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Database: PDB
Entry: 5T8F
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HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       07-SEP-16   5T8F              
TITLE     P110DELTA/P85ALPHA WITH TASELISIB (GDC-0032)                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT DELTA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PTDINS-3-KINASE SUBUNIT DELTA,PHOSPHATIDYLINOSITOL 4,5-     
COMPND   6 BISPHOSPHATE 3-KINASE 110 KDA CATALYTIC SUBUNIT DELTA,P110DELTA;     
COMPND   7 EC: 2.7.1.153;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT ALPHA;    
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: PI3-KINASE P110 DELTA AND P85 FRAGMENT;                    
COMPND  13 SYNONYM: PTDINS-3-KINASE REGULATORY SUBUNIT ALPHA,                   
COMPND  14 PHOSPHATIDYLINOSITOL 3-KINASE 85 KDA REGULATORY SUBUNIT ALPHA,PTDINS-
COMPND  15 3-KINASE REGULATORY SUBUNIT P85-ALPHA;                               
COMPND  16 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: PIK3CD;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  10 ORGANISM_COMMON: BOVINE;                                             
SOURCE  11 ORGANISM_TAXID: 9913;                                                
SOURCE  12 GENE: PIK3R1;                                                        
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PI3KDELTA KINASE, PROTEROS BIOSTRUCTURES GMBH, INHIBITOR, LIPID       
KEYWDS   2 KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MOERTL,S.STEINBACHER,C.EIGENBROT                                    
REVDAT   3   08-FEB-17 5T8F    1       JRNL                                     
REVDAT   2   25-JAN-17 5T8F    1       JRNL                                     
REVDAT   1   11-JAN-17 5T8F    0                                                
JRNL        AUTH   G.M.CASTANEDO,N.BLAQUIERE,M.BERESINI,B.BRAVO,H.BRIGHTBILL,   
JRNL        AUTH 2 J.CHEN,H.F.CUI,C.EIGENBROT,C.EVERETT,J.FENG,R.GODEMANN,      
JRNL        AUTH 3 E.GOGOL,S.HYMOWITZ,A.JOHNSON,N.KAYAGAKI,P.B.KOHLI,K.KNUPPEL, 
JRNL        AUTH 4 J.KRAEMER,S.KRUGER,P.LOKE,P.MCEWAN,C.MONTALBETTI,            
JRNL        AUTH 5 D.A.ROBERTS,M.SMITH,S.STEINBACHER,S.SUJATHA-BHASKAR,         
JRNL        AUTH 6 R.TAKAHASHI,X.WANG,L.C.WU,Y.ZHANG,S.T.STABEN                 
JRNL        TITL   STRUCTURE-BASED DESIGN OF TRICYCLIC NF-KAPPA B INDUCING      
JRNL        TITL 2 KINASE (NIK) INHIBITORS THAT HAVE HIGH SELECTIVITY OVER      
JRNL        TITL 3 PHOSPHOINOSITIDE-3-KINASE (PI3K).                            
JRNL        REF    J. MED. CHEM.                 V.  60   627 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28005357                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01363                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.91 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 86.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 30936                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.243                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.304                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 667                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.91                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.99                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2227                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 57                           
REMARK   3   BIN FREE R VALUE                    : 0.3410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8502                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 1                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.65000                                              
REMARK   3    B22 (A**2) : 4.72000                                              
REMARK   3    B33 (A**2) : -7.36000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.468         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.422         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 50.797        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.878                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8714 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8207 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11822 ; 1.121 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18738 ; 2.591 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1079 ; 5.205 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   393 ;35.333 ;24.071       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1450 ;13.109 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;14.400 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1330 ; 0.058 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9861 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2008 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4349 ; 0.554 ; 5.379       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4348 ; 0.553 ; 5.379       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5417 ; 0.867 ; 9.077       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5418 ; 0.867 ; 9.078       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4365 ; 0.580 ; 5.449       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4366 ; 0.580 ; 5.450       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6406 ; 0.921 ; 9.173       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  9727 ; 1.278 ;23.833       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  9728 ; 1.278 ;23.834       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    17        A   108                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.3320  17.3140 -11.2190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1322 T22:   0.0580                                     
