GenomeNet

Database: PDB
Entry: 3QAQ
LinkDB: 3QAQ
Original site: 3QAQ 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       11-JAN-11   3QAQ              
TITLE     CRYSTAL STRUCTURE OF PI3K-GAMMA IN COMPLEX WITH TRIAZINE-BENZIMIDAZOLE
TITLE    2 1                                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT GAMMA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 144-1102);                  
COMPND   6 SYNONYM: PI3-KINASE SUBUNIT GAMMA, PI3K-GAMMA, PTDINS-3-KINASE       
COMPND   7 SUBUNIT GAMMA, PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE 110 KDA
COMPND   8 CATALYTIC SUBUNIT GAMMA, PTDINS-3-KINASE SUBUNIT P110-GAMMA, P120-   
COMPND   9 PI3K;                                                                
COMPND  10 EC: 2.7.1.153;                                                       
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: PIK3CG;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    INHIBITOR, P110, KINASE, TRANSFERASE, ATP BINDING, P84, P101,         
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.WHITTINGTON,J.TANG,P.YAKOWEC                                      
REVDAT   1   30-MAR-11 3QAQ    0                                                
JRNL        AUTH   E.A.PETERSON,P.S.ANDREWS,X.BE,A.A.BOEZIO,T.L.BUSH,A.C.CHENG, 
JRNL        AUTH 2 J.R.COATS,A.E.COLLETTI,K.W.COPELAND,M.DUPONT,R.GRACEFFA,     
JRNL        AUTH 3 B.GRUBINSKA,J.C.HARMANGE,J.L.KIM,E.L.MULLADY,P.OLIVIERI,     
JRNL        AUTH 4 L.B.SCHENKEL,M.K.STANTON,Y.TEFFERA,D.A.WHITTINGTON,T.CAI,    
JRNL        AUTH 5 D.S.LA                                                       
JRNL        TITL   DISCOVERY OF TRIAZINE-BENZIMIDAZOLES AS SELECTIVE INHIBITORS 
JRNL        TITL 2 OF MTOR.                                                     
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  21  2064 2011              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   21376583                                                     
JRNL        DOI    10.1016/J.BMCL.2011.02.007                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 21655                          
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) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1688                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1535                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 133                          
REMARK   3   BIN FREE R VALUE                    : 0.3850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6773                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 13                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 88.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.58000                                             
REMARK   3    B22 (A**2) : 5.10000                                              
REMARK   3    B33 (A**2) : -1.33000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.16000                                              
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): 0.444         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.365         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.009        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6957 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9411 ; 1.032 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   826 ; 5.234 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   323 ;36.239 ;24.303       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1259 ;16.675 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;15.630 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1057 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5156 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2930 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4694 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   173 ; 0.127 ; 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):    29 ; 0.152 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.138 ; 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):  4302 ; 0.579 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6766 ; 1.054 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3027 ; 1.110 ; 4.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2645 ; 1.871 ; 6.000       
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   144        A   245                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9067 -14.1376  27.0035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2448 T22:  -0.2908                                     
