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Database: PDB
Entry: 4ANX
LinkDB: 4ANX
Original site: 4ANX 
HEADER    TRANSFERASE                             22-MAR-12   4ANX              
TITLE     COMPLEXES OF PI3KGAMMA WITH ISOFORM SELECTIVE INHIBITORS.             
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 SUBUNIT GAMMA, RESIDUES 144-1102;                
COMPND   6 SYNONYM: PI3-KINASE SUBUNIT GAMMA, PI3K-GAMMA, PI3KGAMMA, PTDINS-3-  
COMPND   7 KINASE SUBUNIT GAMMA, PHOSPHATIDYLINOSITOL-4\,5-BISPHOSPHATE 3-KINASE
COMPND   8 110 KDA CATALYTIC SUBUNIT GAMMA, PTDINS-3-KINASE SUBUNIT P110-GAMMA, 
COMPND   9 P110GAMMA, PHOSPHOINOSITIDE-3-KINASE CATALYTIC GAMMA POLYPEPTIDE,    
COMPND  10 SERINE/THREONINE PROTEIN KINASE PIK3CG, P120-PI3K;                   
COMPND  11 EC: 2.7.1.137, 2.7.1.153, 2.7.11.1;                                  
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.G.FOSTER,J.C.LOUGHEED                                               
REVDAT   3   08-MAY-19 4ANX    1       REMARK                                   
REVDAT   2   27-JUN-12 4ANX    1       JRNL                                     
REVDAT   1   09-MAY-12 4ANX    0                                                
JRNL        AUTH   J.W.LEAHY,C.A.BUHR,H.W.B.JOHNSON,B.G.KIM,T.BAIK,J.CANNOY,    
JRNL        AUTH 2 T.P.FORSYTH,J.W.JEONG,M.S.LEE,S.MA,K.NOSON,L.WANG,           
JRNL        AUTH 3 M.WILLIAMS,J.M.NUSS,E.BROOKS,N.HEALD,C.HOLST,C.JAEGER,S.LAM, 
JRNL        AUTH 4 J.C.LOUGHEED,L.NGUYEN,A.PLONOWSKI,T.STOUT,P.G.FOSTER,X.WU,   
JRNL        AUTH 5 M.F.YAKES,R.YU,W.ZHANG,P.LAMB,O.RAEBER                       
JRNL        TITL   THE DISCOVERY OF A NOVEL SERIES OF POTENT AND ORALLY         
JRNL        TITL 2 BIOAVAILABLE PHOSPHOINOSITIDE 3-KINASE GAMMA INHIBITORS      
JRNL        REF    J.MED.CHEM.                   V.  55  5467 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22548342                                                     
JRNL        DOI    10.1021/JM300403A                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.73 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.73                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 26019                          
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) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1375                            
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) : 2.73                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.80                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1900                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.30                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.3860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6757                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 34                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.03000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.07000                                              
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): 0.402         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.360         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.206        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6942 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4766 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9393 ; 1.601 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11597 ; 0.996 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   826 ; 7.916 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   328 ;37.075 ;24.329       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1260 ;19.999 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;15.206 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1051 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7557 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1378 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1952 ; 0.260 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5161 ; 0.217 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3376 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3774 ; 0.093 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   240 ; 0.196 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     6 ; 0.098 ; 0.200       
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):    21 ; 0.137 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    27 ; 0.245 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.085 ; 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):  4331 ; 0.943 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1667 ; 0.081 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6743 ; 1.277 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3059 ; 1.682 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2650 ; 2.409 ; 4.500       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 4ANX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290051745.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 155                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27406                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.730                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.73                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: IN-HOUSE PI3KG STRUCTURE                             
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN AT 19C IN HANGING    
