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Database: PDB
Entry: 4WWO
LinkDB: 4WWO
Original site: 4WWO 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       11-NOV-14   4WWO              
TITLE     CRYSTAL STRUCTURE OF HUMAN PI3K-GAMMA IN COMPLEX WITH PHENYLQUINOLINE 
TITLE    2 INHIBITOR N-{(1S)-1-[8-CHLORO-2-(3-FLUOROPHENYL)QUINOLIN-3-YL]ETHYL}-
TITLE    3 9H-PURIN-6-AMINE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT GAMMA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PTDINS-3-KINASE SUBUNIT GAMMA,PHOSPHATIDYLINOSITOL 4,5-     
COMPND   6 BISPHOSPHATE 3-KINASE 110 KDA CATALYTIC SUBUNIT GAMMA,P110GAMMA,     
COMPND   7 PHOSPHOINOSITIDE-3-KINASE CATALYTIC GAMMA POLYPEPTIDE,               
COMPND   8 SERINE/THREONINE PROTEIN KINASE PIK3CG,P120-PI3K;                    
COMPND   9 EC: 2.7.1.153,2.7.11.1;                                              
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PIK3CG;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    KINASE, PHOSPHOTRANSFER, PIP2, TRANSFERASE-TRANSFERASE INHIBITOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.WHITTINGTON,J.TANG,P.YAKOWEC                                      
REVDAT   3   22-NOV-17 4WWO    1       SOURCE KEYWDS JRNL   REMARK              
REVDAT   2   28-JAN-15 4WWO    1       JRNL                                     
REVDAT   1   17-DEC-14 4WWO    0                                                
JRNL        AUTH   T.D.CUSHING,X.HAO,Y.SHIN,K.ANDREWS,M.BROWN,M.CARDOZO,Y.CHEN, 
JRNL        AUTH 2 J.DUQUETTE,B.FISHER,F.GONZALEZ-LOPEZ DE TURISO,X.HE,         
JRNL        AUTH 3 K.R.HENNE,Y.L.HU,R.HUNGATE,M.G.JOHNSON,R.C.KELLY,B.LUCAS,    
JRNL        AUTH 4 J.D.MCCARTER,L.R.MCGEE,J.C.MEDINA,T.SAN MIGUEL,D.MOHN,       
JRNL        AUTH 5 V.PATTAROPONG,L.H.PETTUS,A.REICHELT,R.M.RZASA,J.SEGANISH,    
JRNL        AUTH 6 A.S.TASKER,R.C.WAHL,S.WANNBERG,D.A.WHITTINGTON,J.WHORISKEY,  
JRNL        AUTH 7 G.YU,L.ZALAMEDA,D.ZHANG,D.P.METZ                             
JRNL        TITL   DISCOVERY AND IN VIVO EVALUATION OF                          
JRNL        TITL 2 (S)-N-(1-(7-FLUORO-2-(PYRIDIN-2-YL)QUINOLIN-3-YL)ETHYL)      
JRNL        TITL 3 -9H-PURIN-6-AMINE (AMG319) AND RELATED PI3K DELTA INHIBITORS 
JRNL        TITL 4 FOR INFLAMMATION AND AUTOIMMUNE DISEASE.                     