REMARK   3      T33:   0.1343 T12:  -0.0362                                     
REMARK   3      T13:  -0.0215 T23:   0.0966                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0286 L22:   1.1203                                     
REMARK   3      L33:   2.5976 L12:  -0.9294                                     
REMARK   3      L13:   0.2793 L23:  -0.2903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1354 S12:  -0.0124 S13:  -1.3484                       
REMARK   3      S21:  -0.0641 S22:   0.1607 S23:   0.5216                       
REMARK   3      S31:   0.2077 S32:  -0.4352 S33:  -0.2960                       
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   269        A   321                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7734 -12.5220  31.3204              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3948 T22:   0.0099                                     
REMARK   3      T33:   0.1868 T12:  -0.1122                                     
REMARK   3      T13:   0.0726 T23:   0.3445                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8388 L22:   3.5567                                     
REMARK   3      L33:   6.6447 L12:  -2.1681                                     
REMARK   3      L13:   0.1028 L23:   1.6511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2565 S12:  -0.7129 S13:  -0.9151                       
REMARK   3      S21:  -0.0656 S22:   0.3647 S23:   0.5880                       
REMARK   3      S31:  -0.0160 S32:  -1.0828 S33:  -0.6212                       
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   351        A   436                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.3361  -5.6387  14.8727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2184 T22:   0.3278                                     
REMARK   3      T33:  -0.1967 T12:   0.0182                                     
REMARK   3      T13:   0.0238 T23:  -0.1119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3464 L22:   3.2965                                     
REMARK   3      L33:   3.9156 L12:   0.4220                                     
REMARK   3      L13:  -1.2308 L23:  -1.7639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0421 S12:   0.3496 S13:   0.0369                       
REMARK   3      S21:   0.0132 S22:   0.0075 S23:  -0.0885                       
REMARK   3      S31:  -0.0269 S32:   0.4857 S33:  -0.0496                       
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   457        A   532                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.6855  -7.9223  13.4539              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1260 T22:   0.2213                                     
REMARK   3      T33:  -0.2092 T12:   0.0386                                     
REMARK   3      T13:   0.0305 T23:  -0.1715                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7874 L22:   2.9825                                     
REMARK   3      L33:   3.2085 L12:  -0.8470                                     
REMARK   3      L13:   0.1611 L23:  -1.0874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0298 S12:   0.6791 S13:  -0.1455                       
REMARK   3      S21:  -0.0189 S22:   0.1614 S23:  -0.0775                       
REMARK   3      S31:  -0.1330 S32:   0.4147 S33:  -0.1912                       
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   546        A   725                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.7465 -10.0782  34.2070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0647 T22:  -0.1337                                     
REMARK   3      T33:  -0.0039 T12:   0.0219                                     
REMARK   3      T13:   0.0331 T23:   0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7012 L22:   0.2939                                     
REMARK   3      L33:   2.4521 L12:  -0.5289                                     
REMARK   3      L13:   2.0768 L23:  -0.0410                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0711 S12:  -0.1097 S13:  -0.4454                       
REMARK   3      S21:   0.0051 S22:   0.0895 S23:   0.1501                       
REMARK   3      S31:  -0.0226 S32:   0.1151 S33:  -0.1606                       
