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Database: PDB
Entry: 5DXT
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HEADER    TRANSFERASE/INHIBITOR                   23-SEP-15   5DXT              
TITLE     P110ALPHA WITH GDC-0326                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT ALPHA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: PI3-KINASE P110 ALPHA, UNP RESIDUES 107-1068;              
COMPND   6 SYNONYM: PTDINS-3-KINASE SUBUNIT ALPHA,PHOSPHATIDYLINOSITOL 4,5-     
COMPND   7 BISPHOSPHATE 3-KINASE 110 KDA CATALYTIC SUBUNIT ALPHA,P110ALPHA,     
COMPND   8 PHOSPHOINOSITIDE-3-KINASE CATALYTIC ALPHA POLYPEPTIDE,               
COMPND   9 SERINE/THREONINE PROTEIN KINASE PIK3CA;                              
COMPND  10 EC: 2.7.1.153,2.7.11.1;                                              
COMPND  11 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: PIK3CA;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    LIPID KINASE, TRANSFERASE-INHIBITOR COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.P.HEFFRON,R.A.HEALD,C.NDUBAKU,B.Q.WEI,M.AUGUSTIN,S.DO,K.EDGAR,      
AUTHOR   2 C.EIGENBROT,L.FRIEDMAN,E.GANCIA,P.S.JACKSON,G.JONES,A.KOLESNIKOV,    
AUTHOR   3 L.B.LEE,J.D.LESNICK,C.LEWIS,N.MCLEAN,M.MORTLE,J.NONOMIYA,J.PANG,     
AUTHOR   4 S.PRICE,W.W.PRIOR,L.SALPHATI,S.SIDERIS,S.T.STABEN,S.STEINBACHER,     
AUTHOR   5 V.TSUI,J.WALLIN,D.SAMPATH,A.OLIVERO                                  
REVDAT   2   24-FEB-16 5DXT    1       JRNL                                     
REVDAT   1   27-JAN-16 5DXT    0                                                
JRNL        AUTH   T.P.HEFFRON,R.A.HEALD,C.NDUBAKU,B.WEI,M.AUGISTIN,S.DO,       
JRNL        AUTH 2 K.EDGAR,C.EIGENBROT,L.FRIEDMAN,E.GANCIA,P.S.JACKSON,G.JONES, 
JRNL        AUTH 3 A.KOLESNIKOV,L.B.LEE,J.D.LESNICK,C.LEWIS,N.MCLEAN,M.MORTL,   
JRNL        AUTH 4 J.NONOMIYA,J.PANG,S.PRICE,W.W.PRIOR,L.SALPHATI,S.SIDERIS,    
JRNL        AUTH 5 S.T.STABEN,S.STEINBACHER,V.TSUI,J.WALLIN,D.SAMPATH,          
JRNL        AUTH 6 A.G.OLIVERO                                                  
JRNL        TITL   THE RATIONAL DESIGN OF SELECTIVE BENZOXAZEPIN INHIBITORS OF  
JRNL        TITL 2 THE ALPHA-ISOFORM OF PHOSPHOINOSITIDE 3-KINASE CULMINATING   
JRNL        TITL 3 IN THE IDENTIFICATION OF                                     
JRNL        TITL 4 (S)-2-((2-(1-ISOPROPYL-1H-1,2,4-TRIAZOL-5-YL)-5,             
JRNL        TITL 5 6-DIHYDROBENZO[F]IMIDAZO[1,2-D][1,4]OXAZEPIN-9-YL)OXY)       
JRNL        TITL 6 PROPANAMIDE (GDC-0326).                                      