JRNL        REF    J.MED.CHEM.                   V.  58   480 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25469863                                                     
JRNL        DOI    10.1021/JM501624R                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 46680                          
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) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2350                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6594                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 65.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.13000                                             
REMARK   3    B22 (A**2) : 2.86000                                              
REMARK   3    B33 (A**2) : -0.61000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.63000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.319         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.250         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.197         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.840        
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 4WWO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204638.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-07                          
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               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46753                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG 3350, 100 MM TRIS (PH 7.3),      
REMARK 280  250 MM AMMONIUM SULFATE, 1 MM DITHIOTHREITOL, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, 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       72.95050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.08750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       72.95050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.08750            
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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 TOTAL BURIED SURFACE AREA: 840 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 35880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   144                                                      
REMARK 465     GLU A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     SER A   247                                                      
REMARK 465     PHE A   248                                                      
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     ASP A   269                                                      
REMARK 465     PHE A   270                                                      
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     PRO A   374                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     ASN A   376                                                      
REMARK 465     THR A   377                                                      
REMARK 465     ASP A   378                                                      
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     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     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     ARG A   544                                                      
REMARK 465     ALA A   754                                                      
REMARK 465     GLU A   755                                                      
REMARK 465     LYS A   756                                                      
REMARK 465     TYR A   757                                                      
REMARK 465     ASP A   758                                                      
REMARK 465     ASN A   898                                                      
REMARK 465     THR A   899                                                      