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   726        A   885                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6045   5.2738  17.4245              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0649 T22:  -0.0376                                     
REMARK   3      T33:  -0.0816 T12:   0.0828                                     
REMARK   3      T13:   0.0264 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1065 L22:   2.2514                                     
REMARK   3      L33:   1.8408 L12:  -1.1393                                     
REMARK   3      L13:   1.2327 L23:  -0.6581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0230 S12:   0.3428 S13:  -0.1016                       
REMARK   3      S21:  -0.1161 S22:   0.0892 S23:   0.3045                       
REMARK   3      S31:  -0.3591 S32:  -0.1398 S33:  -0.1122                       
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 :   A   886        A  1088                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.1375  19.3666  37.5296              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2747 T22:  -0.1842                                     
REMARK   3      T33:  -0.0560 T12:   0.1779                                     
REMARK   3      T13:  -0.1539 T23:  -0.1741                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7400 L22:   2.4015                                     
REMARK   3      L33:   1.7021 L12:  -0.9990                                     
REMARK   3      L13:   1.6858 L23:  -0.3280                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7785 S12:  -0.4775 S13:   0.8984                       
REMARK   3      S21:   0.4860 S22:   0.1630 S23:  -0.2034                       
REMARK   3      S31:  -0.6378 S32:  -0.1593 S33:   0.6155                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3QAQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063407.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23346                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1E8Y                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG 3350, 0.1 M TRIS PH 7.3, 245     
REMARK 280  MM AMMONIUM SULFATE, 5 MM EDTA, VAPOR DIFFUSION, TEMPERATURE 298K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       72.69750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.28950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       72.69750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.28950            
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     GLY A   143                                                      
REMARK 465     PHE A   249                                                      
REMARK 465     THR A   250                                                      
REMARK 465     LYS A   251                                                      
REMARK 465     MET A   252                                                      
REMARK 465     ALA A   253                                                      
REMARK 465     LYS A   254                                                      
REMARK 465     LYS A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     SER A   257                                                      
REMARK 465     LEU A   258                                                      
REMARK 465     MET A   259                                                      
REMARK 465     ASP A   260                                                      
REMARK 465     ILE A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     GLU A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     GLN A   265                                                      
REMARK 465     SER A   266                                                      
REMARK 465     GLU A   267                                                      
REMARK 465     GLN A   268                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     TRP A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     LEU A   325                                                      
REMARK 465     VAL A   326                                                      
REMARK 465     ASP A   327                                                      
REMARK 465     ASP A   328                                                      
REMARK 465     CYS A   329                                                      
REMARK 465     THR A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     VAL A   332                                                      