REMARK   3      T33:   0.0929 T12:  -0.0294                                     
REMARK   3      T13:  -0.0170 T23:  -0.0411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1567 L22:   4.6121                                     
REMARK   3      L33:   7.6801 L12:   1.9202                                     
REMARK   3      L13:  -2.9467 L23:  -0.9280                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2309 S12:  -0.0708 S13:   0.2225                       
REMARK   3      S21:   0.1159 S22:   0.2075 S23:  -0.3879                       
REMARK   3      S31:  -0.2861 S32:  -0.0279 S33:   0.0233                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   109        A   278                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.6350  34.0270  17.0850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5713 T22:   0.0603                                     
REMARK   3      T33:   0.4288 T12:  -0.0189                                     
REMARK   3      T13:   0.0718 T23:   0.0315                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8669 L22:   4.4666                                     
REMARK   3      L33:   5.7948 L12:   0.3555                                     
REMARK   3      L13:  -0.4652 L23:   2.4247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1928 S12:  -0.0545 S13:   0.7145                       
REMARK   3      S21:   0.1404 S22:   0.2458 S23:  -0.2198                       
REMARK   3      S31:  -1.3122 S32:   0.2081 S33:  -0.4385                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   279        A   474                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.2390  -8.8590   7.1870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5194 T22:   0.2177                                     
REMARK   3      T33:   0.3221 T12:  -0.2215                                     
REMARK   3      T13:   0.0246 T23:  -0.1500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3266 L22:   4.0079                                     
REMARK   3      L33:   2.5926 L12:   0.2617                                     
REMARK   3      L13:  -0.7775 L23:   0.0927                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2853 S12:   0.3411 S13:  -0.3632                       
REMARK   3      S21:  -0.1870 S22:   0.0491 S23:   0.5078                       
REMARK   3      S31:   0.7316 S32:  -0.4596 S33:   0.2363                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   475        A   675                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0560  10.6790  17.2990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1909 T22:   0.2972                                     
REMARK   3      T33:   0.2612 T12:  -0.0450                                     
REMARK   3      T13:  -0.0362 T23:   0.1026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7397 L22:   1.8321                                     
REMARK   3      L33:   2.7608 L12:   0.2363                                     
REMARK   3      L13:  -1.1559 L23:   0.2945                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0763 S12:   0.3636 S13:  -0.2494                       
REMARK   3      S21:   0.1034 S22:   0.1470 S23:   0.5945                       
REMARK   3      S31:   0.2079 S32:  -0.8551 S33:  -0.0706                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   676        A   830                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.4330  16.4590  22.9980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1899 T22:   0.1898                                     
REMARK   3      T33:   0.1744 T12:  -0.0637                                     
REMARK   3      T13:  -0.0614 T23:   0.0301                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7010 L22:   1.6595                                     
REMARK   3      L33:   5.6628 L12:   0.4853                                     
REMARK   3      L13:  -2.0691 L23:  -0.1769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0310 S12:  -0.2575 S13:  -0.0773                       
REMARK   3      S21:   0.1772 S22:  -0.0374 S23:  -0.4152                       
REMARK   3      S31:  -0.2967 S32:   0.9999 S33:   0.0064                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   831        A  1031                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9230  12.5920  45.2630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4400 T22:   0.0995                                     
REMARK   3      T33:   0.1506 T12:  -0.0486                                     
REMARK   3      T13:  -0.0457 T23:   0.0485                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8388 L22:   1.7947                                     
REMARK   3      L33:   6.3141 L12:   1.2376                                     
REMARK   3      L13:   1.4784 L23:   0.6557                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1870 S12:  -0.5161 S13:  -0.2910                       
REMARK   3      S21:   0.5574 S22:  -0.1554 S23:  -0.1263                       
REMARK   3      S31:  -0.0366 S32:   0.2107 S33:  -0.0315                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   431        B   599                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0780  -9.2770   8.4670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3950 T22:   0.0315                                     
REMARK   3      T33:   0.2660 T12:  -0.0349                                     
