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Database: PDB
Entry: 3IBE
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HEADER    TRANSFERASE                             15-JUL-09   3IBE              
TITLE     CRYSTAL STRUCTURE OF A PYRAZOLOPYRIMIDINE INHIBITOR BOUND TO PI3      
TITLE    2 KINASE GAMMA                                                         
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: PI3 KINASE GAMMA (UNP RESIDUES 144 TO 1102);               
COMPND   6 SYNONYM: PI3-KINASE P110 SUBUNIT GAMMA, PTDINS-3-KINASE SUBUNIT P110,
COMPND   7 PI3KGAMMA, PI3K, P120-PI3K;                                          
COMPND   8 EC: 2.7.1.153;                                                       
COMPND   9 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                                        
KEYWDS    PI3KINASE INHIBITOR, ATP-BINDING, KINASE, NUCLEOTIDE-BINDING,         
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.BARD,K.SVENSON                                                      
REVDAT   2   01-NOV-17 3IBE    1       REMARK                                   
REVDAT   1   01-SEP-09 3IBE    0                                                
JRNL        AUTH   A.ZASK,J.C.VERHEIJEN,K.CURRAN,J.KAPLAN,D.J.RICHARD,P.NOWAK,  
JRNL        AUTH 2 D.J.MALWITZ,N.BROOIJMANS,J.BARD,K.SVENSON,J.LUCAS,           
JRNL        AUTH 3 L.TORAL-BARZA,W.G.ZHANG,I.HOLLANDER,J.J.GIBBONS,R.T.ABRAHAM, 
JRNL        AUTH 4 S.AYRAL-KALOUSTIAN,T.S.MANSOUR,K.YU                          
JRNL        TITL   ATP-COMPETITIVE INHIBITORS OF THE MAMMALIAN TARGET OF        
JRNL        TITL 2 RAPAMYCIN: DESIGN AND SYNTHESIS OF HIGHLY POTENT AND         
JRNL        TITL 3 SELECTIVE PYRAZOLOPYRIMIDINES.                               
JRNL        REF    J.MED.CHEM.                   V.  52  5013 2009              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   19645448                                                     
JRNL        DOI    10.1021/JM900851F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.71                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.150                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 83.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 21693                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.150                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1117                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.7170 -  5.5920    0.99     3175   167  0.2100 0.2580        
REMARK   3     2  5.5920 -  4.4400    0.99     3074   167  0.1680 0.2350        
REMARK   3     3  4.4400 -  3.8790    0.98     3050   155  0.1740 0.2470        
REMARK   3     4  3.8790 -  3.5250    0.97     2984   160  0.1990 0.2790        
REMARK   3     5  3.5250 -  3.2720    0.93     2853   154  0.2460 0.3260        
REMARK   3     6  3.2720 -  3.0790    0.80     2435   128  0.2670 0.3860        
REMARK   3     7  3.0790 -  2.9250    0.59     1824   103  0.2770 0.3630        
REMARK   3     8  2.9250 -  2.7980    0.39     1181    83  0.2920 0.4320        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.29                                          
REMARK   3   B_SOL              : 55.21                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.62700                                              
REMARK   3    B22 (A**2) : 15.39800                                             
REMARK   3    B33 (A**2) : 5.01500                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 12.67100                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           6727                                  
REMARK   3   ANGLE     :  1.356           9158                                  
REMARK   3   CHIRALITY :  0.066           1055                                  
REMARK   3   PLANARITY :  0.006           1165                                  
REMARK   3   DIHEDRAL  : 18.563           2345                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3IBE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054201.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23209                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 48.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43300                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX RIGID BODY                                     
