225 -1  N  ILE A 224   O  GLN A 231           
SHEET    3   A 3 LYS A 234  VAL A 235 -1  O  VAL A 235   N  ILE A 220           
SHEET    1   B 4 SER A 230  GLN A 231  0                                        
SHEET    2   B 4 ILE A 220  HIS A 225 -1  N  ILE A 224   O  GLN A 231           
SHEET    3   B 4 ILE A 303  ASP A 308  1  O  LEU A 307   N  HIS A 225           
SHEET    4   B 4 VAL A 271  VAL A 274 -1  N  ARG A 273   O  VAL A 306           
SHEET    1   C 4 GLU A 407  LYS A 419  0                                        
SHEET    2   C 4 LYS A 360  ASP A 369 -1  N  ILE A 365   O  VAL A 412           
SHEET    3   C 4 SER A 515  LEU A 520 -1  O  SER A 515   N  ASP A 369           
SHEET    4   C 4 GLY A 478  HIS A 483 -1  N  GLY A 478   O  LEU A 520           
SHEET    1   D 3 VAL A 393  ARG A 398  0                                        
SHEET    2   D 3 THR A 380  GLN A 388 -1  N  ILE A 387   O  LEU A 394           
SHEET    3   D 3 LYS A 402  PRO A 403 -1  O  LYS A 402   N  VAL A 381           
SHEET    1   E 5 VAL A 393  ARG A 398  0                                        
SHEET    2   E 5 THR A 380  GLN A 388 -1  N  ILE A 387   O  LEU A 394           
SHEET    3   E 5 LEU A 428  TYR A 434 -1  O  GLN A 432   N  GLU A 384           
SHEET    4   E 5 TYR A 462  LEU A 467 -1  O  VAL A 464   N  LEU A 431           
SHEET    5   E 5 TRP A 485  GLN A 486 -1  O  TRP A 485   N  TYR A 463           
SHEET    1   F 4 PHE A 783  VAL A 785  0                                        
SHEET    2   F 4 ASP A 788  LEU A 796 -1  O  ALA A 793   N  PHE A 783           
SHEET    3   F 4 LEU A 811  CYS A 817 -1  O  LYS A 816   N  GLY A 794           
SHEET    4   F 4 LYS A 802  VAL A 803 -1  N  LYS A 802   O  TRP A 812           
SHEET    1   G 6 PHE A 783  VAL A 785  0                                        
SHEET    2   G 6 ASP A 788  LEU A 796 -1  O  ALA A 793   N  PHE A 783           
SHEET    3   G 6 LEU A 811  CYS A 817 -1  O  LYS A 816   N  GLY A 794           
SHEET    4   G 6 ILE A 828  HIS A 834 -1  O  PHE A 832   N  LEU A 811           
SHEET    5   G 6 ILE A 876  GLU A 880 -1  O  ILE A 879   N  ILE A 831           
SHEET    6   G 6 CYS A 869  GLY A 873 -1  N  ILE A 870   O  MET A 878           
SHEET    1   H 3 ALA A 885  THR A 887  0                                        
SHEET    2   H 3 ILE A 952  THR A 955 -1  O  ILE A 954   N  THR A 886           
SHEET    3   H 3 LEU A 960  HIS A 962 -1  O  PHE A 961   N  MET A 953           
CISPEP   1 THR A  377    ASP A  378          0        -1.12                     
SITE     1 AC1 11 MET A 804  ILE A 831  LYS A 833  TYR A 867                    
SITE     2 AC1 11 GLU A 880  ILE A 881  VAL A 882  THR A 887                    
SITE     3 AC1 11 LYS A 890  ILE A 963  ASP A 964                               
CRYST1  144.966   67.965  106.989  90.00  95.57  90.00 C 1 2 1       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      0.006898  0.000000  0.000672        0.00000                         
SCALE2      0.000000  0.014713  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009391        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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