JRNL        REF    J.MED.CHEM.                   V.  59   985 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26741947                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B01483                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 97.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 50478                          
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) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1388                            
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3667                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 115                          
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7187                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 198                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.04000                                              
REMARK   3    B22 (A**2) : 1.54000                                              
REMARK   3    B33 (A**2) : -2.59000                                             
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): 0.300         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.227         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.184         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.795        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7163 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  6422 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9714 ; 1.051 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14875 ; 0.882 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   869 ; 5.066 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   332 ;35.132 ;24.277       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1209 ;12.798 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;10.930 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1073 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7910 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1440 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1328 ; 0.149 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6169 ; 0.126 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3377 ; 0.154 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3674 ; 0.073 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   260 ; 0.078 ; 0.200       
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):     5 ; 0.069 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    33 ; 0.094 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.111 ; 0.200       
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):  5703 ; 1.068 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1757 ; 0.158 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7063 ; 1.273 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3280 ; 1.847 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2651 ; 2.603 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   107        A   165                          
REMARK   3    RESIDUE RANGE :   A   291        A   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):   16.251   -3.453   36.974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1301 T22:  -0.0276                                     
REMARK   3      T33:  -0.1235 T12:   0.0436                                     
REMARK   3      T13:  -0.0285 T23:  -0.0313                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5293 L22:   3.1028                                     
REMARK   3      L33:   2.2009 L12:  -1.6732                                     
REMARK   3      L13:  -0.7738 L23:  -0.4009                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0047 S12:  -0.4420 S13:   0.0294                       
REMARK   3      S21:   0.8036 S22:   0.0531 S23:  -0.4408                       
REMARK   3      S31:   0.2898 S32:   0.5789 S33:  -0.0484                       
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   322        A   487                          
REMARK   3    ORIGIN FOR THE GROUP (A):    8.641  -19.824    3.953              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1936 T22:  -0.2265                                     
REMARK   3      T33:  -0.1160 T12:  -0.0147                                     
REMARK   3      T13:   0.0274 T23:  -0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8730 L22:   2.8093                                     
REMARK   3      L33:   4.8555 L12:   2.0862                                     
REMARK   3      L13:  -1.6161 L23:  -0.6805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1600 S12:   0.2807 S13:  -0.2526                       
REMARK   3      S21:  -0.2007 S22:   0.1228 S23:   0.0670                       
REMARK   3      S31:   1.0756 S32:  -0.2749 S33:   0.0371                       
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   488        A   699                          