REMARK 465     GLY A   900                                                      
REMARK 465     ALA A   901                                                      
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     GLN A  1041                                                      
REMARK 465     LEU A  1042                                                      
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     LYS A 807    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 167       49.60   -140.36                                   
REMARK 500    ASN A 217       72.59     34.13                                   
REMARK 500    ARG A 226      -73.89   -111.45                                   
REMARK 500    SER A 227      -54.37   -133.43                                   
REMARK 500    SER A 230       78.20   -150.61                                   
REMARK 500    SER A 488      144.61     82.28                                   
REMARK 500    PHE A 578       42.25   -102.27                                   
REMARK 500    SER A 760      116.99    174.69                                   
REMARK 500    SER A 777      -63.59   -131.21                                   
REMARK 500    ASP A 788       76.82   -150.02                                   
REMARK 500    ALA A 805       93.10    -66.00                                   
REMARK 500    THR A1002      107.13   -161.12                                   
REMARK 500    THR A1056       69.09     34.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 3VD A 1205                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WWN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WWP   RELATED DB: PDB                                   
DBREF  4WWO A  144  1102  UNP    P48736   PK3CG_HUMAN    144   1102             
SEQRES   1 A  959  SER GLU GLU SER GLN ALA PHE GLN ARG GLN LEU THR ALA          
SEQRES   2 A  959  LEU ILE GLY TYR ASP VAL THR ASP VAL SER ASN VAL HIS          
SEQRES   3 A  959  ASP ASP GLU LEU GLU PHE THR ARG ARG GLY LEU VAL THR          
SEQRES   4 A  959  PRO ARG MET ALA GLU VAL ALA SER ARG ASP PRO LYS LEU          
SEQRES   5 A  959  TYR ALA MET HIS PRO TRP VAL THR SER LYS PRO LEU PRO          
SEQRES   6 A  959  GLU TYR LEU TRP LYS LYS ILE ALA ASN ASN CYS ILE PHE          
SEQRES   7 A  959  ILE VAL ILE HIS ARG SER THR THR SER GLN THR ILE LYS          
SEQRES   8 A  959  VAL SER PRO ASP ASP THR PRO GLY ALA ILE LEU GLN SER          
SEQRES   9 A  959  PHE PHE THR LYS MET ALA LYS LYS LYS SER LEU MET ASP          
SEQRES  10 A  959  ILE PRO GLU SER GLN SER GLU GLN ASP PHE VAL LEU ARG          
SEQRES  11 A  959  VAL CYS GLY ARG ASP GLU TYR LEU VAL GLY GLU THR PRO          
SEQRES  12 A  959  ILE LYS ASN PHE GLN TRP VAL ARG HIS CYS LEU LYS ASN          
SEQRES  13 A  959  GLY GLU GLU ILE HIS VAL VAL LEU ASP THR PRO PRO ASP          
SEQRES  14 A  959  PRO ALA LEU ASP GLU VAL ARG LYS GLU GLU TRP PRO LEU          
SEQRES  15 A  959  VAL ASP ASP CYS THR GLY VAL THR GLY TYR HIS GLU GLN          
SEQRES  16 A  959  LEU THR ILE HIS GLY LYS ASP HIS GLU SER VAL PHE THR          
SEQRES  17 A  959  VAL SER LEU TRP ASP CYS ASP ARG LYS PHE ARG VAL LYS          
SEQRES  18 A  959  ILE ARG GLY ILE ASP ILE PRO VAL LEU PRO ARG ASN THR          
SEQRES  19 A  959  ASP LEU THR VAL PHE VAL GLU ALA ASN ILE GLN HIS GLY          
SEQRES  20 A  959  GLN GLN VAL LEU CYS GLN ARG ARG THR SER PRO LYS PRO          
SEQRES  21 A  959  PHE THR GLU GLU VAL LEU TRP ASN VAL TRP LEU GLU PHE          
SEQRES  22 A  959  SER ILE LYS ILE LYS ASP LEU PRO LYS GLY ALA LEU LEU          
SEQRES  23 A  959  ASN LEU GLN ILE TYR CYS GLY LYS ALA PRO ALA LEU SER          
SEQRES  24 A  959  SER LYS ALA SER ALA GLU SER PRO SER SER GLU SER LYS          
SEQRES  25 A  959  GLY LYS VAL GLN LEU LEU TYR TYR VAL ASN LEU LEU LEU          
SEQRES  26 A  959  ILE ASP HIS ARG PHE LEU LEU ARG ARG GLY GLU TYR VAL          