REMARK 200 STARTING MODEL: PDB ENTRY 1E8Y                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.3, 100 MM AMMONIUM      
REMARK 280  SULFATE, 17% PEG 3350, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
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       72.57950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.22900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       72.57950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.22900            
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     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     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     PRO A   374                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     ASN A   376                                                      
REMARK 465     THR A   377                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     ALA A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 465     ALA A   440                                                      
REMARK 465     LEU A   441                                                      
REMARK 465     SER A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     ALA A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     ALA A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     SER A   449                                                      
REMARK 465     PRO A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     SER A   452                                                      
REMARK 465     GLU A   453                                                      
REMARK 465     SER A   454                                                      
REMARK 465     LYS A   455                                                      
REMARK 465     GLY A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     GLY A   489                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     GLY A   491                                                      
REMARK 465     GLU A   492                                                      
REMARK 465     ASP A   493                                                      
REMARK 465     GLN A   494                                                      
REMARK 465     GLY A   495                                                      
REMARK 465     TYR A   523                                                      
REMARK 465     CYS A   524                                                      
REMARK 465     PRO A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     PRO A   538                                                      
REMARK 465     GLU A   539                                                      
REMARK 465     GLY A   540                                                      
REMARK 465     THR A   895                                                      
REMARK 465     VAL A   896                                                      
REMARK 465     GLY A   897                                                      
REMARK 465     ASN A   898                                                      
REMARK 465     ILE A   968                                                      
REMARK 465     LEU A   969                                                      
REMARK 465     GLY A   970                                                      
REMARK 465     ASN A   971                                                      
REMARK 465     TYR A   972                                                      
REMARK 465     LYS A   973                                                      
REMARK 465     SER A   974                                                      
REMARK 465     PHE A   975                                                      
REMARK 465     LEU A   976                                                      
REMARK 465     GLY A   977                                                      
REMARK 465     ILE A   978                                                      
REMARK 465     ASN A   979                                                      