REMARK   3    ORIGIN FOR THE GROUP (A):   16.026    3.970    8.438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2620 T22:  -0.1997                                     
REMARK   3      T33:  -0.1993 T12:  -0.0184                                     
REMARK   3      T13:  -0.0011 T23:  -0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8857 L22:   0.1749                                     
REMARK   3      L33:   4.2576 L12:  -0.1226                                     
REMARK   3      L13:  -1.1443 L23:   0.1738                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0563 S12:   0.0961 S13:   0.0524                       
REMARK   3      S21:  -0.0873 S22:   0.0214 S23:  -0.0535                       
REMARK   3      S31:  -0.2294 S32:   0.2795 S33:  -0.0776                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   700        A   785                          
REMARK   3    RESIDUE RANGE :   A   796        A   850                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -10.679    6.625   34.236              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2584 T22:  -0.1327                                     
REMARK   3      T33:  -0.1871 T12:   0.0349                                     
REMARK   3      T13:   0.0078 T23:  -0.0370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7478 L22:   1.5706                                     
REMARK   3      L33:   3.2428 L12:  -0.6253                                     
REMARK   3      L13:   0.6044 L23:  -0.6862                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0535 S12:  -0.2221 S13:  -0.0736                       
REMARK   3      S21:   0.0745 S22:   0.0993 S23:   0.3035                       
REMARK   3      S31:  -0.0315 S32:  -0.5538 S33:  -0.1529                       
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   786        A   795                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.621   21.967   45.299              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0060 T22:  -0.0640                                     
REMARK   3      T33:  -0.0103 T12:   0.1011                                     
REMARK   3      T13:   0.0555 T23:  -0.1271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1882 L22:  30.9197                                     
REMARK   3      L33:   5.2568 L12:  12.5170                                     
REMARK   3      L13:  -5.2187 L23: -12.5175                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2116 S12:   0.0131 S13:   0.7919                       
REMARK   3      S21:   0.4317 S22:  -0.8655 S23:   0.6940                       
REMARK   3      S31:  -0.7538 S32:  -0.0366 S33:   0.6539                       
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   851        A  1333                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.753   21.255   12.830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1172 T22:  -0.0903                                     
REMARK   3      T33:  -0.1110 T12:   0.0448                                     
REMARK   3      T13:  -0.0372 T23:   0.0928                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3186 L22:   2.6682                                     
REMARK   3      L33:   2.9038 L12:  -1.2786                                     
REMARK   3      L13:  -0.9587 L23:   0.4740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0528 S12:   0.3574 S13:   0.2291                       
REMARK   3      S21:  -0.2048 S22:   0.1051 S23:   0.3164                       
REMARK   3      S31:  -0.3976 S32:  -0.4869 S33:  -0.0523                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
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 5DXT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213994.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51953                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 97.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, 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       29.25350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.66950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.83600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.66950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.25350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.83600            
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     SER A   199                                                      
REMARK 465     PRO A   200                                                      
REMARK 465     ASN A   201                                                      
REMARK 465     ASN A   202                                                      
REMARK 465     LEU A   233                                                      
REMARK 465     LEU A   234                                                      
REMARK 465     SER A   235                                                      
