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Database: PDB
Entry: 5G2N
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HEADER    TRANSFERASE                             11-APR-16   5G2N              
TITLE     X-RAY STRUCTURE OF PI3KINASE GAMMA IN COMPLEX WITH                    
TITLE    2 COPANLISIB                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3  SUBUNIT GAMMA ISOFORM;                                              
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: CATALYTIC SUBUNIT GAMMA, RESIDUES 144-1102;                
COMPND   6 EC: 2.7.1.137, 2.7.1.153;                                            
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SCHAEFER,W.J.SCOTT,M.F.HENTEMANN,R.B.ROWLEY,C.O.BULL,S.JENKINS,     
AUTHOR   2 A.M.BULLION,J.JOHNSON,A.REDMAN,A.H.ROBBINS,W.ESLER,R.P.FRACASSO,     
AUTHOR   3 T.GARRISON,M.HAMILTON,M.MICHELS,J.E.WOOD,D.P.WILKIE,H.XIAO,J.LEVY,   
AUTHOR   4 N.LIU,E.STASIK,M.BRANDS,J.LEFRANC                                    
REVDAT   3   10-AUG-16 5G2N    1       JRNL                                     
REVDAT   2   29-JUN-16 5G2N    1       JRNL                                     
REVDAT   1   20-APR-16 5G2N    0                                                
JRNL        AUTH   M.SCHAEFER,W.J.SCOTT,M.F.HENTEMANN,R.B.ROWLEY,C.O.BULL,      
JRNL        AUTH 2 S.JENKINS,A.M.BULLION,J.JOHNSON,A.REDMAN,A.H.ROBBINS,        
JRNL        AUTH 3 W.ESLER,R.P.FRACASSO,T.GARRISON,M.HAMILTON,M.MICHELS,        
JRNL        AUTH 4 J.E.WOOD,D.P.WILKIE,H.XIAO,J.LEVY,N.LIU,E.STASIK,M.BRANDS,   
JRNL        AUTH 5 J.LEFRANC                                                    
JRNL        TITL   DISCOVERY AND SAR OF NOVEL 2,3-DIHYDROIMIDAZO(1,2-           
JRNL        TITL 2 C)QUINAZOLINE PI3K INHIBITORS: IDENTIFICATION OF COPANLISIB  
JRNL        TITL 3 (BAY 80-6946)                                                
JRNL        REF    CHEMMEDCHEM                   V.  11  1517 2016              
JRNL        REFN                   ISSN 1860-7179                               
JRNL        PMID   27310202                                                     
JRNL        DOI    10.1002/CMDC.201600148                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.68 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0124                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.68                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 61.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.95                          
REMARK   3   NUMBER OF REFLECTIONS             : 26776                          
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) : 0.21512                         
REMARK   3   R VALUE            (WORKING SET) : 0.21142                         
REMARK   3   FREE R VALUE                     : 0.28454                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1410                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.680                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.749                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1970                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.321                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 104                          
REMARK   3   BIN FREE R VALUE                    : 0.349                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6687                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 11                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.627                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.55                                                 
REMARK   3    B22 (A**2) : -5.58                                                
REMARK   3    B33 (A**2) : 0.66                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 2.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.394         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.418         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 48.274        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6845 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6623 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9263 ; 1.909 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15187 ; 1.078 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   812 ; 7.547 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   318 ;36.045 ;24.277       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1226 ;18.971 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    39 ;18.037 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1041 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7561 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1567 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3281 ; 1.314 ; 2.849       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3280 ; 1.314 ; 2.849       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4082 ; 2.213 ; 4.263       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3564 ; 1.303 ; 2.955       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP :     1                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   144        A  2001                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.6481  -1.5416  25.8449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0408 T22:   0.6747                                     
REMARK   3      T33:   0.0517 T12:  -0.0178                                     
REMARK   3      T13:   0.0207 T23:  -0.0424                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4507 L22:   1.4049                                     
REMARK   3      L33:   1.4765 L12:   0.5467                                     
REMARK   3      L13:   0.0792 L23:   0.0285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0161 S12:  -0.0393 S13:   0.0024                       
REMARK   3      S21:  -0.0179 S22:   0.0862 S23:  -0.2379                       
REMARK   3      S31:  -0.2435 S32:   0.0909 S33:  -0.1023                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 5G2N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-16.                  