SEQRES  27 A  959  LEU HIS MET TRP GLN ILE SER GLY LYS GLY GLU ASP GLN          
SEQRES  28 A  959  GLY SER PHE ASN ALA ASP LYS LEU THR SER ALA THR ASN          
SEQRES  29 A  959  PRO ASP LYS GLU ASN SER MET SER ILE SER ILE LEU LEU          
SEQRES  30 A  959  ASP ASN TYR CYS HIS PRO ILE ALA LEU PRO LYS HIS GLN          
SEQRES  31 A  959  PRO THR PRO ASP PRO GLU GLY ASP ARG VAL ARG ALA GLU          
SEQRES  32 A  959  MET PRO ASN GLN LEU ARG LYS GLN LEU GLU ALA ILE ILE          
SEQRES  33 A  959  ALA THR ASP PRO LEU ASN PRO LEU THR ALA GLU ASP LYS          
SEQRES  34 A  959  GLU LEU LEU TRP HIS PHE ARG TYR GLU SER LEU LYS HIS          
SEQRES  35 A  959  PRO LYS ALA TYR PRO LYS LEU PHE SER SER VAL LYS TRP          
SEQRES  36 A  959  GLY GLN GLN GLU ILE VAL ALA LYS THR TYR GLN LEU LEU          
SEQRES  37 A  959  ALA ARG ARG GLU VAL TRP ASP GLN SER ALA LEU ASP VAL          
SEQRES  38 A  959  GLY LEU THR MET GLN LEU LEU ASP CYS ASN PHE SER ASP          
SEQRES  39 A  959  GLU ASN VAL ARG ALA ILE ALA VAL GLN LYS LEU GLU SER          
SEQRES  40 A  959  LEU GLU ASP ASP ASP VAL LEU HIS TYR LEU LEU GLN LEU          
SEQRES  41 A  959  VAL GLN ALA VAL LYS PHE GLU PRO TYR HIS ASP SER ALA          
SEQRES  42 A  959  LEU ALA ARG PHE LEU LEU LYS ARG GLY LEU ARG ASN LYS          
SEQRES  43 A  959  ARG ILE GLY HIS PHE LEU PHE TRP PHE LEU ARG SER GLU          
SEQRES  44 A  959  ILE ALA GLN SER ARG HIS TYR GLN GLN ARG PHE ALA VAL          
SEQRES  45 A  959  ILE LEU GLU ALA TYR LEU ARG GLY CYS GLY THR ALA MET          
SEQRES  46 A  959  LEU HIS ASP PHE THR GLN GLN VAL GLN VAL ILE GLU MET          
SEQRES  47 A  959  LEU GLN LYS VAL THR LEU ASP ILE LYS SER LEU SER ALA          
SEQRES  48 A  959  GLU LYS TYR ASP VAL SER SER GLN VAL ILE SER GLN LEU          
SEQRES  49 A  959  LYS GLN LYS LEU GLU ASN LEU GLN ASN SER GLN LEU PRO          
SEQRES  50 A  959  GLU SER PHE ARG VAL PRO TYR ASP PRO GLY LEU LYS ALA          
SEQRES  51 A  959  GLY ALA LEU ALA ILE GLU LYS CYS LYS VAL MET ALA SER          
SEQRES  52 A  959  LYS LYS LYS PRO LEU TRP LEU GLU PHE LYS CYS ALA ASP          
SEQRES  53 A  959  PRO THR ALA LEU SER ASN GLU THR ILE GLY ILE ILE PHE          
SEQRES  54 A  959  LYS HIS GLY ASP ASP LEU ARG GLN ASP MET LEU ILE LEU          
SEQRES  55 A  959  GLN ILE LEU ARG ILE MET GLU SER ILE TRP GLU THR GLU          
SEQRES  56 A  959  SER LEU ASP LEU CYS LEU LEU PRO TYR GLY CYS ILE SER          
SEQRES  57 A  959  THR GLY ASP LYS ILE GLY MET ILE GLU ILE VAL LYS ASP          
SEQRES  58 A  959  ALA THR THR ILE ALA LYS ILE GLN GLN SER THR VAL GLY          
SEQRES  59 A  959  ASN THR GLY ALA PHE LYS ASP GLU VAL LEU ASN HIS TRP          
SEQRES  60 A  959  LEU LYS GLU LYS SER PRO THR GLU GLU LYS PHE GLN ALA          
SEQRES  61 A  959  ALA VAL GLU ARG PHE VAL TYR SER CYS ALA GLY TYR CYS          
SEQRES  62 A  959  VAL ALA THR PHE VAL LEU GLY ILE GLY ASP ARG HIS ASN          
SEQRES  63 A  959  ASP ASN ILE MET ILE THR GLU THR GLY ASN LEU PHE HIS          
SEQRES  64 A  959  ILE ASP PHE GLY HIS ILE LEU GLY ASN TYR LYS SER PHE          
SEQRES  65 A  959  LEU GLY ILE ASN LYS GLU ARG VAL PRO PHE VAL LEU THR          
SEQRES  66 A  959  PRO ASP PHE LEU PHE VAL MET GLY THR SER GLY LYS LYS          
SEQRES  67 A  959  THR SER PRO HIS PHE GLN LYS PHE GLN ASP ILE CYS VAL          
SEQRES  68 A  959  LYS ALA TYR LEU ALA LEU ARG HIS HIS THR ASN LEU LEU          
SEQRES  69 A  959  ILE ILE LEU PHE SER MET MET LEU MET THR GLY MET PRO          
SEQRES  70 A  959  GLN LEU THR SER LYS GLU ASP ILE GLU TYR ILE ARG ASP          
SEQRES  71 A  959  ALA LEU THR VAL GLY LYS ASN GLU GLU ASP ALA LYS LYS          
SEQRES  72 A  959  TYR PHE LEU ASP GLN ILE GLU VAL CYS ARG ASP LYS GLY          
SEQRES  73 A  959  TRP THR VAL GLN PHE ASN TRP PHE LEU HIS LEU VAL LEU          