REMARK 280  DROPS USING VAPOR DIFFUSION. THE COMPLEX WAS FORMED BY              
REMARK 280  INCUBATING 49.5UL OF PI3KG-HIS6 (7.2 MG/ML IN 20 MM TRIS-HCL, PH    
REMARK 280  7.2, 50 MM (NH4)2SO4, AND 1 MM TCEP) WITH 0.5UL OF LIGAND (100      
REMARK 280  MM STOCK IN 100% DMSO) FOR 30 MINUTES AT 4C. CRYSTALS OF THE        
REMARK 280  BINARY COMPLEX WERE OBTAINED BY MIXING 1.0UL OF THE PI3KG:          
REMARK 280  INHIBITOR COMPLEX WITH 1.0UL OF A RESERVOIR SOLUTION CONSISTING     
REMARK 280  OF 16-21% PEG 4K, 0.25 M (NH4)2SO4, AND 0.1 M TRIS-HCL, PH 7.5.,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K                     
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       71.71200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.26550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.71200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.26550            
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     MET A   139                                                      
REMARK 465     LEU A   140                                                      
REMARK 465     LEU A   141                                                      
REMARK 465     GLY A   142                                                      
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   322                                                      
REMARK 465     TRP A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     LEU A   325                                                      
REMARK 465     VAL A   326                                                      
REMARK 465     ASP A   327                                                      
REMARK 465     ASP A   328                                                      
REMARK 465     CYS A   329                                                      
REMARK 465     THR A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     VAL A   332                                                      
REMARK 465     THR A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     TYR A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     GLN A   338                                                      
REMARK 465     LEU A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     ASP A   345                                                      
REMARK 465     HIS A   346                                                      
REMARK 465     GLU A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     VAL A   349                                                      
REMARK 465     PHE A   350                                                      
REMARK 465     THR A   351                                                      
REMARK 465     VAL A   352                                                      
REMARK 465     SER A   353                                                      
REMARK 465     LEU A   354                                                      
REMARK 465     TRP A   355                                                      
REMARK 465     ASP A   356                                                      
REMARK 465     GLY A   436                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     ALA A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 465     ALA A   440                                                      
REMARK 465     LEU A   441                                                      
REMARK 465     SER A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     ALA A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     ALA A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     SER A   449                                                      
REMARK 465     PRO A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     SER A   452                                                      
REMARK 465     GLU A   453                                                      
REMARK 465     SER A   454                                                      
REMARK 465     LYS A   455                                                      
REMARK 465     GLY A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     VAL A   458                                                      
REMARK 465     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     SER A   496                                                      
REMARK 465     TYR A   523                                                      
REMARK 465     CYS A   524                                                      
REMARK 465     HIS A   525                                                      
REMARK 465     PRO A   526                                                      
REMARK 465     ILE A   527                                                      
REMARK 465     ALA A   528                                                      
REMARK 465     LEU A   529                                                      
REMARK 465     PRO A   530                                                      
REMARK 465     LYS A   531                                                      
REMARK 465     HIS A   532                                                      
REMARK 465     GLN A   533                                                      
REMARK 465     PRO A   534                                                      
REMARK 465     THR A   535                                                      