REMARK 465     GLN A  1041                                                      
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     HIS A  1103                                                      
REMARK 465     HIS A  1104                                                      
REMARK 465     HIS A  1105                                                      
REMARK 465     HIS A  1106                                                      
REMARK 465     HIS A  1107                                                      
REMARK 465     HIS A  1108                                                      
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     MET A 143    CG   SD   CE                                        
REMARK 470     GLU A 146    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 148    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 152    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 178    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 213    CG   CD   CE   NZ                                   
REMARK 470     LYS A 214    CG   CD   CE   NZ                                   
REMARK 470     ILE A 215    CG1  CG2  CD1                                       
REMARK 470     ASN A 217    CG   OD1  ND2                                       
REMARK 470     ILE A 220    CG1  CG2  CD1                                       
REMARK 470     GLN A 231    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 251    CG   CD   CE   NZ                                   
REMARK 470     MET A 252    CG   SD   CE                                        
REMARK 470     GLU A 267    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 268    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 307    CG   CD1  CD2                                       
REMARK 470     LYS A 320    CG   CD   CE   NZ                                   
REMARK 470     TRP A 323    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 323    CZ3  CH2                                            
REMARK 470     LEU A 354    CG   CD1  CD2                                       
REMARK 470     ARG A 359    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 364    CG   CD   CE   NZ                                   
REMARK 470     LEU A 373    CG   CD1  CD2                                       
REMARK 470     ASP A 378    CG   OD1  OD2                                       
REMARK 470     ARG A 398    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 406    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 419    CG   CD   CE   NZ                                   
REMARK 470     LYS A 421    CG   CD   CE   NZ                                   
REMARK 470     ARG A 459    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 461    CG   CD1  CD2                                       
REMARK 470     ARG A 477    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 486    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 497    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 511    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 522    CG   OD1  ND2                                       
REMARK 470     HIS A 525    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 529    CG   CD1  CD2                                       
REMARK 470     LYS A 531    CG   CD   CE   NZ                                   
REMARK 470     HIS A 532    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 533    CG   CD   OE1  NE2                                  
REMARK 470     THR A 535    OG1  CG2                                            
REMARK 470     ASP A 541    CG   OD1  OD2                                       
REMARK 470     ARG A 542    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 544    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 546    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 581    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 602    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 613    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 615    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 638    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 743    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 744    CG   CD   CE   NZ                                   