REMARK 465     SER A   236                                                      
REMARK 465     GLU A   237                                                      
REMARK 465     GLN A   238                                                      
REMARK 465     LEU A   239                                                      
REMARK 465     LYS A   240                                                      
REMARK 465     LEU A   241                                                      
REMARK 465     CYS A   242                                                      
REMARK 465     VAL A   243                                                      
REMARK 465     LEU A   244                                                      
REMARK 465     GLU A   245                                                      
REMARK 465     TYR A   246                                                      
REMARK 465     GLN A   247                                                      
REMARK 465     ILE A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     THR A   313                                                      
REMARK 465     ALA A   314                                                      
REMARK 465     THR A   315                                                      
REMARK 465     PRO A   316                                                      
REMARK 465     TYR A   317                                                      
REMARK 465     MET A   318                                                      
REMARK 465     ASN A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     ILE A   348                                                      
REMARK 465     ARG A   349                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     ILE A   351                                                      
REMARK 465     ASP A   352                                                      
REMARK 465     LYS A   353                                                      
REMARK 465     LYS A   410                                                      
REMARK 465     GLY A   411                                                      
REMARK 465     ARG A   412                                                      
REMARK 465     LYS A   413                                                      
REMARK 465     GLY A   414                                                      
REMARK 465     ALA A   415                                                      
REMARK 465     LYS A   416                                                      
REMARK 465     HIS A   450                                                      
REMARK 465     GLY A   451                                                      
REMARK 465     LEU A   452                                                      
REMARK 465     GLU A   453                                                      
REMARK 465     LYS A   863                                                      
REMARK 465     GLY A   864                                                      
REMARK 465     GLY A   865                                                      
REMARK 465     LEU A   866                                                      
REMARK 465     LYS A   867                                                      
REMARK 465     GLY A   868                                                      
REMARK 465     ALA A   869                                                      
REMARK 465     LEU A   870                                                      
REMARK 465     GLN A   871                                                      
REMARK 465     PHE A   872                                                      
REMARK 465     LYS A   941                                                      
REMARK 465     LYS A   942                                                      
REMARK 465     LYS A   943                                                      
REMARK 465     LYS A   944                                                      
REMARK 465     PHE A   945                                                      
REMARK 465     GLY A   946                                                      
REMARK 465     TYR A   947                                                      
REMARK 465     LYS A   948                                                      
REMARK 465     GLN A   969                                                      
REMARK 465     THR A  1052                                                      
REMARK 465     THR A  1053                                                      
REMARK 465     LYS A  1054                                                      
REMARK 465     MET A  1055                                                      
REMARK 465     ASP A  1056                                                      
REMARK 465     TRP A  1057                                                      