REMARK 100 THE PDBE ID CODE IS EBI-66669.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PILATUS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29372                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.68                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.78                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 2.5                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.67                               
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: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG4000,0.15M (NH4)2SO4,             
REMARK 280  0.1M TRIS PH7.5                                                     
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       72.38100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.16800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       72.38100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.16800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   139                                                      
REMARK 465     LEU A   140                                                      
REMARK 465     LEU A   141                                                      
REMARK 465     GLY A   142                                                      
REMARK 465     SER A   143                                                      
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     PRO A   324                                                      
REMARK 465     LEU A   325                                                      
REMARK 465     VAL A   326                                                      
REMARK 465     ASP A   327                                                      
REMARK 465     ASP A   328                                                      
REMARK 465     CYS A   329                                                      
REMARK 465     THR A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     VAL A   332                                                      
REMARK 465     THR A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     TYR A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     GLN A   338                                                      
REMARK 465     LEU A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     ILE A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     ASP A   345                                                      
REMARK 465     HIS A   346                                                      
REMARK 465     GLU A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     VAL A   349                                                      
REMARK 465     PHE A   350                                                      
REMARK 465     THR A   351                                                      
REMARK 465     VAL A   352                                                      
REMARK 465     SER A   353                                                      
REMARK 465     LEU A   354                                                      
REMARK 465     TRP A   355                                                      
REMARK 465     ASP A   356                                                      
REMARK 465     PRO A   374                                                      
REMARK 465     ARG A   375                                                      
REMARK 465     ASN A   376                                                      
REMARK 465     THR A   377                                                      
REMARK 465     GLY A   436                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     ALA A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 465     ALA A   440                                                      
REMARK 465     LEU A   441                                                      
REMARK 465     SER A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     ALA A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     ALA A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     SER A   449                                                      
REMARK 465     PRO A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     SER A   452                                                      
REMARK 465     GLU A   453                                                      
REMARK 465     SER A   454                                                      
REMARK 465     LYS A   455                                                      
REMARK 465     GLY A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     VAL A   458                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     GLY A   491                                                      
REMARK 465     GLU A   492                                                      
REMARK 465     ASP A   493                                                      
REMARK 465     GLN A   494                                                      
REMARK 465     GLY A   495                                                      
REMARK 465     SER A   496                                                      
REMARK 465     TYR A   523                                                      
REMARK 465     CYS A   524                                                      