REMARK 470     LYS A 750    CG   CD   CE   NZ                                   
REMARK 470     GLU A 755    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 756    CG   CD   CE   NZ                                   
REMARK 470     TYR A 757    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A 759    CG1  CG2                                            
REMARK 470     GLN A 762    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 766    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 767    CG   CD1  CD2                                       
REMARK 470     LYS A 768    CG   CD   CE   NZ                                   
REMARK 470     GLN A 769    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 770    CG   CD   CE   NZ                                   
REMARK 470     GLU A 772    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 773    CG   OD1  ND2                                       
REMARK 470     LEU A 774    CG   CD1  CD2                                       
REMARK 470     GLN A 775    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 776    CG   OD1  ND2                                       
REMARK 470     GLN A 778    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 779    CG   CD1  CD2                                       
REMARK 470     GLU A 781    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 808    CG   CD   CE   NZ                                   
REMARK 470     LYS A 816    CG   CD   CE   NZ                                   
REMARK 470     LEU A 823    CG   CD1  CD2                                       
REMARK 470     SER A 824    OG                                                  
REMARK 470     GLU A 826    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 890    CG   CD   CE   NZ                                   
REMARK 470     THR A 899    OG1  CG2                                            
REMARK 470     LYS A 903    CG   CD   CE   NZ                                   
REMARK 470     LEU A 907    CG   CD1  CD2                                       
REMARK 470     LEU A 911    CG   CD1  CD2                                       
REMARK 470     LYS A 912    CG   CD   CE   NZ                                   
REMARK 470     GLU A 926    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 967    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 980    CG   CD   CE   NZ                                   
REMARK 470     GLU A 981    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 982    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1000    CG   CD   CE   NZ                                   
REMARK 470     LYS A1001    CG   CD   CE   NZ                                   
REMARK 470     GLN A1007    CG   CD   OE1  NE2                                  
REMARK 470     LEU A1042    CG   CD1  CD2                                       
REMARK 470     LYS A1045    CG   CD   CE   NZ                                   
REMARK 470     GLU A1046    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1065    CG   CD   CE   NZ                                   
REMARK 470     LYS A1066    CG   CD   CE   NZ                                   
REMARK 470     LYS A1078    CG   CD   CE   NZ                                   
REMARK 470     LEU A1092    CG   CD1  CD2                                       
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   O    THR A  1081     OD1  ASN A  1085              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    PRO A 810   C   -  N   -  CA  ANGL. DEV. =  10.0 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       22.39    -71.00                                   
REMARK 500    VAL A 162       11.73    -65.36                                   
REMARK 500    ASN A 167       43.10   -145.57                                   
REMARK 500    HIS A 199       45.46     31.72                                   
REMARK 500    ILE A 215      -71.19    -49.05                                   
REMARK 500    ALA A 216       49.02     86.08                                   
REMARK 500    SER A 227      -74.01   -125.22                                   