REMARK 465     PRO A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     PRO A   538                                                      
REMARK 465     GLU A   539                                                      
REMARK 465     GLY A   540                                                      
REMARK 465     ASP A   541                                                      
REMARK 465     ARG A   542                                                      
REMARK 465     VAL A   543                                                      
REMARK 465     ASN A   969                                                      
REMARK 465     GLY A   970                                                      
REMARK 465     ASN A   971                                                      
REMARK 465     TYR A   972                                                      
REMARK 465     LYS A   973                                                      
REMARK 465     SER A   974                                                      
REMARK 465     PHE A   975                                                      
REMARK 465     LEU A   976                                                      
REMARK 465     GLY A   977                                                      
REMARK 465     ILE A   978                                                      
REMARK 465     ASN A   979                                                      
REMARK 465     LYS A   980                                                      
REMARK 465     LEU A  1088                                                      
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 465     GLU A  1103                                                      
REMARK 465     PHE A  1104                                                      
REMARK 465     GLY A  1105                                                      
REMARK 465     LEU A  1106                                                      
REMARK 465     VAL A  1107                                                      
REMARK 465     PRO A  1108                                                      
REMARK 465     ARG A  1109                                                      
REMARK 465     GLY A  1110                                                      
REMARK 465     SER A  1111                                                      
REMARK 465     GLY A  1112                                                      
REMARK 465     HIS A  1113                                                      
REMARK 465     HIS A  1114                                                      
REMARK 465     HIS A  1115                                                      
REMARK 465     HIS A  1116                                                      
REMARK 465     HIS A  1117                                                      
REMARK 465     HIS A  1118                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 143    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   236     OD1  ASP A   239              2.08            
REMARK 500   O    SER A   620     NZ   LYS A   647              2.17            
REMARK 500   OE2  GLU A   926     NZ   LYS A  1008              2.18            
REMARK 500   O    LYS A   668     O    HOH A  2023              2.18            
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    TYR A 210   N   -  CA  -  C   ANGL. DEV. =  17.8 DEGREES          
REMARK 500    LEU A 575   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    HIS A 967   O   -  C   -  N   ANGL. DEV. =  -9.7 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    SER A 144     -149.06    -83.19                                   
REMARK 500    GLU A 145       62.18   -163.49                                   
REMARK 500    GLU A 146      172.10     55.38                                   
REMARK 500    SER A 147      -51.06     43.02                                   
REMARK 500    PHE A 150      -72.86    -61.62                                   
REMARK 500    ALA A 189       30.28    -87.91                                   
REMARK 500    SER A 190      -25.32   -153.91                                   
REMARK 500    ARG A 191      123.72    -37.70                                   
REMARK 500    HIS A 199       49.50     37.75                                   
REMARK 500    LEU A 211      -80.02    106.12                                   
REMARK 500    LYS A 213       17.98    -69.74                                   
REMARK 500    ASN A 217       69.78    175.10                                   
REMARK 500    SER A 227      -71.37   -158.07                                   
REMARK 500    GLN A 231      139.68    167.58                                   
REMARK 500    PRO A 237      -35.60    -38.89                                   
REMARK 500    PHE A 248      -54.88   -175.94                                   
REMARK 500    ASP A 269       35.92    -93.90                                   
REMARK 500    LEU A 281       78.82   -114.91                                   
REMARK 500    ASN A 299       21.04    -79.81                                   
REMARK 500    LEU A 373      -60.17   -106.37                                   
REMARK 500    PRO A 374      100.82    -17.72                                   
REMARK 500    ASN A 376     -142.50   -162.61                                   
REMARK 500    ASP A 378       95.57    -12.46                                   