SEQRES  74 A  959  GLY ILE LYS GLN GLY GLU LYS HIS SER ALA                      
HET    SO4  A1201       5                                                       
HET    SO4  A1202       5                                                       
HET    SO4  A1203       5                                                       
HET    SO4  A1204       5                                                       
HET    3VD  A1205      30                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     3VD N-{(1S)-1-[8-CHLORO-2-(3-FLUOROPHENYL)QUINOLIN-3-                
HETNAM   2 3VD  YL]ETHYL}-9H-PURIN-6-AMINE                                      
FORMUL   2  SO4    4(O4 S 2-)                                                   
FORMUL   6  3VD    C22 H16 CL F N6                                              
FORMUL   7  HOH   *88(H2 O)                                                     
HELIX    1 AA1 GLN A  148  GLY A  159  1                                  12    
HELIX    2 AA2 ASP A  171  LEU A  180  1                                  10    
HELIX    3 AA3 LEU A  180  ARG A  191  1                                  12    
HELIX    4 AA4 ASP A  192  HIS A  199  1                                   8    
HELIX    5 AA5 PRO A  208  LYS A  213  1                                   6    
HELIX    6 AA6 THR A  240  LEU A  245  1                                   6    
HELIX    7 AA7 PRO A  286  ASN A  289  5                                   4    
HELIX    8 AA8 PHE A  290  GLY A  300  1                                  11    
HELIX    9 AA9 ASP A  312  GLU A  317  5                                   6    
HELIX   10 AB1 SER A  353  CYS A  357  5                                   5    
HELIX   11 AB2 LYS A  421  LEU A  423  5                                   3    
HELIX   12 AB3 ASN A  498  THR A  503  5                                   6    
HELIX   13 AB4 PRO A  548  THR A  561  1                                  14    
HELIX   14 AB5 THR A  568  PHE A  578  1                                  11    
HELIX   15 AB6 PHE A  578  LEU A  583  1                                   6    
HELIX   16 AB7 LYS A  584  LYS A  587  5                                   4    
HELIX   17 AB8 ALA A  588  SER A  594  1                                   7    
HELIX   18 AB9 GLN A  600  ALA A  612  1                                  13    
HELIX   19 AC1 ARG A  614  SER A  620  1                                   7    
HELIX   20 AC2 ASP A  623  LEU A  630  1                                   8    
HELIX   21 AC3 ASP A  637  GLU A  649  1                                  13    
HELIX   22 AC4 GLU A  652  ALA A  666  1                                  15    
HELIX   23 AC5 VAL A  667  GLU A  670  5                                   4    
HELIX   24 AC6 SER A  675  ASN A  688  1                                  14    
HELIX   25 AC7 ASN A  688  ALA A  704  1                                  17    
HELIX   26 AC8 TYR A  709  ARG A  722  1                                  14    
HELIX   27 AC9 GLY A  725  LEU A  752  1                                  28    
HELIX   28 AD1 SER A  761  ASN A  776  1                                  16    
HELIX   29 AD2 ILE A  798  CYS A  801  5                                   4    
HELIX   30 AD3 ASP A  837  GLU A  858  1                                  22    
HELIX   31 AD4 ILE A  888  GLY A  897  1                                  10    
HELIX   32 AD5 GLU A  905  SER A  915  1                                  11    
HELIX   33 AD6 THR A  917  LEU A  942  1                                  26    
HELIX   34 AD7 THR A  988  GLY A  996  1                                   9    
HELIX   35 AD8 SER A 1003  HIS A 1022  1                                  20    
HELIX   36 AD9 HIS A 1023  MET A 1039  1                                  17    
HELIX   37 AE1 SER A 1044  GLU A 1049  1                                   6    