REMARK   3      T13:   0.1127 T23:  -0.0649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6355 L22:   1.6173                                     
REMARK   3      L33:   7.8435 L12:   1.7235                                     
REMARK   3      L13:  -3.7454 L23:  -3.2630                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2368 S12:  -0.0965 S13:  -0.2887                       
REMARK   3      S21:  -0.2089 S22:  -0.0865 S23:  -0.2257                       
REMARK   3      S31:   0.3409 S32:   0.2225 S33:   0.3233                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS                                                          
REMARK   4                                                                      
REMARK   4 5T8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223891.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JAN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99988                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31603                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.910                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 86.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.91                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.04400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5DXU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
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       45.54800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.11150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.30200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.11150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.54800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.30200            
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: 4330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 52430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A   174                                                      
REMARK 465     ALA A   175                                                      
REMARK 465     GLN A   176                                                      
REMARK 465     THR A   177                                                      
REMARK 465     TRP A   178                                                      
REMARK 465     GLY A   179                                                      
REMARK 465     PRO A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     THR A   182                                                      
REMARK 465     LEU A   183                                                      
REMARK 465     ARG A   184                                                      
REMARK 465     THR A   226                                                      
REMARK 465     VAL A   227                                                      
REMARK 465     PHE A   228                                                      
REMARK 465     ARG A   229                                                      
REMARK 465     GLN A   230                                                      
REMARK 465     PRO A   231                                                      
REMARK 465     LEU A   232                                                      
REMARK 465     VAL A   233                                                      
REMARK 465     SER A   290                                                      
REMARK 465     ASN A   291                                                      
REMARK 465     PRO A   292                                                      
REMARK 465     ALA A   293                                                      
REMARK 465     PRO A   294                                                      
REMARK 465     GLN A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     GLN A   297                                                      
REMARK 465     LYS A   298                                                      
REMARK 465     PRO A   299                                                      
REMARK 465     ARG A   300                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     PRO A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     PRO A   305                                                      
REMARK 465     ILE A   306                                                      
REMARK 465     PRO A   307                                                      
REMARK 465     ALA A   308                                                      
REMARK 465     LYS A   309                                                      
REMARK 465     LYS A   310                                                      
REMARK 465     PRO A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     SER A   313                                                      
REMARK 465     VAL A   314                                                      
REMARK 465     LYS A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     ALA A   404                                                      
REMARK 465     ARG A   405                                                      
REMARK 465     SER A   406                                                      
REMARK 465     THR A   407                                                      
REMARK 465     LYS A   408                                                      
REMARK 465     LYS A   409                                                      
REMARK 465     LYS A   410                                                      
REMARK 465     SER A   411                                                      
REMARK 465     LYS A   412                                                      