REMARK 500    LEU A 379     -160.38   -104.73                                   
REMARK 500    HIS A 389      -84.02   -122.21                                   
REMARK 500    GLN A 391       -3.26     61.01                                   
REMARK 500    ALA A 545      150.35     72.97                                   
REMARK 500    ASN A 549      -81.43    -23.58                                   
REMARK 500    ARG A 613       45.04    -89.41                                   
REMARK 500    ARG A 614        0.93    -65.04                                   
REMARK 500    GLN A 705       23.00   -152.83                                   
REMARK 500    LEU A 752       36.57    -63.78                                   
REMARK 500    SER A 753      116.54   -170.39                                   
REMARK 500    GLU A 755       14.17    -67.94                                   
REMARK 500    ASP A 758      148.86   -170.54                                   
REMARK 500    ASN A 773        6.51    -65.36                                   
REMARK 500    ASN A 776      -59.08     93.12                                   
REMARK 500    SER A 777      -75.78    -83.76                                   
REMARK 500    GLN A 778      -88.43    140.22                                   
REMARK 500    SER A 782      140.64   -171.10                                   
REMARK 500    TYR A 787      -26.84     74.80                                   
REMARK 500    ASP A 788       73.85   -158.64                                   
REMARK 500    ALA A 797       66.02   -104.56                                   
REMARK 500    TYR A 867      150.93    -48.12                                   
REMARK 500    SER A 894     -131.67    -78.75                                   
REMARK 500    ASN A 898     -112.59    -74.13                                   
REMARK 500    GLU A 905     -132.86    -63.33                                   
REMARK 500    VAL A 906      -67.15     72.69                                   
REMARK 500    ARG A 927      -36.95    -37.48                                   
REMARK 500    THR A 957       15.20    -69.65                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  209     TYR A  210                 -144.53                    
REMARK 500 TYR A  210     LEU A  211                  -30.69                    
REMARK 500 SER A  777     GLN A  778                  -45.32                    
REMARK 500 PHE A  965     GLY A  966                  146.68                    
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 534 A 2088                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E8Y   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINANTS OF PHOSPHOINOSITIDE 3-KINASE INHIBITION BY    
REMARK 900 WORTMANNIN, LY294002, QUERCETIN, MYRICETIN AND STAUROSPORINE         
REMARK 900 RELATED ID: 1E8Z   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINANTS OF PHOSPHOINOSITIDE 3-KINASE INHIBITION BY    
REMARK 900 WORTMANNIN, LY294002, QUERCETIN, MYRICETIN AND STAUROSPORINE         
REMARK 900 RELATED ID: 1HE8   RELATED DB: PDB                                   
REMARK 900 RAS G12V - PI 3-KINASE GAMMA COMPLEX                                 
REMARK 900 RELATED ID: 2A4Z   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PI3KGAMMA COMPLEXED WITH AS604850         
REMARK 900 RELATED ID: 2A5U   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PI3KGAMMA COMPLEXED WITH AS605240         
REMARK 900 RELATED ID: 2CHW   RELATED DB: PDB                                   
REMARK 900 A PHARMACOLOGICAL MAP OF THE PI3-K FAMILY DEFINES A ROLE FOR P110    
REMARK 900 ALPHA IN SIGNALING: THE STRUCTURE OF COMPLEX OF PHOSPHOINOSITIDE 3-  
REMARK 900 KINASE GAMMA WITH INHIBITOR PIK-39                                   
REMARK 900 RELATED ID: 2CHX   RELATED DB: PDB                                   
REMARK 900 A PHARMACOLOGICAL MAP OF THE PI3-K FAMILY DEFINES A ROLE FOR         
REMARK 900 P110ALPHA IN SIGNALING: THE STRUCTURE OF COMPLEX OF                  
REMARK 900 PHOSPHOINOSITIDE 3-KINASE GAMMA WITH INHIBITOR PIK-90                
REMARK 900 RELATED ID: 2CHZ   RELATED DB: PDB                                   
REMARK 900 A PHARMACOLOGICAL MAP OF THE PI3-K FAMILY DEFINES A ROLE FOR         
REMARK 900 P110ALPHA IN SIGNALING: THE STRUCTURE OF COMPLEX OF                  
REMARK 900 PHOSPHOINOSITIDE 3-KINASE GAMMA WITH INHIBITOR PIK-93.               
REMARK 900 RELATED ID: 2V4L   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF HUMAN PHOSPHOINOSITIDE 3-KINASE CATALYTIC SUBUNIT GAMMA   
REMARK 900 (P110 GAMMA) WITH PIK-284                                            
REMARK 900 RELATED ID: 3ZVV   RELATED DB: PDB                                   
REMARK 900 FRAGMENT BOUND TO PI3KINASE GAMMA                                    
REMARK 900 RELATED ID: 3ZW3   RELATED DB: PDB                                   
REMARK 900 FRAGMENT BASED DISCOVERY OF A NOVEL AND SELECTIVE PI3 KINASE         
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4ANU   RELATED DB: PDB                                   
REMARK 900 COMPLEXES OF PI3KGAMMA WITH ISOFORM SELECTIVE INHIBITORS.            
REMARK 900 RELATED ID: 4ANV   RELATED DB: PDB                                   
REMARK 900 COMPLEXES OF PI3KGAMMA WITH ISOFORM SELECTIVE INHIBITORS.            
REMARK 900 RELATED ID: 4ANW   RELATED DB: PDB                                   
REMARK 900 COMPLEXES OF PI3KGAMMA WITH ISOFORM SELECTIVE INHIBITORS.            