REMARK 465     ILE A  1058                                                      
REMARK 465     PHE A  1059                                                      
REMARK 465     HIS A  1060                                                      
REMARK 465     THR A  1061                                                      
REMARK 465     ILE A  1062                                                      
REMARK 465     LYS A  1063                                                      
REMARK 465     GLN A  1064                                                      
REMARK 465     HIS A  1065                                                      
REMARK 465     ALA A  1066                                                      
REMARK 465     LEU A  1067                                                      
REMARK 465     ASN A  1068                                                      
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     ARG A  108   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A  111   CD   CE   NZ                                        
REMARK 480     LYS A  132   CG   CD   CE   NZ                                   
REMARK 480     LYS A  148   CD   CE   NZ                                        
REMARK 480     LEU A  177   CG   CD1  CD2                                       
REMARK 480     LYS A  179   CG   CD   CE   NZ                                   
REMARK 480     ASN A  183   CG   OD1  ND2                                       
REMARK 480     LYS A  184   CG   CD   CE   NZ                                   
REMARK 480     LYS A  187   CG   CD   CE   NZ                                   
REMARK 480     LYS A  204   CG   CD   CE   NZ                                   
REMARK 480     GLU A  223   CG   CD   OE1  OE2                                  
REMARK 480     ARG A  226   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A  249   CG   CD   CE   NZ                                   
REMARK 480     LYS A  264   CG   CD   CE   NZ                                   
REMARK 480     MET A  278   SD   CE                                             
REMARK 480     ARG A  281   NE   CZ   NH1  NH2                                  
REMARK 480     LYS A  290   CD   CE   NZ                                        
REMARK 480     GLN A  296   CG   CD   OE1  NE2                                  
REMARK 480     CYS A  301   SG                                                  
REMARK 480     ARG A  309   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A  325   CD   CE   NZ                                        
REMARK 480     VAL A  344   CG1  CG2                                            
REMARK 480     VAL A  346   CG1  CG2                                            
REMARK 480     ASN A  347   CG   OD1  ND2                                       
REMARK 480     GLN A  374   CG   CD   OE1  NE2                                  
REMARK 480     ARG A  382   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU A  418   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  440   CD   CE   NZ                                        
REMARK 480     ILE A  459   CG1  CG2  CD1                                       
REMARK 480     LEU A  473   CG   CD1  CD2                                       
REMARK 480     GLU A  494   CG   CD   OE1  OE2                                  
REMARK 480     ASN A  497   CG   OD1  ND2                                       
REMARK 480     ARG A  502   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ASP A  520   CG   OD1  OD2                                       
REMARK 480     ASN A  521   CG   OD1  ND2                                       
REMARK 480     LEU A  523   CG   CD1  CD2                                       
REMARK 480     ARG A  524   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU A  525   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  532   CG   CD   CE   NZ                                   
REMARK 480     LEU A  540   CG   CD1  CD2                                       
REMARK 480     GLU A  542   CG   CD   OE1  OE2                                  
REMARK 480     GLN A  546   CD   OE1  NE2                                       
REMARK 480     LYS A  621   CG   CD   CE   NZ                                   
REMARK 480     LYS A  724   CD   CE   NZ                                        
REMARK 480     ASP A  725   CG   OD1  OD2                                       
REMARK 480     LYS A  733   CG   CD   CE   NZ                                   
REMARK 480     GLN A  795   CD   OE1  NE2                                       
REMARK 480     LEU A  877   CG   CD1  CD2                                       
REMARK 480     GLN A  879   CG   CD   OE1  NE2                                  
REMARK 480     LEU A  881   CG   CD1  CD2                                       
REMARK 480     LYS A  886   CG   CD   CE   NZ                                   
REMARK 480     ASN A  918   CG   OD1  ND2                                       