REMARK 465     THR A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     TYR A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     GLN A   338                                                      
REMARK 465     LEU A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     ASP A   345                                                      
REMARK 465     HIS A   346                                                      
REMARK 465     GLU A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     VAL A   349                                                      
REMARK 465     PHE A   350                                                      
REMARK 465     PRO A   374                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     ASN A   376                                                      
REMARK 465     THR A   377                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     ALA A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 465     ALA A   440                                                      
REMARK 465     LEU A   441                                                      
REMARK 465     SER A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     ALA A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     ALA A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     SER A   449                                                      
REMARK 465     PRO A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     SER A   452                                                      
REMARK 465     GLU A   453                                                      
REMARK 465     SER A   454                                                      
REMARK 465     LYS A   455                                                      
REMARK 465     GLY A   456                                                      
REMARK 465     GLY A   489                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     GLY A   491                                                      
REMARK 465     GLU A   492                                                      
REMARK 465     ASP A   493                                                      
REMARK 465     GLN A   494                                                      
REMARK 465     GLY A   495                                                      
REMARK 465     TYR A   523                                                      
REMARK 465     CYS A   524                                                      
REMARK 465     PRO A   534                                                      
REMARK 465     THR A   535                                                      
REMARK 465     PRO A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     PRO A   538                                                      
REMARK 465     GLU A   539                                                      
REMARK 465     GLY A   540                                                      
REMARK 465     ASP A   541                                                      
REMARK 465     ARG A   542                                                      
REMARK 465     GLU A   755                                                      
REMARK 465     LYS A   756                                                      
REMARK 465     TYR A   757                                                      
REMARK 465     ASN A   898                                                      
REMARK 465     THR A   899                                                      
REMARK 465     ILE A   968                                                      
REMARK 465     LEU A   969                                                      
REMARK 465     GLY A   970                                                      
REMARK 465     ASN A   971                                                      
REMARK 465     TYR A   972                                                      
REMARK 465     LYS A   973                                                      
REMARK 465     SER A   974                                                      
REMARK 465     PHE A   975                                                      
REMARK 465     LEU A   976                                                      
REMARK 465     GLY A   977                                                      
REMARK 465     ILE A   978                                                      
REMARK 465     ASN A   979                                                      
REMARK 465     HIS A  1089                                                      