DBREF  4ANX A  144  1102  UNP    P48736   PK3CG_HUMAN    144   1102             
SEQADV 4ANX MET A  139  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX LEU A  140  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX LEU A  141  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX GLY A  142  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX SER A  143  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX GLU A 1103  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX PHE A 1104  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX GLY A 1105  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX LEU A 1106  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX VAL A 1107  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX PRO A 1108  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX ARG A 1109  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX GLY A 1110  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX SER A 1111  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX GLY A 1112  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX HIS A 1113  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX HIS A 1114  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX HIS A 1115  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX HIS A 1116  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX HIS A 1117  UNP  P48736              EXPRESSION TAG                 
SEQADV 4ANX HIS A 1118  UNP  P48736              EXPRESSION TAG                 
SEQRES   1 A  980  MET LEU LEU GLY SER SER GLU GLU SER GLN ALA PHE GLN          
SEQRES   2 A  980  ARG GLN LEU THR ALA LEU ILE GLY TYR ASP VAL THR ASP          
SEQRES   3 A  980  VAL SER ASN VAL HIS ASP ASP GLU LEU GLU PHE THR ARG          
SEQRES   4 A  980  ARG GLY LEU VAL THR PRO ARG MET ALA GLU VAL ALA SER          
SEQRES   5 A  980  ARG ASP PRO LYS LEU TYR ALA MET HIS PRO TRP VAL THR          
SEQRES   6 A  980  SER LYS PRO LEU PRO GLU TYR LEU TRP LYS LYS ILE ALA          
SEQRES   7 A  980  ASN ASN CYS ILE PHE ILE VAL ILE HIS ARG SER THR THR          
SEQRES   8 A  980  SER GLN THR ILE LYS VAL SER PRO ASP ASP THR PRO GLY          
SEQRES   9 A  980  ALA ILE LEU GLN SER PHE PHE THR LYS MET ALA LYS LYS          
SEQRES  10 A  980  LYS SER LEU MET ASP ILE PRO GLU SER GLN SER GLU GLN          
SEQRES  11 A  980  ASP PHE VAL LEU ARG VAL CYS GLY ARG ASP GLU TYR LEU          
SEQRES  12 A  980  VAL GLY GLU THR PRO ILE LYS ASN PHE GLN TRP VAL ARG          
SEQRES  13 A  980  HIS CYS LEU LYS ASN GLY GLU GLU ILE HIS VAL VAL LEU          
SEQRES  14 A  980  ASP THR PRO PRO ASP PRO ALA LEU ASP GLU VAL ARG LYS          
SEQRES  15 A  980  GLU GLU TRP PRO LEU VAL ASP ASP CYS THR GLY VAL THR          
SEQRES  16 A  980  GLY TYR HIS GLU GLN LEU THR ILE HIS GLY LYS ASP HIS          
SEQRES  17 A  980  GLU SER VAL PHE THR VAL SER LEU TRP ASP CYS ASP ARG          
SEQRES  18 A  980  LYS PHE ARG VAL LYS ILE ARG GLY ILE ASP ILE PRO VAL          
SEQRES  19 A  980  LEU PRO ARG ASN THR ASP LEU THR VAL PHE VAL GLU ALA          
SEQRES  20 A  980  ASN ILE GLN HIS GLY GLN GLN VAL LEU CYS GLN ARG ARG          
SEQRES  21 A  980  THR SER PRO LYS PRO PHE THR GLU GLU VAL LEU TRP ASN          
SEQRES  22 A  980  VAL TRP LEU GLU PHE SER ILE LYS ILE LYS ASP LEU PRO          
SEQRES  23 A  980  LYS GLY ALA LEU LEU ASN LEU GLN ILE TYR CYS GLY LYS          
SEQRES  24 A  980  ALA PRO ALA LEU SER SER LYS ALA SER ALA GLU SER PRO          
SEQRES  25 A  980  SER SER GLU SER LYS GLY LYS VAL GLN LEU LEU TYR TYR          
SEQRES  26 A  980  VAL ASN LEU LEU LEU ILE ASP HIS ARG PHE LEU LEU ARG          
SEQRES  27 A  980  ARG GLY GLU TYR VAL LEU HIS MET TRP GLN ILE SER GLY          
SEQRES  28 A  980  LYS GLY GLU ASP GLN GLY SER PHE ASN ALA ASP LYS LEU          