REMARK 500    SER A 230      135.39   -179.18                                   
REMARK 500    THR A 232      150.75    -40.03                                   
REMARK 500    ASP A 269       54.43    -94.63                                   
REMARK 500    LEU A 272       97.33    -69.07                                   
REMARK 500    ASP A 278       51.07    -99.14                                   
REMARK 500    LEU A 281       75.94   -101.01                                   
REMARK 500    ILE A 303       78.73    -52.25                                   
REMARK 500    ARG A 366      -74.58    -69.08                                   
REMARK 500    PRO A 371     -157.99    -54.04                                   
REMARK 500    VAL A 372      108.52    -25.67                                   
REMARK 500    LEU A 379     -176.31    165.10                                   
REMARK 500    GLN A 391      -20.22     76.73                                   
REMARK 500    TRP A 410      -46.13   -156.68                                   
REMARK 500    ASN A 411        6.35     51.54                                   
REMARK 500    LYS A 419      158.51    -44.84                                   
REMARK 500    PHE A 473       -6.01     73.96                                   
REMARK 500    LYS A 531      108.98    -57.59                                   
REMARK 500    HIS A 532      155.11    -39.42                                   
REMARK 500    PRO A 548      162.95    -48.76                                   
REMARK 500    LEU A 555      -70.71    -53.57                                   
REMARK 500    LEU A 611       -5.70    -59.84                                   
REMARK 500    GLU A 638      -49.55    -21.09                                   
REMARK 500    LYS A 683      -71.16    -60.26                                   
REMARK 500    ARG A 690      -76.95    -75.10                                   
REMARK 500    ILE A 691      -45.39    -21.81                                   
REMARK 500    TYR A 757      153.28    -48.55                                   
REMARK 500    ASP A 758     -151.31    -95.84                                   
REMARK 500    SER A 777      -78.99   -158.70                                   
REMARK 500    ASP A 788       73.53   -171.81                                   
REMARK 500    ALA A 797       73.32   -104.72                                   
REMARK 500    SER A 806      151.41    -37.92                                   
REMARK 500    LYS A 809       83.84     45.12                                   
REMARK 500    GLU A 814      135.69   -175.08                                   
REMARK 500    ALA A 818      -11.21    -45.31                                   
REMARK 500    LEU A 823      -73.43    -54.58                                   
REMARK 500    SER A 824     -168.37    -77.22                                   
REMARK 500    GLU A 826      142.73    -37.96                                   
REMARK 500    PHE A 832      109.36    -55.58                                   
REMARK 500    SER A 859       70.58     56.16                                   
REMARK 500    CYS A 869      108.79   -161.05                                   
REMARK 500    THR A 887     -178.96    -67.74                                   
REMARK 500    LEU A 907      -72.01    -48.95                                   
REMARK 500    TYR A 935       -6.70    -56.55                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      65 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE L64 A 1109                
DBREF  3IBE A  144  1102  UNP    P48736   PK3CG_HUMAN    144   1102             
SEQADV 3IBE MET A  143  UNP  P48736              EXPRESSION TAG                 
SEQADV 3IBE ARG A  459  UNP  P48736    GLN   459 VARIANT                        
SEQADV 3IBE HIS A 1103  UNP  P48736              EXPRESSION TAG                 
SEQADV 3IBE HIS A 1104  UNP  P48736              EXPRESSION TAG                 
SEQADV 3IBE HIS A 1105  UNP  P48736              EXPRESSION TAG                 
SEQADV 3IBE HIS A 1106  UNP  P48736              EXPRESSION TAG                 
SEQADV 3IBE HIS A 1107  UNP  P48736              EXPRESSION TAG                 