REMARK 465     LEU A  1090                                                      
REMARK 465     VAL A  1091                                                      
REMARK 465     LEU A  1092                                                      
REMARK 465     GLY A  1093                                                      
REMARK 465     ILE A  1094                                                      
REMARK 465     LYS A  1095                                                      
REMARK 465     GLN A  1096                                                      
REMARK 465     GLY A  1097                                                      
REMARK 465     GLU A  1098                                                      
REMARK 465     LYS A  1099                                                      
REMARK 465     HIS A  1100                                                      
REMARK 465     SER A  1101                                                      
REMARK 465     ALA A  1102                                                      
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     HIS A 525    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 980    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP A 904   CG    ASP A 904   OD1     0.142                       
REMARK 500    ASP A 904   CG    ASP A 904   OD2     0.178                       
REMARK 500    GLU A 905   CD    GLU A 905   OE1     0.095                       
REMARK 500    GLU A 905   CD    GLU A 905   OE2     0.081                       
REMARK 500    GLU A 918   CD    GLU A 918   OE1     0.342                       
REMARK 500    GLU A 918   CD    GLU A 918   OE2     0.114                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A 918   OE1 -  CD  -  OE2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 145     -107.08    -80.75                                   
REMARK 500    ASN A 167       56.70   -116.16                                   
REMARK 500    HIS A 169       18.32   -145.92                                   
REMARK 500    ASP A 170     -165.76   -164.54                                   
REMARK 500    HIS A 199       48.60     34.71                                   
REMARK 500    ARG A 226      -80.95    -92.61                                   
REMARK 500    SER A 227      -81.58   -135.22                                   
REMARK 500    PRO A 241      -39.36    -39.18                                   
REMARK 500    TRP A 410      -38.38   -130.87                                   
REMARK 500    ALA A 545       11.15   -145.54                                   
REMARK 500    PRO A 548      170.95    -50.10                                   
REMARK 500    ARG A 579      -60.32    -13.05                                   
REMARK 500    ARG A 613       57.49   -116.82                                   
REMARK 500    GLN A 705       20.97   -145.14                                   
REMARK 500    ARG A 722        5.08    -69.58                                   
REMARK 500    VAL A 759       80.50    -67.63                                   
REMARK 500    ALA A 805       45.42    -78.92                                   
REMARK 500    SER A 859       17.26     59.87                                   
REMARK 500    VAL A 896      -99.24   -110.89                                   
REMARK 500    THR A 917     -159.04   -114.38                                   
REMARK 500    PHE A 961      137.81   -175.15                                   
REMARK 500    ASP A 964       78.37     46.79                                   
REMARK 500    PHE A 965       33.98    -94.64                                   
REMARK 500    LYS A1000       77.58   -158.34                                   
REMARK 500    GLN A1041        6.50   -150.07                                   
REMARK 500    ARG A1076       52.61    -99.72                                   
REMARK 500    ASP A1077      -30.33   -156.00                                   
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 SO4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QAQ A 1103                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QAR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PI3K-GAMMA IN COMPLEX WITH TRIAZINE-            
REMARK 900 BENZIMIDAZOLE 32                                                     
DBREF  3QAQ A  144  1102  UNP    P48736   PK3CG_HUMAN    144   1102             
SEQADV 3QAQ GLY A  143  UNP  P48736              EXPRESSION TAG                 