SEQRES  29 A  980  THR SER ALA THR ASN PRO ASP LYS GLU ASN SER MET SER          
SEQRES  30 A  980  ILE SER ILE LEU LEU ASP ASN TYR CYS HIS PRO ILE ALA          
SEQRES  31 A  980  LEU PRO LYS HIS GLN PRO THR PRO ASP PRO GLU GLY ASP          
SEQRES  32 A  980  ARG VAL ARG ALA GLU MET PRO ASN GLN LEU ARG LYS GLN          
SEQRES  33 A  980  LEU GLU ALA ILE ILE ALA THR ASP PRO LEU ASN PRO LEU          
SEQRES  34 A  980  THR ALA GLU ASP LYS GLU LEU LEU TRP HIS PHE ARG TYR          
SEQRES  35 A  980  GLU SER LEU LYS HIS PRO LYS ALA TYR PRO LYS LEU PHE          
SEQRES  36 A  980  SER SER VAL LYS TRP GLY GLN GLN GLU ILE VAL ALA LYS          
SEQRES  37 A  980  THR TYR GLN LEU LEU ALA ARG ARG GLU VAL TRP ASP GLN          
SEQRES  38 A  980  SER ALA LEU ASP VAL GLY LEU THR MET GLN LEU LEU ASP          
SEQRES  39 A  980  CYS ASN PHE SER ASP GLU ASN VAL ARG ALA ILE ALA VAL          
SEQRES  40 A  980  GLN LYS LEU GLU SER LEU GLU ASP ASP ASP VAL LEU HIS          
SEQRES  41 A  980  TYR LEU LEU GLN LEU VAL GLN ALA VAL LYS PHE GLU PRO          
SEQRES  42 A  980  TYR HIS ASP SER ALA LEU ALA ARG PHE LEU LEU LYS ARG          
SEQRES  43 A  980  GLY LEU ARG ASN LYS ARG ILE GLY HIS PHE LEU PHE TRP          
SEQRES  44 A  980  PHE LEU ARG SER GLU ILE ALA GLN SER ARG HIS TYR GLN          
SEQRES  45 A  980  GLN ARG PHE ALA VAL ILE LEU GLU ALA TYR LEU ARG GLY          
SEQRES  46 A  980  CYS GLY THR ALA MET LEU HIS ASP PHE THR GLN GLN VAL          
SEQRES  47 A  980  GLN VAL ILE GLU MET LEU GLN LYS VAL THR LEU ASP ILE          
SEQRES  48 A  980  LYS SER LEU SER ALA GLU LYS TYR ASP VAL SER SER GLN          
SEQRES  49 A  980  VAL ILE SER GLN LEU LYS GLN LYS LEU GLU ASN LEU GLN          
SEQRES  50 A  980  ASN SER GLN LEU PRO GLU SER PHE ARG VAL PRO TYR ASP          
SEQRES  51 A  980  PRO GLY LEU LYS ALA GLY ALA LEU ALA ILE GLU LYS CYS          
SEQRES  52 A  980  LYS VAL MET ALA SER LYS LYS LYS PRO LEU TRP LEU GLU          
SEQRES  53 A  980  PHE LYS CYS ALA ASP PRO THR ALA LEU SER ASN GLU THR          
SEQRES  54 A  980  ILE GLY ILE ILE PHE LYS HIS GLY ASP ASP LEU ARG GLN          
SEQRES  55 A  980  ASP MET LEU ILE LEU GLN ILE LEU ARG ILE MET GLU SER          
SEQRES  56 A  980  ILE TRP GLU THR GLU SER LEU ASP LEU CYS LEU LEU PRO          
SEQRES  57 A  980  TYR GLY CYS ILE SER THR GLY ASP LYS ILE GLY MET ILE          
SEQRES  58 A  980  GLU ILE VAL LYS ASP ALA THR THR ILE ALA LYS ILE GLN          
SEQRES  59 A  980  GLN SER THR VAL GLY ASN THR GLY ALA PHE LYS ASP GLU          
SEQRES  60 A  980  VAL LEU ASN HIS TRP LEU LYS GLU LYS SER PRO THR GLU          
SEQRES  61 A  980  GLU LYS PHE GLN ALA ALA VAL GLU ARG PHE VAL TYR SER          
SEQRES  62 A  980  CYS ALA GLY TYR CYS VAL ALA THR PHE VAL LEU GLY ILE          
SEQRES  63 A  980  GLY ASP ARG HIS ASN ASP ASN ILE MET ILE THR GLU THR          
SEQRES  64 A  980  GLY ASN LEU PHE HIS ILE ASP PHE GLY HIS ILE ASN GLY          
SEQRES  65 A  980  ASN TYR LYS SER PHE LEU GLY ILE ASN LYS GLU ARG VAL          
SEQRES  66 A  980  PRO PHE VAL LEU THR PRO ASP PHE LEU PHE VAL MET GLY          
SEQRES  67 A  980  THR SER GLY LYS LYS THR SER PRO HIS PHE GLN LYS PHE          
SEQRES  68 A  980  GLN ASP ILE CYS VAL LYS ALA TYR LEU ALA LEU ARG HIS          
SEQRES  69 A  980  HIS THR ASN LEU LEU ILE ILE LEU PHE SER MET MET LEU          
SEQRES  70 A  980  MET THR GLY MET PRO GLN LEU THR SER LYS GLU ASP ILE          
SEQRES  71 A  980  GLU TYR ILE ARG ASP ALA LEU THR VAL GLY LYS ASN GLU          
SEQRES  72 A  980  GLU ASP ALA LYS LYS TYR PHE LEU ASP GLN ILE GLU VAL          
SEQRES  73 A  980  CYS ARG ASP LYS GLY TRP THR VAL GLN PHE ASN TRP PHE          
SEQRES  74 A  980  LEU HIS LEU VAL LEU GLY ILE LYS GLN GLY GLU LYS HIS          