HELIX   38 AE2 GLU A 1049  LEU A 1055  1                                   7    
HELIX   39 AE3 ASN A 1060  GLY A 1079  1                                  20    
HELIX   40 AE4 TRP A 1080  LEU A 1090  1                                  11    
SHEET    1 AA1 5 GLN A 231  VAL A 235  0                                        
SHEET    2 AA1 5 ILE A 220  HIS A 225 -1  N  ILE A 220   O  VAL A 235           
SHEET    3 AA1 5 ILE A 303  LEU A 307  1  O  LEU A 307   N  HIS A 225           
SHEET    4 AA1 5 LEU A 272  VAL A 274 -1  N  ARG A 273   O  VAL A 306           
SHEET    5 AA1 5 TYR A 280  LEU A 281 -1  O  LEU A 281   N  LEU A 272           
SHEET    1 AA2 4 GLU A 407  LYS A 419  0                                        
SHEET    2 AA2 4 LYS A 360  ASP A 369 -1  N  PHE A 361   O  PHE A 416           
SHEET    3 AA2 4 SER A 515  LEU A 520 -1  O  SER A 517   N  GLY A 367           
SHEET    4 AA2 4 GLY A 478  HIS A 483 -1  N  GLY A 478   O  LEU A 520           
SHEET    1 AA3 3 GLN A 392  ARG A 398  0                                        
SHEET    2 AA3 3 THR A 380  HIS A 389 -1  N  ILE A 387   O  LEU A 394           
SHEET    3 AA3 3 LYS A 402  PRO A 403 -1  O  LYS A 402   N  VAL A 381           
SHEET    1 AA4 5 GLN A 392  ARG A 398  0                                        
SHEET    2 AA4 5 THR A 380  HIS A 389 -1  N  ILE A 387   O  LEU A 394           
SHEET    3 AA4 5 LEU A 428  GLY A 436 -1  O  GLN A 432   N  GLU A 384           
SHEET    4 AA4 5 GLN A 459  LEU A 467 -1  O  LEU A 466   N  LEU A 429           
SHEET    5 AA4 5 TRP A 485  GLN A 486 -1  O  TRP A 485   N  TYR A 463           
SHEET    1 AA5 4 PHE A 783  VAL A 785  0                                        
SHEET    2 AA5 4 ASP A 788  LEU A 796 -1  O  ALA A 793   N  PHE A 783           
SHEET    3 AA5 4 LEU A 811  CYS A 817 -1  O  LYS A 816   N  GLY A 794           
SHEET    4 AA5 4 LYS A 802  VAL A 803 -1  N  LYS A 802   O  TRP A 812           
SHEET    1 AA6 6 PHE A 783  VAL A 785  0                                        
SHEET    2 AA6 6 ASP A 788  LEU A 796 -1  O  ALA A 793   N  PHE A 783           
SHEET    3 AA6 6 LEU A 811  CYS A 817 -1  O  LYS A 816   N  GLY A 794           
SHEET    4 AA6 6 ILE A 828  HIS A 834 -1  O  ILE A 830   N  LEU A 813           
SHEET    5 AA6 6 ILE A 876  GLU A 880 -1  O  ILE A 879   N  ILE A 831           
SHEET    6 AA6 6 CYS A 869  GLY A 873 -1  N  THR A 872   O  ILE A 876           
SHEET    1 AA7 3 ALA A 885  THR A 887  0                                        
SHEET    2 AA7 3 ILE A 952  THR A 955 -1  O  ILE A 954   N  THR A 886           
SHEET    3 AA7 3 LEU A 960  HIS A 962 -1  O  PHE A 961   N  MET A 953           
SITE     1 AC1  5 PRO A 206  LEU A 207  TRP A 212  LYS A 288                    
SITE     2 AC1  5 LYS A1066                                                     
SITE     1 AC2  4 ALA A 545  TRP A 576  ARG A 579  LYS A 606                    
SITE     1 AC3  5 LEU A 657  PHE A 694  PHE A 698  GLN A 846                    
SITE     2 AC3  5 HOH A1342                                                     
SITE     1 AC4  4 ASP A 946  ARG A 947  HIS A 948  ASN A 951                    
SITE     1 AC5 13 LYS A 802  MET A 804  PRO A 810  TRP A 812                    
SITE     2 AC5 13 ILE A 831  ILE A 879  GLU A 880  ILE A 881                    
SITE     3 AC5 13 VAL A 882  ALA A 885  MET A 953  ILE A 963                    
SITE     4 AC5 13 HOH A1385                                                     
CRYST1  145.901   68.175  107.381  90.00  95.39  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      0.006854  0.000000  0.000647        0.00000                         
SCALE2      0.000000  0.014668  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009354        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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