SEQRES   1 A  960  GLY SER GLU GLU SER GLN ALA PHE GLN ARG GLN LEU THR          
SEQRES   2 A  960  ALA LEU ILE GLY TYR ASP VAL THR ASP VAL SER ASN VAL          
SEQRES   3 A  960  HIS ASP ASP GLU LEU GLU PHE THR ARG ARG GLY LEU VAL          
SEQRES   4 A  960  THR PRO ARG MET ALA GLU VAL ALA SER ARG ASP PRO LYS          
SEQRES   5 A  960  LEU TYR ALA MET HIS PRO TRP VAL THR SER LYS PRO LEU          
SEQRES   6 A  960  PRO GLU TYR LEU TRP LYS LYS ILE ALA ASN ASN CYS ILE          
SEQRES   7 A  960  PHE ILE VAL ILE HIS ARG SER THR THR SER GLN THR ILE          
SEQRES   8 A  960  LYS VAL SER PRO ASP ASP THR PRO GLY ALA ILE LEU GLN          
SEQRES   9 A  960  SER PHE PHE THR LYS MET ALA LYS LYS LYS SER LEU MET          
SEQRES  10 A  960  ASP ILE PRO GLU SER GLN SER GLU GLN ASP PHE VAL LEU          
SEQRES  11 A  960  ARG VAL CYS GLY ARG ASP GLU TYR LEU VAL GLY GLU THR          
SEQRES  12 A  960  PRO ILE LYS ASN PHE GLN TRP VAL ARG HIS CYS LEU LYS          
SEQRES  13 A  960  ASN GLY GLU GLU ILE HIS VAL VAL LEU ASP THR PRO PRO          
SEQRES  14 A  960  ASP PRO ALA LEU ASP GLU VAL ARG LYS GLU GLU TRP PRO          
SEQRES  15 A  960  LEU VAL ASP ASP CYS THR GLY VAL THR GLY TYR HIS GLU          
SEQRES  16 A  960  GLN LEU THR ILE HIS GLY LYS ASP HIS GLU SER VAL PHE          
SEQRES  17 A  960  THR VAL SER LEU TRP ASP CYS ASP ARG LYS PHE ARG VAL          
SEQRES  18 A  960  LYS ILE ARG GLY ILE ASP ILE PRO VAL LEU PRO ARG ASN          
SEQRES  19 A  960  THR ASP LEU THR VAL PHE VAL GLU ALA ASN ILE GLN HIS          
SEQRES  20 A  960  GLY GLN GLN VAL LEU CYS GLN ARG ARG THR SER PRO LYS          
SEQRES  21 A  960  PRO PHE THR GLU GLU VAL LEU TRP ASN VAL TRP LEU GLU          
SEQRES  22 A  960  PHE SER ILE LYS ILE LYS ASP LEU PRO LYS GLY ALA LEU          
SEQRES  23 A  960  LEU ASN LEU GLN ILE TYR CYS GLY LYS ALA PRO ALA LEU          
SEQRES  24 A  960  SER SER LYS ALA SER ALA GLU SER PRO SER SER GLU SER          
SEQRES  25 A  960  LYS GLY LYS VAL GLN LEU LEU TYR TYR VAL ASN LEU LEU          
SEQRES  26 A  960  LEU ILE ASP HIS ARG PHE LEU LEU ARG ARG GLY GLU TYR          
SEQRES  27 A  960  VAL LEU HIS MET TRP GLN ILE SER GLY LYS GLY GLU ASP          
SEQRES  28 A  960  GLN GLY SER PHE ASN ALA ASP LYS LEU THR SER ALA THR          
SEQRES  29 A  960  ASN PRO ASP LYS GLU ASN SER MET SER ILE SER ILE LEU          
SEQRES  30 A  960  LEU ASP ASN TYR CYS HIS PRO ILE ALA LEU PRO LYS HIS          
SEQRES  31 A  960  GLN PRO THR PRO ASP PRO GLU GLY ASP ARG VAL ARG ALA          
SEQRES  32 A  960  GLU MET PRO ASN GLN LEU ARG LYS GLN LEU GLU ALA ILE          
SEQRES  33 A  960  ILE ALA THR ASP PRO LEU ASN PRO LEU THR ALA GLU ASP          
SEQRES  34 A  960  LYS GLU LEU LEU TRP HIS PHE ARG TYR GLU SER LEU LYS          
SEQRES  35 A  960  HIS PRO LYS ALA TYR PRO LYS LEU PHE SER SER VAL LYS          
SEQRES  36 A  960  TRP GLY GLN GLN GLU ILE VAL ALA LYS THR TYR GLN LEU          
SEQRES  37 A  960  LEU ALA ARG ARG GLU VAL TRP ASP GLN SER ALA LEU ASP          
SEQRES  38 A  960  VAL GLY LEU THR MET GLN LEU LEU ASP CYS ASN PHE SER          
SEQRES  39 A  960  ASP GLU ASN VAL ARG ALA ILE ALA VAL GLN LYS LEU GLU          
SEQRES  40 A  960  SER LEU GLU ASP ASP ASP VAL LEU HIS TYR LEU LEU GLN          
SEQRES  41 A  960  LEU VAL GLN ALA VAL LYS PHE GLU PRO TYR HIS ASP SER          
SEQRES  42 A  960  ALA LEU ALA ARG PHE LEU LEU LYS ARG GLY LEU ARG ASN          
SEQRES  43 A  960  LYS ARG ILE GLY HIS PHE LEU PHE TRP PHE LEU ARG SER          
SEQRES  44 A  960  GLU ILE ALA GLN SER ARG HIS TYR GLN GLN ARG PHE ALA          
SEQRES  45 A  960  VAL ILE LEU GLU ALA TYR LEU ARG GLY CYS GLY THR ALA          
SEQRES  46 A  960  MET LEU HIS ASP PHE THR GLN GLN VAL GLN VAL ILE GLU          
SEQRES  47 A  960  MET LEU GLN LYS VAL THR LEU ASP ILE LYS SER LEU SER          
SEQRES  48 A  960  ALA GLU LYS TYR ASP VAL SER SER GLN VAL ILE SER GLN          
SEQRES  49 A  960  LEU LYS GLN LYS LEU GLU ASN LEU GLN ASN SER GLN LEU          
SEQRES  50 A  960  PRO GLU SER PHE ARG VAL PRO TYR ASP PRO GLY LEU LYS          
SEQRES  51 A  960  ALA GLY ALA LEU ALA ILE GLU LYS CYS LYS VAL MET ALA          
SEQRES  52 A  960  SER LYS LYS LYS PRO LEU TRP LEU GLU PHE LYS CYS ALA          
SEQRES  53 A  960  ASP PRO THR ALA LEU SER ASN GLU THR ILE GLY ILE ILE          
SEQRES  54 A  960  PHE LYS HIS GLY ASP ASP LEU ARG GLN ASP MET LEU ILE          
SEQRES  55 A  960  LEU GLN ILE LEU ARG ILE MET GLU SER ILE TRP GLU THR          
SEQRES  56 A  960  GLU SER LEU ASP LEU CYS LEU LEU PRO TYR GLY CYS ILE          