REMARK 465     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     GLN A   893                                                      
REMARK 465     SER A   894                                                      
REMARK 465     THR A   895                                                      
REMARK 465     VAL A   896                                                      
REMARK 465     GLY A   897                                                      
REMARK 465     ASN A   898                                                      
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     LYS A   980                                                      
REMARK 465     GLN A  1041                                                      
REMARK 465     LEU A  1042                                                      
REMARK 465     THR A  1043                                                      
REMARK 465     SER A  1044                                                      
REMARK 465     LYS A  1045                                                      
REMARK 465     GLU A  1046                                                      
REMARK 465     LEU A  1092                                                      
REMARK 465     GLY A  1093                                                      
REMARK 465     ILE A  1094                                                      
REMARK 465     LYS A  1095                                                      
REMARK 465     GLN A  1096                                                      
REMARK 465     GLY A  1097                                                      
REMARK 465     GLU A  1098                                                      
REMARK 465     LYS A  1099                                                      
REMARK 465     HIS A  1100                                                      
REMARK 465     SER A  1101                                                      
REMARK 465     ALA A  1102                                                      
REMARK 465     GLU A  1103                                                      
REMARK 465     PHE A  1104                                                      
REMARK 465     GLY A  1105                                                      
REMARK 465     LEU A  1106                                                      
REMARK 465     VAL A  1107                                                      
REMARK 465     PRO A  1108                                                      
REMARK 465     ARG A  1109                                                      
REMARK 465     GLY A  1110                                                      
REMARK 465     SER A  1111                                                      
REMARK 465     GLY A  1112                                                      
REMARK 465     HIS A  1113                                                      
REMARK 465     HIS A  1114                                                      
REMARK 465     HIS A  1115                                                      
REMARK 465     HIS A  1116                                                      
REMARK 465     HIS A  1117                                                      
REMARK 465     HIS A  1118                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 145    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 194    CD   CE   NZ                                        
REMARK 470     LYS A 213    CG   CD   CE   NZ                                   
REMARK 470     ARG A 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 231    CD   OE1  NE2                                       
REMARK 470     LYS A 807    CD   CE   NZ                                        
REMARK 470     HIS A 967    CG   ND1  CD2  CE1  NE2                             
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  145   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  194   CD   CE   NZ                                        
REMARK 480     LYS A  213   CG   CD   CE   NZ                                   
REMARK 480     ARG A  226   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN A  231   CD   OE1  NE2                                       
REMARK 480     LYS A  807   CD   CE   NZ                                        
REMARK 480     HIS A  967   CG   ND1  CD2  CE1  NE2                             
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   OD1  ASP A   161     OG1  THR A   163              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A 659   CE1   TYR A 659   CZ     -0.099                       
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    ARG A 366   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A 366   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    CYS A 633   CA  -  CB  -  SG  ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ARG A 641   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 684   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 707   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    CYS A 932   CA  -  CB  -  SG  ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG A 947   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 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    TYR A 160      142.58   -170.17                                   