SEQRES  75 A  980  SER ALA GLU PHE GLY LEU VAL PRO ARG GLY SER GLY HIS          
SEQRES  76 A  980  HIS HIS HIS HIS HIS                                          
HET    534  A2088      37                                                       
HETNAM     534 5-{3-[(4-{3-[4-(1-METHYLETHYL)PHENYL]PYRAZIN-2-                  
HETNAM   2 534  YL}PIPERAZIN-1-YL)SULFONYL]PHENYL}PYRIMIDIN-2-AMINE             
FORMUL   2  534    C27 H29 N7 O2 S                                              
FORMUL   3  HOH   *34(H2 O)                                                     
HELIX    1   1 SER A  147  GLY A  159  1                                  13    
HELIX    2   2 ASP A  171  ALA A  189  1                                  19    
HELIX    3   3 ASP A  192  HIS A  199  1                                   8    
HELIX    4   4 PRO A  208  LYS A  213  1                                   6    
HELIX    5   5 THR A  240  THR A  250  1                                  11    
HELIX    6   6 PRO A  286  ASN A  289  5                                   4    
HELIX    7   7 PHE A  290  ASN A  299  1                                  10    
HELIX    8   8 ASP A  312  GLU A  317  5                                   6    
HELIX    9   9 LYS A  421  LEU A  423  5                                   3    
HELIX   10  10 ASN A  498  THR A  503  5                                   6    
HELIX   11  11 PRO A  548  THR A  561  1                                  14    
HELIX   12  12 THR A  568  PHE A  578  1                                  11    
HELIX   13  13 PHE A  578  LEU A  583  1                                   6    
HELIX   14  14 LYS A  584  LYS A  587  5                                   4    
HELIX   15  15 ALA A  588  SER A  594  1                                   7    
HELIX   16  16 GLN A  600  ALA A  612  1                                  13    
HELIX   17  17 ARG A  614  SER A  620  1                                   7    
HELIX   18  18 ASP A  623  LEU A  630  1                                   8    
HELIX   19  19 ASP A  637  GLU A  649  1                                  13    
HELIX   20  20 GLU A  652  VAL A  667  1                                  16    
HELIX   21  21 LYS A  668  GLU A  670  5                                   3    
HELIX   22  22 SER A  675  ASN A  688  1                                  14    
HELIX   23  23 ASN A  688  ALA A  704  1                                  17    
HELIX   24  24 TYR A  709  ARG A  722  1                                  14    
HELIX   25  25 GLY A  725  LEU A  752  1                                  28    
HELIX   26  26 SER A  760  ASN A  773  1                                  14    
HELIX   27  27 ALA A  797  CYS A  801  5                                   5    
HELIX   28  28 ASP A  837  THR A  857  1                                  21    
HELIX   29  29 ILE A  888  GLN A  893  1                                   6    
HELIX   30  30 VAL A  906  SER A  915  1                                  10    
HELIX   31  31 THR A  917  GLY A  943  1                                  27    
HELIX   32  32 HIS A  948  ASP A  950  5                                   3    
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 LYS A 1045  LEU A 1055  1                                  11    
HELIX   37  37 ASN A 1060  ASP A 1077  1                                  18    
HELIX   38  38 TRP A 1080  TRP A 1086  1                                   7    
SHEET    1  AA 5 SER A 230  VAL A 235  0                                        
SHEET    2  AA 5 ILE A 220  HIS A 225 -1  O  ILE A 220   N  VAL A 235           
SHEET    3  AA 5 HIS A 304  ASP A 308  1  O  VAL A 305   N  HIS A 225           