SEQRES  57 A  960  SER THR GLY ASP LYS ILE GLY MET ILE GLU ILE VAL LYS          
SEQRES  58 A  960  ASP ALA THR THR ILE ALA LYS ILE GLN GLN SER THR VAL          
SEQRES  59 A  960  GLY ASN THR GLY ALA PHE LYS ASP GLU VAL LEU ASN HIS          
SEQRES  60 A  960  TRP LEU LYS GLU LYS SER PRO THR GLU GLU LYS PHE GLN          
SEQRES  61 A  960  ALA ALA VAL GLU ARG PHE VAL TYR SER CYS ALA GLY TYR          
SEQRES  62 A  960  CYS VAL ALA THR PHE VAL LEU GLY ILE GLY ASP ARG HIS          
SEQRES  63 A  960  ASN ASP ASN ILE MET ILE THR GLU THR GLY ASN LEU PHE          
SEQRES  64 A  960  HIS ILE ASP PHE GLY HIS ILE LEU GLY ASN TYR LYS SER          
SEQRES  65 A  960  PHE LEU GLY ILE ASN LYS GLU ARG VAL PRO PHE VAL LEU          
SEQRES  66 A  960  THR PRO ASP PHE LEU PHE VAL MET GLY THR SER GLY LYS          
SEQRES  67 A  960  LYS THR SER PRO HIS PHE GLN LYS PHE GLN ASP ILE CYS          
SEQRES  68 A  960  VAL LYS ALA TYR LEU ALA LEU ARG HIS HIS THR ASN LEU          
SEQRES  69 A  960  LEU ILE ILE LEU PHE SER MET MET LEU MET THR GLY MET          
SEQRES  70 A  960  PRO GLN LEU THR SER LYS GLU ASP ILE GLU TYR ILE ARG          
SEQRES  71 A  960  ASP ALA LEU THR VAL GLY LYS ASN GLU GLU ASP ALA LYS          
SEQRES  72 A  960  LYS TYR PHE LEU ASP GLN ILE GLU VAL CYS ARG ASP LYS          
SEQRES  73 A  960  GLY TRP THR VAL GLN PHE ASN TRP PHE LEU HIS LEU VAL          
SEQRES  74 A  960  LEU GLY ILE LYS GLN GLY GLU LYS HIS SER ALA                  
HET    SO4  A   1       5                                                       
HET    SO4  A   2       5                                                       
HET    SO4  A   3       5                                                       
HET    QAQ  A1103      27                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     QAQ [(4-{2-[(3-HYDROXYPHENYL)AMINO]-1H-BENZIMIDAZOL-1-YL}-           
HETNAM   2 QAQ  1,3,5-TRIAZIN-2-YL)AMINO]ACETONITRILE                           
HETSYN     QAQ 2-(4-(2-(3-HYDROXYPHENYLAMINO)-1H-BENZO[D]IMIDAZOL-1-            
HETSYN   2 QAQ  YL)-1,3,5-TRIAZIN-2-YLAMINO)ACETONITRILE                        
FORMUL   2  SO4    3(O4 S 2-)                                                   
FORMUL   5  QAQ    C18 H14 N8 O                                                 
FORMUL   6  HOH   *13(H2 O)                                                     
HELIX    1   1 GLU A  146  GLY A  159  1                                  14    
HELIX    2   2 ASP A  171  ARG A  191  1                                  21    
HELIX    3   3 LYS A  194  HIS A  199  1                                   6    
HELIX    4   4 PRO A  208  LYS A  213  1                                   6    
HELIX    5   5 PRO A  241  GLN A  246  1                                   6    
HELIX    6   6 PRO A  286  ASN A  289  5                                   4    
HELIX    7   7 PHE A  290  GLY A  300  1                                  11    
HELIX    8   8 ASP A  312  GLU A  317  5                                   6    
HELIX    9   9 TRP A  355  CYS A  357  5                                   3    
HELIX   10  10 LYS A  421  LEU A  423  5                                   3    
HELIX   11  11 ASN A  498  THR A  503  5                                   6    
HELIX   12  12 PRO A  548  ALA A  560  1                                  13    
HELIX   13  13 THR A  568  PHE A  578  1                                  11    
HELIX   14  14 PHE A  578  LEU A  583  1                                   6    
HELIX   15  15 LYS A  584  LYS A  587  5                                   4    
HELIX   16  16 ALA A  588  SER A  594  1                                   7    
HELIX   17  17 GLN A  600  ALA A  612  1                                  13    
HELIX   18  18 ARG A  614  SER A  620  1                                   7    
HELIX   19  19 ASP A  623  LEU A  631  1                                   9    
HELIX   20  20 ASP A  637  GLU A  649  1                                  13    
HELIX   21  21 GLU A  652  ALA A  666  1                                  15    
HELIX   22  22 VAL A  667  GLU A  670  5                                   4    
HELIX   23  23 SER A  675  ARG A  687  1                                  13    
HELIX   24  24 ASN A  688  ALA A  704  1                                  17    
HELIX   25  25 TYR A  709  ARG A  722  1                                  14    
HELIX   26  26 GLY A  725  LEU A  752  1                                  28    
HELIX   27  27 SER A  760  LEU A  774  1                                  15    