REMARK 465     LYS A   413                                                      
REMARK 465     ALA A   414                                                      
REMARK 465     SER A   498                                                      
REMARK 465     GLU A   499                                                      
REMARK 465     CYS A   500                                                      
REMARK 465     VAL A   501                                                      
REMARK 465     HIS A   502                                                      
REMARK 465     VAL A   503                                                      
REMARK 465     THR A   504                                                      
REMARK 465     ARG A   518                                                      
REMARK 465     GLY A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     GLY A   521                                                      
REMARK 465     GLU A   522                                                      
REMARK 465     LEU A   523                                                      
REMARK 465     GLY A   769                                                      
REMARK 465     SER A   770                                                      
REMARK 465     GLY A   771                                                      
REMARK 465     LYS A   841                                                      
REMARK 465     SER A   842                                                      
REMARK 465     ASN A   843                                                      
REMARK 465     MET A   844                                                      
REMARK 465     ALA A   845                                                      
REMARK 465     ALA A   846                                                      
REMARK 465     THR A   847                                                      
REMARK 465     ALA A   848                                                      
REMARK 465     ALA A   849                                                      
REMARK 465     PHE A   850                                                      
REMARK 465     ASN A   851                                                      
REMARK 465     LYS A   852                                                      
REMARK 465     PHE A   919                                                      
REMARK 465     LYS A   920                                                      
REMARK 465     THR A   921                                                      
REMARK 465     LYS A   922                                                      
REMARK 465     PHE A   923                                                      
REMARK 465     GLY A   924                                                      
REMARK 465     ILE A   925                                                      
REMARK 465     ASN A   926                                                      
REMARK 465     ARG A   927                                                      
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     ASN A  17    CG   OD1  ND2                                       
REMARK 470     GLN A  18    CG   CD   OE1  NE2                                  
REMARK 470     HIS A  60    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 108    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 111    CG   CD   CE   NZ                                   
REMARK 470     LEU A 112    CG   CD1  CD2                                       
REMARK 470     GLN A 145    CD   OE1  NE2                                       
REMARK 470     GLN A 156    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 160    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 164    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 185    CG   CD1  CD2                                       
REMARK 470     ASN A 187    CG   OD1  ND2                                       
REMARK 470     ARG A 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 190    CG   CD1  CD2                                       
REMARK 470     LEU A 191    CG   CD1  CD2                                       
REMARK 470     LYS A 195    CD   CE   NZ                                        
REMARK 470     SER A 199    OG                                                  
REMARK 470     GLU A 200    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 201    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 206    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     LEU A 214    CG   CD1  CD2                                       
REMARK 470     LEU A 216    CG   CD1  CD2                                       
REMARK 470     LEU A 221    CG   CD1  CD2                                       
REMARK 470     LYS A 223    CD   CE   NZ                                        
REMARK 470     GLU A 234    CD   OE1  OE2                                       
REMARK 470     SER A 253    OG                                                  
REMARK 470     GLN A 258    CD   OE1  NE2                                       
REMARK 470     LEU A 266    CG   CD1  CD2                                       
REMARK 470     GLU A 288    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 289    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 321    CD   OE1  NE2                                       
REMARK 470     GLU A 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 332    CD   CE   NZ                                        
REMARK 470     GLU A 337    CD   OE1  OE2                                       
REMARK 470     ASN A 351    CG   OD1  ND2                                       
REMARK 470     GLU A 352    CD   OE1  OE2                                       