REMARK 480     ARG A  949   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS A  966   CD   CE   NZ                                        
REMARK 480     GLU A  970   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  973   CD   CE   NZ                                        
REMARK 480     ARG A  975   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU A  982   CG   CD   OE1  OE2                                  
REMARK 480     ILE A 1022   CD1                                                 
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    PHE A 261       67.54   -114.42                                   
REMARK 500    VAL A 329       43.68   -104.09                                   
REMARK 500    LEU A 339      -70.95    -85.35                                   
REMARK 500    GLU A 469       58.08    -97.52                                   
REMARK 500    ASN A 521       44.33    -96.94                                   
REMARK 500    GLU A 522       50.82   -141.40                                   
REMARK 500    GLN A 721      -59.22   -126.68                                   
REMARK 500    ASP A 725       69.82   -100.35                                   
REMARK 500    ASN A 756      100.75   -160.75                                   
REMARK 500    LEU A 938     -146.30     62.95                                   
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 5H5 A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1102                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DXU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DXH   RELATED DB: PDB                                   
DBREF  5DXT A  107  1068  UNP    P42336   PK3CA_HUMAN    107   1068             
SEQRES   1 A  962  ASN ARG GLU GLU LYS ILE LEU ASN ARG GLU ILE GLY PHE          
SEQRES   2 A  962  ALA ILE GLY MET PRO VAL CYS GLU PHE ASP MET VAL LYS          
SEQRES   3 A  962  ASP PRO GLU VAL GLN ASP PHE ARG ARG ASN ILE LEU ASN          
SEQRES   4 A  962  VAL CYS LYS GLU ALA VAL ASP LEU ARG ASP LEU ASN SER          
SEQRES   5 A  962  PRO HIS SER ARG ALA MET TYR VAL TYR PRO PRO ASN VAL          
SEQRES   6 A  962  GLU SER SER PRO GLU LEU PRO LYS HIS ILE TYR ASN LYS          
SEQRES   7 A  962  LEU ASP LYS GLY GLN ILE ILE VAL VAL ILE TRP VAL ILE          
SEQRES   8 A  962  VAL SER PRO ASN ASN ASP LYS GLN LYS TYR THR LEU LYS          
SEQRES   9 A  962  ILE ASN HIS ASP CYS VAL PRO GLU GLN VAL ILE ALA GLU          
SEQRES  10 A  962  ALA ILE ARG LYS LYS THR ARG SER MET LEU LEU SER SER          
SEQRES  11 A  962  GLU GLN LEU LYS LEU CYS VAL LEU GLU TYR GLN GLY LYS          
SEQRES  12 A  962  TYR ILE LEU LYS VAL CYS GLY CYS ASP GLU TYR PHE LEU          
SEQRES  13 A  962  GLU LYS TYR PRO LEU SER GLN TYR LYS TYR ILE ARG SER          
SEQRES  14 A  962  CYS ILE MET LEU GLY ARG MET PRO ASN LEU MET LEU MET          
SEQRES  15 A  962  ALA LYS GLU SER LEU TYR SER GLN LEU PRO MET ASP CYS          
SEQRES  16 A  962  PHE THR MET PRO SER TYR SER ARG ARG ILE SER THR ALA          
SEQRES  17 A  962  THR PRO TYR MET ASN GLY GLU THR SER THR LYS SER LEU          
SEQRES  18 A  962  TRP VAL ILE ASN SER ALA LEU ARG ILE LYS ILE LEU CYS          
SEQRES  19 A  962  ALA THR TYR VAL ASN VAL ASN ILE ARG ASP ILE ASP LYS          
SEQRES  20 A  962  ILE TYR VAL ARG THR GLY ILE TYR HIS GLY GLY GLU PRO          
SEQRES  21 A  962  LEU CYS ASP ASN VAL ASN THR GLN ARG VAL PRO CYS SER          
SEQRES  22 A  962  ASN PRO ARG TRP ASN GLU TRP LEU ASN TYR ASP ILE TYR          
SEQRES  23 A  962  ILE PRO ASP LEU PRO ARG ALA ALA ARG LEU CYS LEU SER          
SEQRES  24 A  962  ILE CYS SER VAL LYS GLY ARG LYS GLY ALA LYS GLU GLU          
SEQRES  25 A  962  HIS CYS PRO LEU ALA TRP GLY ASN ILE ASN LEU PHE ASP          
SEQRES  26 A  962  TYR THR ASP THR LEU VAL SER GLY LYS MET ALA LEU ASN          
SEQRES  27 A  962  LEU TRP PRO VAL PRO HIS GLY LEU GLU ASP LEU LEU ASN          
SEQRES  28 A  962  PRO ILE GLY VAL THR GLY SER ASN PRO ASN LYS GLU THR          
SEQRES  29 A  962  PRO CYS LEU GLU LEU GLU PHE ASP TRP PHE SER SER VAL          
SEQRES  30 A  962  VAL LYS PHE PRO ASP MET SER VAL ILE GLU GLU HIS ALA          
SEQRES  31 A  962  ASN TRP SER VAL SER ARG GLU ALA GLY PHE SER TYR SER          
SEQRES  32 A  962  HIS ALA GLY LEU SER ASN ARG LEU ALA ARG ASP ASN GLU          
SEQRES  33 A  962  LEU ARG GLU ASN ASP LYS GLU GLN LEU LYS ALA ILE SER          
SEQRES  34 A  962  THR ARG ASP PRO LEU SER GLU ILE THR GLU GLN GLU LYS          
SEQRES  35 A  962  ASP PHE LEU TRP SER HIS ARG HIS TYR CYS VAL THR ILE          
SEQRES  36 A  962  PRO GLU ILE LEU PRO LYS LEU LEU LEU SER VAL LYS TRP          
SEQRES  37 A  962  ASN SER ARG ASP GLU VAL ALA GLN MET TYR CYS LEU VAL          
SEQRES  38 A  962  LYS ASP TRP PRO PRO ILE LYS PRO GLU GLN ALA MET GLU          
SEQRES  39 A  962  LEU LEU ASP CYS ASN TYR PRO ASP PRO MET VAL ARG GLY          
SEQRES  40 A  962  PHE ALA VAL ARG CYS LEU GLU LYS TYR LEU THR ASP ASP          