HELIX   28  28 ILE A  798  CYS A  801  5                                   4    
HELIX   29  29 ASP A  837  THR A  857  1                                  21    
HELIX   30  30 ILE A  888  VAL A  896  1                                   9    
HELIX   31  31 GLU A  905  GLU A  913  1                                   9    
HELIX   32  32 GLU A  918  GLY A  943  1                                  26    
HELIX   33  33 THR A  988  GLY A  996  1                                   9    
HELIX   34  34 SER A 1003  HIS A 1022  1                                  20    
HELIX   35  35 HIS A 1023  MET A 1039  1                                  17    
HELIX   36  36 SER A 1044  LEU A 1055  1                                  12    
HELIX   37  37 ASN A 1060  GLY A 1079  1                                  20    
HELIX   38  38 TRP A 1080  PHE A 1087  1                                   8    
SHEET    1   A 4 SER A 230  VAL A 235  0                                        
SHEET    2   A 4 ILE A 220  HIS A 225 -1  N  ILE A 220   O  VAL A 235           
SHEET    3   A 4 ILE A 303  ASP A 308  1  O  VAL A 305   N  VAL A 223           
SHEET    4   A 4 VAL A 271  VAL A 274 -1  N  VAL A 271   O  ASP A 308           
SHEET    1   B 2 VAL A 352  SER A 353  0                                        
SHEET    2   B 2 ILE A 527  ALA A 528  1  O  ALA A 528   N  VAL A 352           
SHEET    1   C 4 GLU A 407  LYS A 419  0                                        
SHEET    2   C 4 LYS A 360  ASP A 369 -1  N  PHE A 361   O  PHE A 416           
SHEET    3   C 4 SER A 515  LEU A 520 -1  O  SER A 515   N  ASP A 369           
SHEET    4   C 4 GLY A 478  HIS A 483 -1  N  GLY A 478   O  LEU A 520           
SHEET    1   D 3 GLN A 392  ARG A 398  0                                        
SHEET    2   D 3 THR A 380  HIS A 389 -1  N  ILE A 387   O  CYS A 395           
SHEET    3   D 3 LYS A 402  PRO A 403 -1  O  LYS A 402   N  VAL A 381           
SHEET    1   E 4 GLN A 392  ARG A 398  0                                        
SHEET    2   E 4 THR A 380  HIS A 389 -1  N  ILE A 387   O  CYS A 395           
SHEET    3   E 4 LEU A 428  GLY A 436 -1  O  GLN A 432   N  GLU A 384           
SHEET    4   E 4 GLN A 459  LEU A 467 -1  O  LEU A 466   N  LEU A 429           
SHEET    1   F 4 PHE A 783  VAL A 785  0                                        
SHEET    2   F 4 ASP A 788  LEU A 796 -1  O  ALA A 793   N  PHE A 783           
SHEET    3   F 4 LEU A 811  CYS A 817 -1  O  LYS A 816   N  GLY A 794           
SHEET    4   F 4 LYS A 802  VAL A 803 -1  N  LYS A 802   O  TRP A 812           
SHEET    1   G 6 PHE A 783  VAL A 785  0                                        
SHEET    2   G 6 ASP A 788  LEU A 796 -1  O  ALA A 793   N  PHE A 783           
SHEET    3   G 6 LEU A 811  CYS A 817 -1  O  LYS A 816   N  GLY A 794           
SHEET    4   G 6 ILE A 828  HIS A 834 -1  O  ILE A 828   N  PHE A 815           
SHEET    5   G 6 ILE A 876  GLU A 880 -1  O  ILE A 879   N  ILE A 831           
SHEET    6   G 6 CYS A 869  GLY A 873 -1  N  ILE A 870   O  MET A 878           
SHEET    1   H 3 ALA A 885  THR A 887  0                                        
SHEET    2   H 3 ILE A 952  THR A 955 -1  O  ILE A 954   N  THR A 886           
SHEET    3   H 3 LEU A 960  HIS A 962 -1  O  PHE A 961   N  MET A 953           
CISPEP   1 SER A  777    GLN A  778          0        -4.51                     
CISPEP   2 ALA A  901    PHE A  902          0       -15.26                     
SITE     1 AC1  4 PRO A 206  LEU A 207  TRP A 212  LYS A 288                    
SITE     1 AC2  5 ARG A 544  GLU A 546  TRP A 576  ARG A 579                    
SITE     2 AC2  5 LYS A 606                                                     
SITE     1 AC3  5 LEU A 657  PHE A 694  PHE A 698  GLN A 846                    
SITE     2 AC3  5 ARG A 849                                                     
SITE     1 AC4 13 MET A 804  TRP A 812  ILE A 831  ASP A 841                    
SITE     2 AC4 13 TYR A 867  GLU A 880  ILE A 881  VAL A 882                    
SITE     3 AC4 13 ASP A 884  ALA A 885  MET A 953  ILE A 963                    
SITE     4 AC4 13 ASP A 964                                                     
CRYST1  145.395   68.579  106.501  90.00  94.69  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006878  0.000000  0.000564        0.00000                         
SCALE2      0.000000  0.014582  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009421        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system