SEQADV 3IBE HIS A 1108  UNP  P48736              EXPRESSION TAG                 
SEQRES   1 A  966  MET SER GLU GLU SER GLN ALA PHE GLN ARG GLN LEU THR          
SEQRES   2 A  966  ALA LEU ILE GLY TYR ASP VAL THR ASP VAL SER ASN VAL          
SEQRES   3 A  966  HIS ASP ASP GLU LEU GLU PHE THR ARG ARG GLY LEU VAL          
SEQRES   4 A  966  THR PRO ARG MET ALA GLU VAL ALA SER ARG ASP PRO LYS          
SEQRES   5 A  966  LEU TYR ALA MET HIS PRO TRP VAL THR SER LYS PRO LEU          
SEQRES   6 A  966  PRO GLU TYR LEU TRP LYS LYS ILE ALA ASN ASN CYS ILE          
SEQRES   7 A  966  PHE ILE VAL ILE HIS ARG SER THR THR SER GLN THR ILE          
SEQRES   8 A  966  LYS VAL SER PRO ASP ASP THR PRO GLY ALA ILE LEU GLN          
SEQRES   9 A  966  SER PHE PHE THR LYS MET ALA LYS LYS LYS SER LEU MET          
SEQRES  10 A  966  ASP ILE PRO GLU SER GLN SER GLU GLN ASP PHE VAL LEU          
SEQRES  11 A  966  ARG VAL CYS GLY ARG ASP GLU TYR LEU VAL GLY GLU THR          
SEQRES  12 A  966  PRO ILE LYS ASN PHE GLN TRP VAL ARG HIS CYS LEU LYS          
SEQRES  13 A  966  ASN GLY GLU GLU ILE HIS VAL VAL LEU ASP THR PRO PRO          
SEQRES  14 A  966  ASP PRO ALA LEU ASP GLU VAL ARG LYS GLU GLU TRP PRO          
SEQRES  15 A  966  LEU VAL ASP ASP CYS THR GLY VAL THR GLY TYR HIS GLU          
SEQRES  16 A  966  GLN LEU THR ILE HIS GLY LYS ASP HIS GLU SER VAL PHE          
SEQRES  17 A  966  THR VAL SER LEU TRP ASP CYS ASP ARG LYS PHE ARG VAL          
SEQRES  18 A  966  LYS ILE ARG GLY ILE ASP ILE PRO VAL LEU PRO ARG ASN          
SEQRES  19 A  966  THR ASP LEU THR VAL PHE VAL GLU ALA ASN ILE GLN HIS          
SEQRES  20 A  966  GLY GLN GLN VAL LEU CYS GLN ARG ARG THR SER PRO LYS          
SEQRES  21 A  966  PRO PHE THR GLU GLU VAL LEU TRP ASN VAL TRP LEU GLU          
SEQRES  22 A  966  PHE SER ILE LYS ILE LYS ASP LEU PRO LYS GLY ALA LEU          
SEQRES  23 A  966  LEU ASN LEU GLN ILE TYR CYS GLY LYS ALA PRO ALA LEU          
SEQRES  24 A  966  SER SER LYS ALA SER ALA GLU SER PRO SER SER GLU SER          
SEQRES  25 A  966  LYS GLY LYS VAL ARG LEU LEU TYR TYR VAL ASN LEU LEU          
SEQRES  26 A  966  LEU ILE ASP HIS ARG PHE LEU LEU ARG ARG GLY GLU TYR          
SEQRES  27 A  966  VAL LEU HIS MET TRP GLN ILE SER GLY LYS GLY GLU ASP          
SEQRES  28 A  966  GLN GLY SER PHE ASN ALA ASP LYS LEU THR SER ALA THR          
SEQRES  29 A  966  ASN PRO ASP LYS GLU ASN SER MET SER ILE SER ILE LEU          
SEQRES  30 A  966  LEU ASP ASN TYR CYS HIS PRO ILE ALA LEU PRO LYS HIS          
SEQRES  31 A  966  GLN PRO THR PRO ASP PRO GLU GLY ASP ARG VAL ARG ALA          
SEQRES  32 A  966  GLU MET PRO ASN GLN LEU ARG LYS GLN LEU GLU ALA ILE          
SEQRES  33 A  966  ILE ALA THR ASP PRO LEU ASN PRO LEU THR ALA GLU ASP          
SEQRES  34 A  966  LYS GLU LEU LEU TRP HIS PHE ARG TYR GLU SER LEU LYS          
SEQRES  35 A  966  HIS PRO LYS ALA TYR PRO LYS LEU PHE SER SER VAL LYS          
SEQRES  36 A  966  TRP GLY GLN GLN GLU ILE VAL ALA LYS THR TYR GLN LEU          
SEQRES  37 A  966  LEU ALA ARG ARG GLU VAL TRP ASP GLN SER ALA LEU ASP          
SEQRES  38 A  966  VAL GLY LEU THR MET GLN LEU LEU ASP CYS ASN PHE SER          
SEQRES  39 A  966  ASP GLU ASN VAL ARG ALA ILE ALA VAL GLN LYS LEU GLU          
SEQRES  40 A  966  SER LEU GLU ASP ASP ASP VAL LEU HIS TYR LEU LEU GLN          
SEQRES  41 A  966  LEU VAL GLN ALA VAL LYS PHE GLU PRO TYR HIS ASP SER          
SEQRES  42 A  966  ALA LEU ALA ARG PHE LEU LEU LYS ARG GLY LEU ARG ASN          
SEQRES  43 A  966  LYS ARG ILE GLY HIS PHE LEU PHE TRP PHE LEU ARG SER          
SEQRES  44 A  966  GLU ILE ALA GLN SER ARG HIS TYR GLN GLN ARG PHE ALA          
SEQRES  45 A  966  VAL ILE LEU GLU ALA TYR LEU ARG GLY CYS GLY THR ALA          
SEQRES  46 A  966  MET LEU HIS ASP PHE THR GLN GLN VAL GLN VAL ILE GLU          
SEQRES  47 A  966  MET LEU GLN LYS VAL THR LEU ASP ILE LYS SER LEU SER          
SEQRES  48 A  966  ALA GLU LYS TYR ASP VAL SER SER GLN VAL ILE SER GLN          
SEQRES  49 A  966  LEU LYS GLN LYS LEU GLU ASN LEU GLN ASN SER GLN LEU          
SEQRES  50 A  966  PRO GLU SER PHE ARG VAL PRO TYR ASP PRO GLY LEU LYS          
SEQRES  51 A  966  ALA GLY ALA LEU ALA ILE GLU LYS CYS LYS VAL MET ALA          