REMARK 470     LYS A 356    CD   CE   NZ                                        
REMARK 470     LYS A 372    CG   CD   CE   NZ                                   
REMARK 470     LEU A 384    CG   CD1  CD2                                       
REMARK 470     LYS A 400    CD   CE   NZ                                        
REMARK 470     LYS A 429    CD   CE   NZ                                        
REMARK 470     GLU A 448    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 449    CG   CD   CE   NZ                                   
REMARK 470     LEU A 452    CG   CD1  CD2                                       
REMARK 470     HIS A 481    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 489    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 490    CG   CD   CE   NZ                                   
REMARK 470     LEU A 494    CG   CD1  CD2                                       
REMARK 470     ARG A 496    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 506    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 508    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 509    CG   CD1  CD2                                       
REMARK 470     GLU A 525    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 526    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 528    CD   CE   NZ                                        
REMARK 470     LYS A 554    CD   CE   NZ                                        
REMARK 470     LYS A 557    CD   CE   NZ                                        
REMARK 470     LYS A 631    CD   CE   NZ                                        
REMARK 470     LYS A 680    CD   CE   NZ                                        
REMARK 470     LYS A 684    CD   CE   NZ                                        
REMARK 470     LYS A 705    CE   NZ                                             
REMARK 470     GLN A 710    CD   OE1  NE2                                       
REMARK 470     LYS A 712    CE   NZ                                             
REMARK 470     LEU A 714    CG   CD1  CD2                                       
REMARK 470     GLN A 748    CD   OE1  NE2                                       
REMARK 470     LYS A 755    CD   CE   NZ                                        
REMARK 470     LYS A 757    CD   CE   NZ                                        
REMARK 470     GLU A 767    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 802    NZ                                                  
REMARK 470     ARG A 830    CZ   NH1  NH2                                       
REMARK 470     LEU A 839    CG   CD1  CD2                                       
REMARK 470     LYS A 860    CD   CE   NZ                                        
REMARK 470     ARG A 870    CD   NE   CZ   NH1  NH2                             
REMARK 470     TYR A 936    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 955    CZ   NH1  NH2                                       
REMARK 470     ARG A 969    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 993    CE   NZ                                             
REMARK 470     GLU A1009    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1013    CD   CE   NZ                                        
REMARK 470     ARG A1016    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A1018    CD   CE   NZ                                        
REMARK 470     ARG A1024    NE   CZ   NH1  NH2                                  
REMARK 470     TRP A1027    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A1027    CZ3  CH2                                            
REMARK 470     LYS A1028    CD   CE   NZ                                        
REMARK 470     LYS A1030    CG   CD   CE   NZ                                   
REMARK 470     ASP B 434    CG   OD1  OD2                                       
REMARK 470     GLN B 435    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 438    CG   CD   CE   NZ                                   
REMARK 470     LYS B 447    CE   NZ                                             
REMARK 470     LYS B 448    CE   NZ                                             
REMARK 470     GLU B 458    CD   OE1  OE2                                       
REMARK 470     ARG B 465    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 492    CE   NZ                                             
REMARK 470     LYS B 506    CG   CD   CE   NZ                                   
REMARK 470     GLU B 510    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 511    CG   CD   CE   NZ                                   
REMARK 470     PHE B 512    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 513    CG   CD   CE   NZ                                   
REMARK 470     ARG B 514    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 515    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 518    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 520    CD   OE1  OE2                                       
REMARK 470     GLN B 522    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 529    CD   OE1  OE2                                       
REMARK 470     LYS B 530    CD   CE   NZ                                        
REMARK 470     GLU B 547    CD   OE1  OE2                                       
REMARK 470     LYS B 550    CD   CE   NZ                                        
REMARK 470     LYS B 551    CD   CE   NZ                                        
REMARK 470     LYS B 561    NZ                                                  
REMARK 470     GLN B 572    CD   OE1  NE2                                       
REMARK 470     LYS B 575    CD   CE   NZ                                        