SEQRES  41 A  962  LYS LEU SER GLN TYR LEU ILE GLN LEU VAL GLN VAL LEU          
SEQRES  42 A  962  LYS TYR GLU GLN TYR LEU ASP ASN LEU LEU VAL ARG PHE          
SEQRES  43 A  962  LEU LEU LYS LYS ALA LEU THR ASN GLN ARG ILE GLY HIS          
SEQRES  44 A  962  PHE PHE PHE TRP HIS LEU LYS SER GLU MET HIS ASN LYS          
SEQRES  45 A  962  THR VAL SER GLN ARG PHE GLY LEU LEU LEU GLU SER TYR          
SEQRES  46 A  962  CYS ARG ALA CYS GLY MET TYR LEU LYS HIS LEU ASN ARG          
SEQRES  47 A  962  GLN VAL GLU ALA MET GLU LYS LEU ILE ASN LEU THR ASP          
SEQRES  48 A  962  ILE LEU LYS GLN GLU LYS LYS ASP GLU THR GLN LYS VAL          
SEQRES  49 A  962  GLN MET LYS PHE LEU VAL GLU GLN MET ARG ARG PRO ASP          
SEQRES  50 A  962  PHE MET ASP ALA LEU GLN GLY PHE LEU SER PRO LEU ASN          
SEQRES  51 A  962  PRO ALA HIS GLN LEU GLY ASN LEU ARG LEU GLU GLU CYS          
SEQRES  52 A  962  ARG ILE MET SER SER ALA LYS ARG PRO LEU TRP LEU ASN          
SEQRES  53 A  962  TRP GLU ASN PRO ASP ILE MET SER GLU LEU LEU PHE GLN          
SEQRES  54 A  962  ASN ASN GLU ILE ILE PHE LYS ASN GLY ASP ASP LEU ARG          
SEQRES  55 A  962  GLN ASP MET LEU THR LEU GLN ILE ILE ARG ILE MET GLU          
SEQRES  56 A  962  ASN ILE TRP GLN ASN GLN GLY LEU ASP LEU ARG MET LEU          
SEQRES  57 A  962  PRO TYR GLY CYS LEU SER ILE GLY ASP CYS VAL GLY LEU          
SEQRES  58 A  962  ILE GLU VAL VAL ARG ASN SER HIS THR ILE MET GLN ILE          
SEQRES  59 A  962  GLN CYS LYS GLY GLY LEU LYS GLY ALA LEU GLN PHE ASN          
SEQRES  60 A  962  SER HIS THR LEU HIS GLN TRP LEU LYS ASP LYS ASN LYS          
SEQRES  61 A  962  GLY GLU ILE TYR ASP ALA ALA ILE ASP LEU PHE THR ARG          
SEQRES  62 A  962  SER CYS ALA GLY TYR CYS VAL ALA THR PHE ILE LEU GLY          
SEQRES  63 A  962  ILE GLY ASP ARG HIS ASN SER ASN ILE MET VAL LYS ASP          
SEQRES  64 A  962  ASP GLY GLN LEU PHE HIS ILE ASP PHE GLY HIS PHE LEU          
SEQRES  65 A  962  ASP HIS LYS LYS LYS LYS PHE GLY TYR LYS ARG GLU ARG          
SEQRES  66 A  962  VAL PRO PHE VAL LEU THR GLN ASP PHE LEU ILE VAL ILE          
SEQRES  67 A  962  SER LYS GLY ALA GLN GLU CYS THR LYS THR ARG GLU PHE          
SEQRES  68 A  962  GLU ARG PHE GLN GLU MET CYS TYR LYS ALA TYR LEU ALA          
SEQRES  69 A  962  ILE ARG GLN HIS ALA ASN LEU PHE ILE ASN LEU PHE SER          
SEQRES  70 A  962  MET MET LEU GLY SER GLY MET PRO GLU LEU GLN SER PHE          
SEQRES  71 A  962  ASP ASP ILE ALA TYR ILE ARG LYS THR LEU ALA LEU ASP          
SEQRES  72 A  962  LYS THR GLU GLN GLU ALA LEU GLU TYR PHE MET LYS GLN          
SEQRES  73 A  962  MET ASN ASP ALA HIS HIS GLY GLY TRP THR THR LYS MET          
SEQRES  74 A  962  ASP TRP ILE PHE HIS THR ILE LYS GLN HIS ALA LEU ASN          
HET    5H5  A1101      28                                                       
HET    EDO  A1102       4                                                       
HETNAM     5H5 (2S)-2-({2-[1-(PROPAN-2-YL)-1H-1,2,4-TRIAZOL-5-YL]-5,6-          
HETNAM   2 5H5  DIHYDROIMIDAZO[1,2-D][1,4]BENZOXAZEPIN-9-YL}OXY)                
HETNAM   3 5H5  PROPANAMIDE                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     5H5 GDC-0326                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  5H5    C19 H22 N6 O3                                                
FORMUL   3  EDO    C2 H6 O2                                                     
FORMUL   4  HOH   *198(H2 O)                                                    
HELIX    1 AA1 ASN A  107  GLY A  122  1                                  16    
HELIX    2 AA2 VAL A  125  MET A  130  1                                   6    
HELIX    3 AA3 ASP A  133  ILE A  143  1                                  11    
HELIX    4 AA4 ILE A  143  LEU A  156  1                                  14    
HELIX    5 AA5 ASN A  157  TYR A  167  1                                  11    
HELIX    6 AA6 PRO A  178  ASN A  183  1                                   6    
HELIX    7 AA7 VAL A  216  SER A  231  1                                  16    
HELIX    8 AA8 PRO A  266  GLN A  269  5                                   4    
HELIX    9 AA9 TYR A  270  GLY A  280  1                                  11    
HELIX   10 AB1 LYS A  290  SER A  295  1                                   6    
HELIX   11 AB2 PRO A  305  ARG A  309  5                                   5    
HELIX   12 AB3 TRP A  328  ILE A  330  5                                   3    
HELIX   13 AB4 PRO A  394  LEU A  396  5                                   3    
HELIX   14 AB5 ASP A  488  GLY A  505  1                                  18    
HELIX   15 AB6 SER A  507  LEU A  513  1                                   7    
HELIX   16 AB7 ARG A  524  THR A  536  1                                  13    
HELIX   17 AB8 THR A  544  HIS A  554  1                                  11    
HELIX   18 AB9 HIS A  554  VAL A  559  1                                   6    