SEQRES  52 A  966  SER LYS LYS LYS PRO LEU TRP LEU GLU PHE LYS CYS ALA          
SEQRES  53 A  966  ASP PRO THR ALA LEU SER ASN GLU THR ILE GLY ILE ILE          
SEQRES  54 A  966  PHE LYS HIS GLY ASP ASP LEU ARG GLN ASP MET LEU ILE          
SEQRES  55 A  966  LEU GLN ILE LEU ARG ILE MET GLU SER ILE TRP GLU THR          
SEQRES  56 A  966  GLU SER LEU ASP LEU CYS LEU LEU PRO TYR GLY CYS ILE          
SEQRES  57 A  966  SER THR GLY ASP LYS ILE GLY MET ILE GLU ILE VAL LYS          
SEQRES  58 A  966  ASP ALA THR THR ILE ALA LYS ILE GLN GLN SER THR VAL          
SEQRES  59 A  966  GLY ASN THR GLY ALA PHE LYS ASP GLU VAL LEU ASN HIS          
SEQRES  60 A  966  TRP LEU LYS GLU LYS SER PRO THR GLU GLU LYS PHE GLN          
SEQRES  61 A  966  ALA ALA VAL GLU ARG PHE VAL TYR SER CYS ALA GLY TYR          
SEQRES  62 A  966  CYS VAL ALA THR PHE VAL LEU GLY ILE GLY ASP ARG HIS          
SEQRES  63 A  966  ASN ASP ASN ILE MET ILE THR GLU THR GLY ASN LEU PHE          
SEQRES  64 A  966  HIS ILE ASP PHE GLY HIS ILE LEU GLY ASN TYR LYS SER          
SEQRES  65 A  966  PHE LEU GLY ILE ASN LYS GLU ARG VAL PRO PHE VAL LEU          
SEQRES  66 A  966  THR PRO ASP PHE LEU PHE VAL MET GLY THR SER GLY LYS          
SEQRES  67 A  966  LYS THR SER PRO HIS PHE GLN LYS PHE GLN ASP ILE CYS          
SEQRES  68 A  966  VAL LYS ALA TYR LEU ALA LEU ARG HIS HIS THR ASN LEU          
SEQRES  69 A  966  LEU ILE ILE LEU PHE SER MET MET LEU MET THR GLY MET          
SEQRES  70 A  966  PRO GLN LEU THR SER LYS GLU ASP ILE GLU TYR ILE ARG          
SEQRES  71 A  966  ASP ALA LEU THR VAL GLY LYS ASN GLU GLU ASP ALA LYS          
SEQRES  72 A  966  LYS TYR PHE LEU ASP GLN ILE GLU VAL CYS ARG ASP LYS          
SEQRES  73 A  966  GLY TRP THR VAL GLN PHE ASN TRP PHE LEU HIS LEU VAL          
SEQRES  74 A  966  LEU GLY ILE LYS GLN GLY GLU LYS HIS SER ALA HIS HIS          
SEQRES  75 A  966  HIS HIS HIS HIS                                              
HET    SO4  A   1       5                                                       
HET    L64  A1109      45                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     L64 1-(4-{4-MORPHOLIN-4-YL-1-[1-(PYRIDIN-3-YLCARBONYL)               
HETNAM   2 L64  PIPERIDIN-4-YL]-1H-PYRAZOLO[3,4-D]PYRIMIDIN-6-                  
HETNAM   3 L64  YL}PHENYL)-3-PYRIDIN-4-YLUREA                                   
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  L64    C32 H32 N10 O3                                               
FORMUL   4  HOH   *42(H2 O)                                                     
HELIX    1   1 ALA A  149  GLY A  159  1                                  11    
HELIX    2   2 ASP A  171  LEU A  180  1                                  10    
HELIX    3   3 LEU A  180  ARG A  191  1                                  12    
HELIX    4   4 ASP A  192  HIS A  199  1                                   8    
HELIX    5   5 PRO A  208  LYS A  213  1                                   6    
HELIX    6   6 PRO A  241  THR A  250  1                                  10    
HELIX    7   7 PRO A  286  ASN A  289  5                                   4    
HELIX    8   8 PHE A  290  ASN A  299  1                                  10    
HELIX    9   9 ASP A  312  ASP A  316  5                                   5    
HELIX   10  10 ASN A  498  THR A  503  5                                   6    
HELIX   11  11 PRO A  548  ILE A  559  1                                  12    
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 HIS A  585  LYS A  587  5                                   3    
HELIX   15  15 ALA A  588  PHE A  593  1                                   6    
HELIX   16  16 GLN A  600  GLN A  609  1                                  10    
HELIX   17  17 LEU A  610  ARG A  613  5                                   4    
HELIX   18  18 ARG A  614  SER A  620  1                                   7    
HELIX   19  19 ASP A  623  LEU A  630  1                                   8    
HELIX   20  20 ASP A  637  GLU A  649  1                                  13    
HELIX   21  21 GLU A  652  ALA A  666  1                                  15    
HELIX   22  22 VAL A  667  PHE A  669  5                                   3    