REMARK 470     GLN B 579    CD   OE1  NE2                                       
REMARK 470     LYS B 587    CE   NZ                                             
REMARK 470     ARG B 590    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 592    CD   CE   NZ                                        
REMARK 470     GLU B 596    CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  33       89.53   -154.05                                   
REMARK 500    PRO A  97       82.56    -69.84                                   
REMARK 500    ARG A 104       80.40    -69.82                                   
REMARK 500    ARG A 222       82.42    -66.23                                   
REMARK 500    ASP A 238       40.32    -99.17                                   
REMARK 500    ASP A 287       87.28    -56.67                                   
REMARK 500    ILE A 328      -72.62    -83.17                                   
REMARK 500    MET A 387       40.06    -94.86                                   
REMARK 500    ALA A 545       37.58    -86.78                                   
REMARK 500    PHE A 587       70.03   -117.98                                   
REMARK 500    HIS A 730       81.73     59.46                                   
REMARK 500    ASP A 736      109.39   -162.12                                   
REMARK 500    ALA A 742      -73.32    -78.68                                   
REMARK 500    THR A 750     -165.21   -168.08                                   
REMARK 500    ASP A 753      -17.81     62.19                                   
REMARK 500    SER A 754      178.27    -55.77                                   
REMARK 500    ASP B 434       84.42   -165.10                                   
REMARK 500    VAL B 436      -50.85   -132.43                                   
REMARK 500    ASP B 440       57.67   -144.35                                   
REMARK 500    GLU B 515       79.24     58.58                                   
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 799 A 1101                
DBREF  5T8F A   17  1031  UNP    O00329   PK3CD_HUMAN     17   1031             
DBREF  5T8F B  431   599  UNP    P23727   P85A_BOVIN     431    599             
SEQRES   1 A 1015  ASN GLN SER VAL VAL VAL ASP PHE LEU LEU PRO THR GLY          
SEQRES   2 A 1015  VAL TYR LEU ASN PHE PRO VAL SER ARG ASN ALA ASN LEU          
SEQRES   3 A 1015  SER THR ILE LYS GLN LEU LEU TRP HIS ARG ALA GLN TYR          
SEQRES   4 A 1015  GLU PRO LEU PHE HIS MET LEU SER GLY PRO GLU ALA TYR          
SEQRES   5 A 1015  VAL PHE THR CYS ILE ASN GLN THR ALA GLU GLN GLN GLU          
SEQRES   6 A 1015  LEU GLU ASP GLU GLN ARG ARG LEU CYS ASP VAL GLN PRO          
SEQRES   7 A 1015  PHE LEU PRO VAL LEU ARG LEU VAL ALA ARG GLU GLY ASP          
SEQRES   8 A 1015  ARG VAL LYS LYS LEU ILE ASN SER GLN ILE SER LEU LEU          
SEQRES   9 A 1015  ILE GLY LYS GLY LEU HIS GLU PHE ASP SER LEU CYS ASP          
SEQRES  10 A 1015  PRO GLU VAL ASN ASP PHE ARG ALA LYS MET CYS GLN PHE          
SEQRES  11 A 1015  CYS GLU GLU ALA ALA ALA ARG ARG GLN GLN LEU GLY TRP          
SEQRES  12 A 1015  GLU ALA TRP LEU GLN TYR SER PHE PRO LEU GLN LEU GLU          
SEQRES  13 A 1015  PRO SER ALA GLN THR TRP GLY PRO GLY THR LEU ARG LEU          
SEQRES  14 A 1015  PRO ASN ARG ALA LEU LEU VAL ASN VAL LYS PHE GLU GLY          
SEQRES  15 A 1015  SER GLU GLU SER PHE THR PHE GLN VAL SER THR LYS ASP          
SEQRES  16 A 1015  VAL PRO LEU ALA LEU MET ALA CYS ALA LEU ARG LYS LYS          
SEQRES  17 A 1015  ALA THR VAL PHE ARG GLN PRO LEU VAL GLU GLN PRO GLU          
SEQRES  18 A 1015  ASP TYR THR LEU GLN VAL ASN GLY ARG HIS GLU TYR LEU          
SEQRES  19 A 1015  TYR GLY SER TYR PRO LEU CYS GLN PHE GLN TYR ILE CYS          
SEQRES  20 A 1015  SER CYS LEU HIS SER GLY LEU THR PRO HIS LEU THR MET          
SEQRES  21 A 1015  VAL HIS SER SER SER ILE LEU ALA MET ARG ASP GLU GLN          
SEQRES  22 A 1015  SER ASN PRO ALA PRO GLN VAL GLN LYS PRO ARG ALA LYS          
SEQRES  23 A 1015  PRO PRO PRO ILE PRO ALA LYS LYS PRO SER SER VAL SER          
SEQRES  24 A 1015  LEU TRP SER LEU GLU GLN PRO PHE ARG ILE GLU LEU ILE          
SEQRES  25 A 1015  GLN GLY SER LYS VAL ASN ALA ASP GLU ARG MET LYS LEU          
SEQRES  26 A 1015  VAL VAL GLN ALA GLY LEU PHE HIS GLY ASN GLU MET LEU          
SEQRES  27 A 1015  CYS LYS THR VAL SER SER SER GLU VAL SER VAL CYS SER          
SEQRES  28 A 1015  GLU PRO VAL TRP LYS GLN ARG LEU GLU PHE ASP ILE ASN          
SEQRES  29 A 1015  ILE CYS ASP LEU PRO ARG MET ALA ARG LEU CYS PHE ALA          
SEQRES  30 A 1015  LEU TYR ALA VAL ILE GLU LYS ALA LYS LYS ALA ARG SER          
SEQRES  31 A 1015  THR LYS LYS LYS SER LYS LYS ALA ASP CYS PRO ILE ALA          
SEQRES  32 A 1015  TRP ALA ASN LEU MET LEU PHE ASP TYR LYS ASP GLN LEU          
SEQRES  33 A 1015  LYS THR GLY GLU ARG CYS LEU TYR MET TRP PRO SER VAL          
SEQRES  34 A 1015  PRO ASP GLU LYS GLY GLU LEU LEU ASN PRO THR GLY THR          
SEQRES  35 A 1015  VAL ARG SER ASN PRO ASN THR ASP SER ALA ALA ALA LEU          
SEQRES  36 A 1015  LEU ILE CYS LEU PRO GLU VAL ALA PRO HIS PRO VAL TYR          
SEQRES  37 A 1015  TYR PRO ALA LEU GLU LYS ILE LEU GLU LEU GLY ARG HIS          
SEQRES  38 A 1015  SER GLU CYS VAL HIS VAL THR GLU GLU GLU GLN LEU GLN          
SEQRES  39 A 1015  LEU ARG GLU ILE LEU GLU ARG ARG GLY SER GLY GLU LEU          
SEQRES  40 A 1015  TYR GLU HIS GLU LYS ASP LEU VAL TRP LYS LEU ARG HIS          
SEQRES  41 A 1015  GLU VAL GLN GLU HIS PHE PRO GLU ALA LEU ALA ARG LEU          
SEQRES  42 A 1015  LEU LEU VAL THR LYS TRP ASN LYS HIS GLU ASP VAL ALA          
SEQRES  43 A 1015  GLN MET LEU TYR LEU LEU CYS SER TRP PRO GLU LEU PRO          