HELIX   19 AC1 THR A  560  GLU A  563  5                                   4    
HELIX   20 AC2 ILE A  564  VAL A  572  1                                   9    
HELIX   21 AC3 SER A  576  ASP A  589  1                                  14    
HELIX   22 AC4 LYS A  594  LEU A  601  1                                   8    
HELIX   23 AC5 ASP A  608  LEU A  623  1                                  16    
HELIX   24 AC6 THR A  624  LEU A  639  1                                  16    
HELIX   25 AC7 LYS A  640  GLU A  642  5                                   3    
HELIX   26 AC8 ASN A  647  ASN A  660  1                                  14    
HELIX   27 AC9 ASN A  660  GLU A  674  1                                  15    
HELIX   28 AD1 VAL A  680  CYS A  695  1                                  16    
HELIX   29 AD2 MET A  697  LYS A  720  1                                  24    
HELIX   30 AD3 THR A  727  ARG A  740  1                                  14    
HELIX   31 AD4 ARG A  741  LEU A  748  1                                   8    
HELIX   32 AD5 MET A  789  LEU A  793  5                                   5    
HELIX   33 AD6 LEU A  807  GLY A  828  1                                  22    
HELIX   34 AD7 ILE A  857  CYS A  862  1                                   6    
HELIX   35 AD8 HIS A  875  ASN A  885  1                                  11    
HELIX   36 AD9 LYS A  886  GLU A  888  5                                   3    
HELIX   37 AE1 ILE A  889  GLY A  912  1                                  24    
HELIX   38 AE2 THR A  957  SER A  965  1                                   9    
HELIX   39 AE3 THR A  974  HIS A  994  1                                  21    
HELIX   40 AE4 HIS A  994  MET A 1004  1                                  11    
HELIX   41 AE5 SER A 1015  LEU A 1026  1                                  12    
HELIX   42 AE6 THR A 1031  HIS A 1048  1                                  18    
SHEET    1 AA1 4 GLN A 205  ASN A 212  0                                        
SHEET    2 AA1 4 GLN A 189  VAL A 196 -1  N  VAL A 192   O  LEU A 209           
SHEET    3 AA1 4 ASN A 284  ALA A 289  1  O  LEU A 285   N  TRP A 195           
SHEET    4 AA1 4 TYR A 250  VAL A 254 -1  N  LYS A 253   O  MET A 286           
SHEET    1 AA2 2 SER A 323  SER A 326  0                                        
SHEET    2 AA2 2 SER A 482  LYS A 485  1  O  VAL A 483   N  SER A 323           
SHEET    1 AA3 4 ARG A 382  TYR A 392  0                                        
SHEET    2 AA3 4 ALA A 333  THR A 342 -1  N  ILE A 336   O  LEU A 387           
SHEET    3 AA3 4 CYS A 472  PHE A 477 -1  O  GLU A 474   N  CYS A 340           
SHEET    4 AA3 4 LYS A 440  ASN A 444 -1  N  MET A 441   O  LEU A 475           
SHEET    1 AA4 3 GLU A 365  PRO A 366  0                                        
SHEET    2 AA4 3 TYR A 355  HIS A 362 -1  N  HIS A 362   O  GLU A 365           
SHEET    3 AA4 3 VAL A 371  ASN A 372 -1  O  VAL A 371   N  THR A 358           
SHEET    1 AA5 5 GLU A 365  PRO A 366  0                                        
SHEET    2 AA5 5 TYR A 355  HIS A 362 -1  N  HIS A 362   O  GLU A 365           
SHEET    3 AA5 5 ALA A 400  SER A 408 -1  O  CYS A 403   N  GLY A 359           
SHEET    4 AA5 5 CYS A 420  ASN A 428 -1  O  LEU A 422   N  ILE A 406           
SHEET    5 AA5 5 TRP A 446  PRO A 447 -1  O  TRP A 446   N  TRP A 424           
SHEET    1 AA6 2 PHE A 751  SER A 753  0                                        
SHEET    2 AA6 2 ASN A 756  LEU A 761 -1  O  LEU A 761   N  PHE A 751           
SHEET    1 AA7 5 ARG A 770  ILE A 771  0                                        
SHEET    2 AA7 5 LEU A 779  GLU A 784 -1  O  TRP A 780   N  ARG A 770           
SHEET    3 AA7 5 ASN A 796  ASN A 803 -1  O  ASN A 797   N  TRP A 783           
SHEET    4 AA7 5 VAL A 845  GLU A 849 -1  O  ILE A 848   N  ILE A 800           
SHEET    5 AA7 5 CYS A 838  GLY A 842 -1  N  LEU A 839   O  LEU A 847           
SHEET    1 AA8 3 SER A 854  THR A 856  0                                        
SHEET    2 AA8 3 ILE A 921  LYS A 924 -1  O  VAL A 923   N  HIS A 855           
SHEET    3 AA8 3 LEU A 929  HIS A 931 -1  O  PHE A 930   N  MET A 922           
SITE     1 AC1 15 SER A 774  TRP A 780  TYR A 836  ILE A 848                    
SITE     2 AC1 15 GLU A 849  VAL A 851  SER A 854  GLN A 859                    
SITE     3 AC1 15 MET A 922  PHE A 930  ILE A 932  ASP A 933                    
SITE     4 AC1 15 EDO A1102  HOH A1205  HOH A1302                               
SITE     1 AC2  4 SER A 774  THR A 856  GLN A 859  5H5 A1101                    
CRYST1   58.507  133.672  141.339  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      0.017092  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007481  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007075        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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