HELIX   23  23 SER A  675  ASN A  688  1                                  14    
HELIX   24  24 ASN A  688  ALA A  704  1                                  17    
HELIX   25  25 TYR A  709  ARG A  722  1                                  14    
HELIX   26  26 GLY A  725  SER A  751  1                                  27    
HELIX   27  27 SER A  760  ASN A  776  1                                  17    
HELIX   28  28 ILE A  798  CYS A  801  5                                   4    
HELIX   29  29 LEU A  838  TRP A  855  1                                  18    
HELIX   30  30 ILE A  888  GLN A  893  1                                   6    
HELIX   31  31 GLU A  905  LYS A  914  1                                  10    
HELIX   32  32 GLU A  919  LEU A  942  1                                  24    
HELIX   33  33 THR A  988  GLY A  996  1                                   9    
HELIX   34  34 HIS A 1005  HIS A 1023  1                                  19    
HELIX   35  35 HIS A 1023  MET A 1039  1                                  17    
HELIX   36  36 ILE A 1048  LEU A 1055  1                                   8    
HELIX   37  37 ASN A 1060  CYS A 1075  1                                  16    
HELIX   38  38 TRP A 1080  HIS A 1089  1                                  10    
SHEET    1   A 2 ILE A 220  PHE A 221  0                                        
SHEET    2   A 2 LYS A 234  VAL A 235 -1  O  VAL A 235   N  ILE A 220           
SHEET    1   B 4 VAL A 223  ILE A 224  0                                        
SHEET    2   B 4 HIS A 304  ASP A 308  1  O  VAL A 305   N  VAL A 223           
SHEET    3   B 4 VAL A 271  VAL A 274 -1  N  ARG A 273   O  VAL A 306           
SHEET    4   B 4 TYR A 280  LEU A 281 -1  O  LEU A 281   N  LEU A 272           
SHEET    1   C 4 GLU A 407  LYS A 419  0                                        
SHEET    2   C 4 LYS A 360  ASP A 369 -1  N  ILE A 368   O  VAL A 408           
SHEET    3   C 4 SER A 517  LEU A 520 -1  O  LEU A 519   N  LYS A 364           
SHEET    4   C 4 GLY A 478  VAL A 481 -1  N  GLY A 478   O  LEU A 520           
SHEET    1   D 5 GLN A 392  ARG A 397  0                                        
SHEET    2   D 5 THR A 380  HIS A 389 -1  N  ILE A 387   O  CYS A 395           
SHEET    3   D 5 LEU A 428  GLY A 436 -1  O  ASN A 430   N  ASN A 386           
SHEET    4   D 5 ARG A 459  LEU A 467 -1  O  LEU A 466   N  LEU A 429           
SHEET    5   D 5 TRP A 485  GLN A 486 -1  O  TRP A 485   N  TYR A 463           
SHEET    1   E 3 PHE A 783  ARG A 784  0                                        
SHEET    2   E 3 LYS A 792  LEU A 796 -1  O  ALA A 793   N  PHE A 783           
SHEET    3   E 3 PHE A 815  CYS A 817 -1  O  LYS A 816   N  ALA A 795           
SHEET    1   F 5 LYS A 802  VAL A 803  0                                        
SHEET    2   F 5 LEU A 811  TRP A 812 -1  O  TRP A 812   N  LYS A 802           
SHEET    3   F 5 ILE A 831  HIS A 834 -1  O  PHE A 832   N  LEU A 811           
SHEET    4   F 5 ILE A 876  ILE A 879 -1  O  ILE A 879   N  ILE A 831           
SHEET    5   F 5 CYS A 869  SER A 871 -1  N  ILE A 870   O  MET A 878           
SHEET    1   G 3 ALA A 885  THR A 887  0                                        
SHEET    2   G 3 ILE A 952  THR A 955 -1  O  ILE A 954   N  THR A 886           
SHEET    3   G 3 LEU A 960  HIS A 962 -1  O  PHE A 961   N  MET A 953           
SITE     1 AC1  4 PRO A 206  LEU A 207  TRP A 212  LYS A 288                    
SITE     1 AC2 18 MET A 804  ALA A 805  SER A 806  ILE A 831                    
SITE     2 AC2 18 LYS A 833  ASP A 836  ASP A 837  LEU A 838                    
SITE     3 AC2 18 GLN A 840  ASP A 841  ILE A 879  GLU A 880                    
SITE     4 AC2 18 ILE A 881  VAL A 882  ASP A 950  MET A 953                    
SITE     5 AC2 18 ASP A 964  GLY A 966                                          
CRYST1  145.159   68.458  106.901  90.00  94.80  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      0.006889  0.000000  0.000578        0.00000                         
SCALE2      0.000000  0.014607  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009387        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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