REMARK 500    ASN A 167       54.61   -107.75                                   
REMARK 500    HIS A 199       60.20     27.56                                   
REMARK 500    ASN A 217       12.22   -157.88                                   
REMARK 500    ARG A 226      -71.15    -73.62                                   
REMARK 500    SER A 227      -52.90   -171.16                                   
REMARK 500    THR A 228      -66.92    -95.43                                   
REMARK 500    GLU A 279      130.76   -177.13                                   
REMARK 500    ILE A 287      -25.06    -38.64                                   
REMARK 500    ARG A 319      150.04    -47.37                                   
REMARK 500    LEU A 379     -159.48    -77.62                                   
REMARK 500    GLN A 391      -30.57     75.39                                   
REMARK 500    HIS A 471       -5.77    -55.94                                   
REMARK 500    ASP A 509       78.50    -67.26                                   
REMARK 500    ILE A 527      -74.41   -136.05                                   
REMARK 500    PHE A 578       53.19    -98.09                                   
REMARK 500    ARG A 613       42.16    -94.05                                   
REMARK 500    GLU A 615      -35.11    -36.21                                   
REMARK 500    GLN A 705      -29.22   -143.06                                   
REMARK 500    SER A 753      115.11   -171.61                                   
REMARK 500    TYR A 757      -42.43     -1.49                                   
REMARK 500    ASP A 758      101.87    -52.22                                   
REMARK 500    GLN A 775      -70.62    -45.76                                   
REMARK 500    SER A 777       53.95   -155.45                                   
REMARK 500    GLN A 778      -63.34   -172.19                                   
REMARK 500    ASP A 788       71.23   -157.06                                   
REMARK 500    ALA A 797       86.29    -69.14                                   
REMARK 500    PRO A 866       91.40    -68.98                                   
REMARK 500    CYS A 869      127.64   -175.47                                   
REMARK 500    ASP A 964       85.33     62.81                                   
REMARK 500    GLU A1049      -45.47    -23.72                                   
REMARK 500    THR A1081      -61.34    -17.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ILE A 287        24.9      L          L   OUTSIDE RANGE           
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 6E2 A2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A2092                 
DBREF  5G2N A  144  1102  UNP    P48736   PK3CG_HUMAN    144   1102             
SEQADV 5G2N MET A  139  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N LEU A  140  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N LEU A  141  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N GLY A  142  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N SER A  143  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N GLU A 1103  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N PHE A 1104  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N GLY A 1105  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N LEU A 1106  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N VAL A 1107  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N PRO A 1108  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N ARG A 1109  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N GLY A 1110  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N SER A 1111  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N GLY A 1112  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N HIS A 1113  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N HIS A 1114  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N HIS A 1115  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N HIS A 1116  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N HIS A 1117  UNP  P48736              EXPRESSION TAG                 
SEQADV 5G2N HIS A 1118  UNP  P48736              EXPRESSION TAG                 
SEQRES   1 A  980  MET LEU LEU GLY SER SER GLU GLU SER GLN ALA PHE GLN          
SEQRES   2 A  980  ARG GLN LEU THR ALA LEU ILE GLY TYR ASP VAL THR ASP          
SEQRES   3 A  980  VAL SER ASN VAL HIS ASP ASP GLU LEU GLU PHE THR ARG          
SEQRES   4 A  980  ARG GLY LEU VAL THR PRO ARG MET ALA GLU VAL ALA SER          
SEQRES   5 A  980  ARG ASP PRO LYS LEU TYR ALA MET HIS PRO TRP VAL THR          
SEQRES   6 A  980  SER LYS PRO LEU PRO GLU TYR LEU TRP LYS LYS ILE ALA          
SEQRES   7 A  980  ASN ASN CYS ILE PHE ILE VAL ILE HIS ARG SER THR THR          
SEQRES   8 A  980  SER GLN THR ILE LYS VAL SER PRO ASP ASP THR PRO GLY          
SEQRES   9 A  980  ALA ILE LEU GLN SER PHE PHE THR LYS MET ALA LYS LYS          
SEQRES  10 A  980  LYS SER LEU MET ASP ILE PRO GLU SER GLN SER GLU GLN          
SEQRES  11 A  980  ASP PHE VAL LEU ARG VAL CYS GLY ARG ASP GLU TYR LEU          
SEQRES  12 A  980  VAL GLY GLU THR PRO ILE LYS ASN PHE GLN TRP VAL ARG          