SEQRES  44 A 1015  VAL LEU SER ALA LEU GLU LEU LEU ASP PHE SER PHE PRO          
SEQRES  45 A 1015  ASP CYS HIS VAL GLY SER PHE ALA ILE LYS SER LEU ARG          
SEQRES  46 A 1015  LYS LEU THR ASP ASP GLU LEU PHE GLN TYR LEU LEU GLN          
SEQRES  47 A 1015  LEU VAL GLN VAL LEU LYS TYR GLU SER TYR LEU ASP CYS          
SEQRES  48 A 1015  GLU LEU THR LYS PHE LEU LEU ASP ARG ALA LEU ALA ASN          
SEQRES  49 A 1015  ARG LYS ILE GLY HIS PHE LEU PHE TRP HIS LEU ARG SER          
SEQRES  50 A 1015  GLU MET HIS VAL PRO SER VAL ALA LEU ARG PHE GLY LEU          
SEQRES  51 A 1015  ILE LEU GLU ALA TYR CYS ARG GLY SER THR HIS HIS MET          
SEQRES  52 A 1015  LYS VAL LEU MET LYS GLN GLY GLU ALA LEU SER LYS LEU          
SEQRES  53 A 1015  LYS ALA LEU ASN ASP PHE VAL LYS LEU SER SER GLN LYS          
SEQRES  54 A 1015  THR PRO LYS PRO GLN THR LYS GLU LEU MET HIS LEU CYS          
SEQRES  55 A 1015  MET ARG GLN GLU ALA TYR LEU GLU ALA LEU SER HIS LEU          
SEQRES  56 A 1015  GLN SER PRO LEU ASP PRO SER THR LEU LEU ALA GLU VAL          
SEQRES  57 A 1015  CYS VAL GLU GLN CYS THR PHE MET ASP SER LYS MET LYS          
SEQRES  58 A 1015  PRO LEU TRP ILE MET TYR SER ASN GLU GLU ALA GLY SER          
SEQRES  59 A 1015  GLY GLY SER VAL GLY ILE ILE PHE LYS ASN GLY ASP ASP          
SEQRES  60 A 1015  LEU ARG GLN ASP MET LEU THR LEU GLN MET ILE GLN LEU          
SEQRES  61 A 1015  MET ASP VAL LEU TRP LYS GLN GLU GLY LEU ASP LEU ARG          
SEQRES  62 A 1015  MET THR PRO TYR GLY CYS LEU PRO THR GLY ASP ARG THR          
SEQRES  63 A 1015  GLY LEU ILE GLU VAL VAL LEU ARG SER ASP THR ILE ALA          
SEQRES  64 A 1015  ASN ILE GLN LEU ASN LYS SER ASN MET ALA ALA THR ALA          
SEQRES  65 A 1015  ALA PHE ASN LYS ASP ALA LEU LEU ASN TRP LEU LYS SER          
SEQRES  66 A 1015  LYS ASN PRO GLY GLU ALA LEU ASP ARG ALA ILE GLU GLU          
SEQRES  67 A 1015  PHE THR LEU SER CYS ALA GLY TYR CYS VAL ALA THR TYR          
SEQRES  68 A 1015  VAL LEU GLY ILE GLY ASP ARG HIS SER ASP ASN ILE MET          
SEQRES  69 A 1015  ILE ARG GLU SER GLY GLN LEU PHE HIS ILE ASP PHE GLY          
SEQRES  70 A 1015  HIS PHE LEU GLY ASN PHE LYS THR LYS PHE GLY ILE ASN          
SEQRES  71 A 1015  ARG GLU ARG VAL PRO PHE ILE LEU THR TYR ASP PHE VAL          
SEQRES  72 A 1015  HIS VAL ILE GLN GLN GLY LYS THR ASN ASN SER GLU LYS          
SEQRES  73 A 1015  PHE GLU ARG PHE ARG GLY TYR CYS GLU ARG ALA TYR THR          
SEQRES  74 A 1015  ILE LEU ARG ARG HIS GLY LEU LEU PHE LEU HIS LEU PHE          
SEQRES  75 A 1015  ALA LEU MET ARG ALA ALA GLY LEU PRO GLU LEU SER CYS          
SEQRES  76 A 1015  SER LYS ASP ILE GLN TYR LEU LYS ASP SER LEU ALA LEU          
SEQRES  77 A 1015  GLY LYS THR GLU GLU GLU ALA LEU LYS HIS PHE ARG VAL          
SEQRES  78 A 1015  LYS PHE ASN GLU ALA LEU ARG GLU SER TRP LYS THR LYS          
SEQRES  79 A 1015  VAL                                                          
SEQRES   1 B  169  TYR GLN GLN ASP GLN VAL VAL LYS GLU ASP ASN ILE GLU          
SEQRES   2 B  169  ALA VAL GLY LYS LYS LEU HIS GLU TYR ASN THR GLN PHE          
SEQRES   3 B  169  GLN GLU LYS SER ARG GLU TYR ASP ARG LEU TYR GLU ASP          
SEQRES   4 B  169  TYR THR ARG THR SER GLN GLU ILE GLN MET LYS ARG THR          
SEQRES   5 B  169  ALA ILE GLU ALA PHE ASN GLU THR ILE LYS ILE PHE GLU          
SEQRES   6 B  169  GLU GLN CYS GLN THR GLN GLU ARG TYR SER LYS GLU TYR          
SEQRES   7 B  169  ILE GLU LYS PHE LYS ARG GLU GLY ASN GLU THR GLU ILE          
SEQRES   8 B  169  GLN ARG ILE MET HIS ASN TYR GLU LYS LEU LYS SER ARG          
SEQRES   9 B  169  ILE SER GLU ILE VAL ASP SER ARG ARG ARG LEU GLU GLU          
SEQRES  10 B  169  ASP LEU LYS LYS GLN ALA ALA GLU TYR ARG GLU ILE ASP          
SEQRES  11 B  169  LYS ARG MET ASN SER ILE LYS PRO ASP LEU ILE GLN LEU          
SEQRES  12 B  169  ARG LYS THR ARG ASP GLN TYR LEU MET TRP LEU THR GLN          
SEQRES  13 B  169  LYS GLY VAL ARG GLN LYS LYS LEU ASN GLU TRP LEU GLY          
HET    799  A1101      34                                                       
HETNAM     799 2-METHYL-2-(4-{2-[3-METHYL-1-(PROPAN-2-YL)-1H-1,2,4-             
HETNAM   2 799  TRIAZOL-5-YL]-5,6-DIHYDROIMIDAZO[1,2-D][1,                      
HETNAM   3 799  4]BENZOXAZEPIN-9-YL}-1H-PYRAZOL-1-YL)PROPANAMIDE                
HETSYN     799 TASELISIB                                                        
FORMUL   3  799    C24 H28 N8 O2                                                
FORMUL   4  HOH   *(H2 O)                                                       
HELIX    1 AA1 ASN A   41  GLN A   54  1                                  14    
HELIX    2 AA2 LEU A   58  LEU A   62  5                                   5    
HELIX    3 AA3 GLY A   64  GLU A   66  5                                   3    
HELIX    4 AA4 ARG A   88  GLN A   93  1                                   6    
HELIX    5 AA5 ASP A  107  GLY A  122  1                                  16    
HELIX    6 AA6 LEU A  125  LEU A  131  1                                   7    
HELIX    7 AA7 ASP A  133  LEU A  157  1                                  25    
HELIX    8 AA8 GLY A  158  PHE A  167  1                                  10    
HELIX    9 AA9 VAL A  212  ARG A  222  1                                  11    
HELIX   10 AB1 GLN A  235  GLU A  237  5                                   3    
HELIX   11 AB2 PRO A  255  GLN A  258  5                                   4    
HELIX   12 AB3 PHE A  259  GLY A  269  1                                  11    
HELIX   13 AB4 SER A  279  ASP A  287  1                                   9    
HELIX   14 AB5 ALA A  487  ARG A  496  1                                  10    
HELIX   15 AB6 GLU A  506  ARG A  517  1                                  12    