SHEET    4  AA 5 VAL A 271  VAL A 274 -1  O  VAL A 271   N  ASP A 308           
SHEET    5  AA 5 TYR A 280  LEU A 281 -1  O  LEU A 281   N  LEU A 272           
SHEET    1  AB 4 GLU A 407  LYS A 419  0                                        
SHEET    2  AB 4 LYS A 360  ASP A 369 -1  O  PHE A 361   N  PHE A 416           
SHEET    3  AB 4 SER A 515  LEU A 519 -1  O  SER A 515   N  ASP A 369           
SHEET    4  AB 4 GLU A 479  HIS A 483 -1  O  TYR A 480   N  ILE A 518           
SHEET    1  AC 2 VAL A 393  ARG A 398  0                                        
SHEET    2  AC 2 THR A 380  GLN A 388 -1  O  ALA A 385   N  ARG A 397           
SHEET    1  AD 2 LYS A 402  PRO A 403  0                                        
SHEET    2  AD 2 THR A 380  GLN A 388 -1  O  VAL A 381   N  LYS A 402           
SHEET    1  AE 5 TRP A 485  GLN A 486  0                                        
SHEET    2  AE 5 LEU A 460  LEU A 467 -1  O  TYR A 463   N  TRP A 485           
SHEET    3  AE 5 LEU A 428  TYR A 434 -1  O  LEU A 429   N  LEU A 466           
SHEET    4  AE 5 THR A 380  GLN A 388 -1  O  PHE A 382   N  TYR A 434           
SHEET    5  AE 5 VAL A 393  ARG A 398 -1  N  LEU A 394   O  ILE A 387           
SHEET    1  AF 5 TRP A 485  GLN A 486  0                                        
SHEET    2  AF 5 LEU A 460  LEU A 467 -1  O  TYR A 463   N  TRP A 485           
SHEET    3  AF 5 LEU A 428  TYR A 434 -1  O  LEU A 429   N  LEU A 466           
SHEET    4  AF 5 THR A 380  GLN A 388 -1  O  PHE A 382   N  TYR A 434           
SHEET    5  AF 5 LYS A 402  PRO A 403 -1  O  LYS A 402   N  VAL A 381           
SHEET    1  AG 2 PHE A 783  ARG A 784  0                                        
SHEET    2  AG 2 LYS A 792  ALA A 793 -1  O  ALA A 793   N  PHE A 783           
SHEET    1  AH 5 LYS A 802  VAL A 803  0                                        
SHEET    2  AH 5 LEU A 811  PHE A 815 -1  O  TRP A 812   N  LYS A 802           
SHEET    3  AH 5 ILE A 828  HIS A 834 -1  O  ILE A 828   N  PHE A 815           
SHEET    4  AH 5 ILE A 876  GLU A 880 -1  O  GLY A 877   N  LYS A 833           
SHEET    5  AH 5 CYS A 869  GLY A 873 -1  O  ILE A 870   N  MET A 878           
SHEET    1  AI 3 ALA A 885  THR A 887  0                                        
SHEET    2  AI 3 ILE A 952  THR A 955 -1  O  ILE A 954   N  THR A 886           
SHEET    3  AI 3 LEU A 960  HIS A 962 -1  O  PHE A 961   N  MET A 953           
CISPEP   1 GLU A  145    GLU A  146          0       -13.82                     
CISPEP   2 TRP A  410    ASN A  411          0        -9.40                     
CISPEP   3 GLN A  775    ASN A  776          0        23.54                     
CISPEP   4 ALA A  901    PHE A  902          0        13.53                     
CISPEP   5 GLY A  966    HIS A  967          0       -27.15                     
CISPEP   6 HIS A  967    ILE A  968          0       -14.66                     
CISPEP   7 SER A  998    GLY A  999          0         8.07                     
CISPEP   8 ASP A 1077    LYS A 1078          0         9.15                     
SITE     1 AC1 15 MET A 804  TRP A 812  ILE A 831  LYS A 833                    
SITE     2 AC1 15 TYR A 867  ILE A 879  GLU A 880  ILE A 881                    
SITE     3 AC1 15 VAL A 882  THR A 887  ASP A 950  ASN A 951                    
SITE     4 AC1 15 MET A 953  ILE A 963  ASP A 964                               
CRYST1  143.424   68.531  106.263  90.00  95.26  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      0.006972  0.000000  0.000642        0.00000                         
SCALE2      0.000000  0.014592  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009450        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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