HELIX   16 AB7 GLU A  525  LEU A  534  1                                  10    
HELIX   17 AB8 LEU A  534  PHE A  542  1                                   9    
HELIX   18 AB9 ALA A  545  THR A  553  1                                   9    
HELIX   19 AC1 LYS A  557  CYS A  569  1                                  13    
HELIX   20 AC2 PRO A  575  LEU A  583  1                                   9    
HELIX   21 AC3 ASP A  589  LEU A  600  1                                  12    
HELIX   22 AC4 ARG A  601  LEU A  603  5                                   3    
HELIX   23 AC5 THR A  604  TYR A  611  1                                   8    
HELIX   24 AC6 TYR A  611  LEU A  619  1                                   9    
HELIX   25 AC7 LYS A  620  GLU A  622  5                                   3    
HELIX   26 AC8 CYS A  627  ASN A  640  1                                  14    
HELIX   27 AC9 ASN A  640  SER A  653  1                                  14    
HELIX   28 AD1 VAL A  657  SER A  675  1                                  19    
HELIX   29 AD2 SER A  675  THR A  706  1                                  32    
HELIX   30 AD3 PRO A  707  GLN A  721  1                                  15    
HELIX   31 AD4 GLN A  721  SER A  729  1                                   9    
HELIX   32 AD5 LEU A  784  GLN A  803  1                                  20    
HELIX   33 AD6 ILE A  834  ASN A  840  1                                   7    
HELIX   34 AD7 ALA A  854  ASN A  863  1                                  10    
HELIX   35 AD8 GLU A  866  GLY A  890  1                                  25    
HELIX   36 AD9 THR A  935  GLN A  943  1                                   9    
HELIX   37 AE1 ASN A  949  HIS A  970  1                                  22    
HELIX   38 AE2 HIS A  970  ARG A  982  1                                  13    
HELIX   39 AE3 ALA A  983  GLY A  985  5                                   3    
HELIX   40 AE4 CYS A  991  LEU A 1002  1                                  12    
HELIX   41 AE5 THR A 1007  VAL A 1031  1                                  25    
HELIX   42 AE6 ASN B  441  ARG B  514  1                                  74    
HELIX   43 AE7 ASN B  517  GLY B  588  1                                  72    
HELIX   44 AE8 ARG B  590  GLY B  599  1                                  10    
SHEET    1 AA1 5 TYR A  31  SER A  37  0                                        
SHEET    2 AA1 5 SER A  19  LEU A  25 -1  N  PHE A  24   O  LEU A  32           
SHEET    3 AA1 5 VAL A  98  ALA A 103  1  O  LEU A  99   N  ASP A  23           
SHEET    4 AA1 5 TYR A  68  ILE A  73 -1  N  THR A  71   O  ARG A 100           
SHEET    5 AA1 5 GLN A  79  GLU A  81 -1  O  GLN A  80   N  CYS A  72           
SHEET    1 AA2 5 PHE A 203  PHE A 205  0                                        
SHEET    2 AA2 5 VAL A 192  PHE A 196 -1  N  VAL A 194   O  PHE A 203           
SHEET    3 AA2 5 HIS A 273  HIS A 278  1  O  MET A 276   N  LYS A 195           
SHEET    4 AA2 5 TYR A 239  VAL A 243 -1  N  GLN A 242   O  THR A 275           
SHEET    5 AA2 5 TYR A 249  LEU A 250 -1  O  LEU A 250   N  LEU A 241           
SHEET    1 AA3 4 VAL A 370  ASN A 380  0                                        
SHEET    2 AA3 4 PRO A 322  SER A 331 -1  N  PHE A 323   O  ILE A 379           
SHEET    3 AA3 4 ALA A 470  LEU A 475 -1  O  LEU A 472   N  GLN A 329           
SHEET    4 AA3 4 GLY A 435  TYR A 440 -1  N  ARG A 437   O  ILE A 473           
SHEET    1 AA4 3 GLU A 352  MET A 353  0                                        
SHEET    2 AA4 3 LYS A 340  HIS A 349 -1  N  HIS A 349   O  GLU A 352           
SHEET    3 AA4 3 VAL A 363  SER A 364 -1  O  VAL A 363   N  LEU A 341           
SHEET    1 AA5 5 GLU A 352  MET A 353  0                                        
SHEET    2 AA5 5 LYS A 340  HIS A 349 -1  N  HIS A 349   O  GLU A 352           
SHEET    3 AA5 5 ARG A 389  VAL A 397 -1  O  TYR A 395   N  VAL A 342           
SHEET    4 AA5 5 CYS A 416  MET A 424 -1  O  ALA A 421   N  PHE A 392           
SHEET    5 AA5 5 TRP A 442  PRO A 443 -1  O  TRP A 442   N  TRP A 420           
SHEET    1 AA6 2 LEU A 731  SER A 733  0                                        
SHEET    2 AA6 2 ASP A 736  LEU A 741 -1  O  LEU A 741   N  LEU A 731           
SHEET    1 AA7 3 GLU A 743  VAL A 744  0                                        
SHEET    2 AA7 3 LEU A 759  SER A 764 -1  O  SER A 764   N  GLU A 743           
SHEET    3 AA7 3 THR A 750  PHE A 751 -1  N  THR A 750   O  TRP A 760           
SHEET    1 AA8 5 GLU A 743  VAL A 744  0                                        
SHEET    2 AA8 5 LEU A 759  SER A 764 -1  O  SER A 764   N  GLU A 743           
SHEET    3 AA8 5 GLY A 775  ASN A 780 -1  O  ILE A 776   N  ILE A 761           
SHEET    4 AA8 5 THR A 822  GLU A 826 -1  O  GLY A 823   N  LYS A 779           
SHEET    5 AA8 5 CYS A 815  GLY A 819 -1  N  LEU A 816   O  LEU A 824           
SHEET    1 AA9 3 SER A 831  THR A 833  0                                        
SHEET    2 AA9 3 ILE A 899  ARG A 902 -1  O  ILE A 901   N  ASP A 832           
SHEET    3 AA9 3 LEU A 907  HIS A 909 -1  O  PHE A 908   N  MET A 900           
SITE     1 AC1 11 PRO A 758  TRP A 760  LYS A 779  ASP A 787                    
SITE     2 AC1 11 ILE A 825  GLU A 826  VAL A 828  SER A 831                    
SITE     3 AC1 11 ASP A 832  PHE A 908  ASP A 911                               
CRYST1   91.096  108.604  142.223  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      0.010977  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009208  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007031        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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