SEQRES  13 A  980  HIS CYS LEU LYS ASN GLY GLU GLU ILE HIS VAL VAL LEU          
SEQRES  14 A  980  ASP THR PRO PRO ASP PRO ALA LEU ASP GLU VAL ARG LYS          
SEQRES  15 A  980  GLU GLU TRP PRO LEU VAL ASP ASP CYS THR GLY VAL THR          
SEQRES  16 A  980  GLY TYR HIS GLU GLN LEU THR ILE HIS GLY LYS ASP HIS          
SEQRES  17 A  980  GLU SER VAL PHE THR VAL SER LEU TRP ASP CYS ASP ARG          
SEQRES  18 A  980  LYS PHE ARG VAL LYS ILE ARG GLY ILE ASP ILE PRO VAL          
SEQRES  19 A  980  LEU PRO ARG ASN THR ASP LEU THR VAL PHE VAL GLU ALA          
SEQRES  20 A  980  ASN ILE GLN HIS GLY GLN GLN VAL LEU CYS GLN ARG ARG          
SEQRES  21 A  980  THR SER PRO LYS PRO PHE THR GLU GLU VAL LEU TRP ASN          
SEQRES  22 A  980  VAL TRP LEU GLU PHE SER ILE LYS ILE LYS ASP LEU PRO          
SEQRES  23 A  980  LYS GLY ALA LEU LEU ASN LEU GLN ILE TYR CYS GLY LYS          
SEQRES  24 A  980  ALA PRO ALA LEU SER SER LYS ALA SER ALA GLU SER PRO          
SEQRES  25 A  980  SER SER GLU SER LYS GLY LYS VAL GLN LEU LEU TYR TYR          
SEQRES  26 A  980  VAL ASN LEU LEU LEU ILE ASP HIS ARG PHE LEU LEU ARG          
SEQRES  27 A  980  ARG GLY GLU TYR VAL LEU HIS MET TRP GLN ILE SER GLY          
SEQRES  28 A  980  LYS GLY GLU ASP GLN GLY SER PHE ASN ALA ASP LYS LEU          
SEQRES  29 A  980  THR SER ALA THR ASN PRO ASP LYS GLU ASN SER MET SER          
SEQRES  30 A  980  ILE SER ILE LEU LEU ASP ASN TYR CYS HIS PRO ILE ALA          
SEQRES  31 A  980  LEU PRO LYS HIS GLN PRO THR PRO ASP PRO GLU GLY ASP          
SEQRES  32 A  980  ARG VAL ARG ALA GLU MET PRO ASN GLN LEU ARG LYS GLN          
SEQRES  33 A  980  LEU GLU ALA ILE ILE ALA THR ASP PRO LEU ASN PRO LEU          
SEQRES  34 A  980  THR ALA GLU ASP LYS GLU LEU LEU TRP HIS PHE ARG TYR          
SEQRES  35 A  980  GLU SER LEU LYS HIS PRO LYS ALA TYR PRO LYS LEU PHE          
SEQRES  36 A  980  SER SER VAL LYS TRP GLY GLN GLN GLU ILE VAL ALA LYS          
SEQRES  37 A  980  THR TYR GLN LEU LEU ALA ARG ARG GLU VAL TRP ASP GLN          
SEQRES  38 A  980  SER ALA LEU ASP VAL GLY LEU THR MET GLN LEU LEU ASP          
SEQRES  39 A  980  CYS ASN PHE SER ASP GLU ASN VAL ARG ALA ILE ALA VAL          
SEQRES  40 A  980  GLN LYS LEU GLU SER LEU GLU ASP ASP ASP VAL LEU HIS          
SEQRES  41 A  980  TYR LEU LEU GLN LEU VAL GLN ALA VAL LYS PHE GLU PRO          
SEQRES  42 A  980  TYR HIS ASP SER ALA LEU ALA ARG PHE LEU LEU LYS ARG          
SEQRES  43 A  980  GLY LEU ARG ASN LYS ARG ILE GLY HIS PHE LEU PHE TRP          
SEQRES  44 A  980  PHE LEU ARG SER GLU ILE ALA GLN SER ARG HIS TYR GLN          
SEQRES  45 A  980  GLN ARG PHE ALA VAL ILE LEU GLU ALA TYR LEU ARG GLY          
SEQRES  46 A  980  CYS GLY THR ALA MET LEU HIS ASP PHE THR GLN GLN VAL          
SEQRES  47 A  980  GLN VAL ILE GLU MET LEU GLN LYS VAL THR LEU ASP ILE          
SEQRES  48 A  980  LYS SER LEU SER ALA GLU LYS TYR ASP VAL SER SER GLN          
SEQRES  49 A  980  VAL ILE SER GLN LEU LYS GLN LYS LEU GLU ASN LEU GLN          
SEQRES  50 A  980  ASN SER GLN LEU PRO GLU SER PHE ARG VAL PRO TYR ASP          
SEQRES  51 A  980  PRO GLY LEU LYS ALA GLY ALA LEU ALA ILE GLU LYS CYS          
SEQRES  52 A  980  LYS VAL MET ALA SER LYS LYS LYS PRO LEU TRP LEU GLU          
SEQRES  53 A  980  PHE LYS CYS ALA ASP PRO THR ALA LEU SER ASN GLU THR          
SEQRES  54 A  980  ILE GLY ILE ILE PHE LYS HIS GLY ASP ASP LEU ARG GLN          
SEQRES  55 A  980  ASP MET LEU ILE LEU GLN ILE LEU ARG ILE MET GLU SER          
SEQRES  56 A  980  ILE TRP GLU THR GLU SER LEU ASP LEU CYS LEU LEU PRO          
SEQRES  57 A  980  TYR GLY CYS ILE SER THR GLY ASP LYS ILE GLY MET ILE          
SEQRES  58 A  980  GLU ILE VAL LYS ASP ALA THR THR ILE ALA LYS ILE GLN          
SEQRES  59 A  980  GLN SER THR VAL GLY ASN THR GLY ALA PHE LYS ASP GLU          
SEQRES  60 A  980  VAL LEU ASN HIS TRP LEU LYS GLU LYS SER PRO THR GLU          
SEQRES  61 A  980  GLU LYS PHE GLN ALA ALA VAL GLU ARG PHE VAL TYR SER          
SEQRES  62 A  980  CYS ALA GLY TYR CYS VAL ALA THR PHE VAL LEU GLY ILE          
SEQRES  63 A  980  GLY ASP ARG HIS ASN ASP ASN ILE MET ILE THR GLU THR          
SEQRES  64 A  980  GLY ASN LEU PHE HIS ILE ASP PHE GLY HIS ILE LEU GLY          
SEQRES  65 A  980  ASN TYR LYS SER PHE LEU GLY ILE ASN LYS GLU ARG VAL          
SEQRES  66 A  980  PRO PHE VAL LEU THR PRO ASP PHE LEU PHE VAL MET GLY          
SEQRES  67 A  980  THR SER GLY LYS LYS THR SER PRO HIS PHE GLN LYS PHE          
SEQRES  68 A  980  GLN ASP ILE CYS VAL LYS ALA TYR LEU ALA LEU ARG HIS          
SEQRES  69 A  980  HIS THR ASN LEU LEU ILE ILE LEU PHE SER MET MET LEU          
SEQRES  70 A  980  MET THR GLY MET PRO GLN LEU THR SER LYS GLU ASP ILE          
SEQRES  71 A  980  GLU TYR ILE ARG ASP ALA LEU THR VAL GLY LYS ASN GLU          
SEQRES  72 A  980  GLU ASP ALA LYS LYS TYR PHE LEU ASP GLN ILE GLU VAL          
SEQRES  73 A  980  CYS ARG ASP LYS GLY TRP THR VAL GLN PHE ASN TRP PHE          
SEQRES  74 A  980  LEU HIS LEU VAL LEU GLY ILE LYS GLN GLY GLU LYS HIS          
SEQRES  75 A  980  SER ALA GLU PHE GLY LEU VAL PRO ARG GLY SER GLY HIS          
SEQRES  76 A  980  HIS HIS HIS HIS HIS                                          
HET    6E2  A2001      35                                                       
HET    SO4  A2092       5                                                       
HETNAM     6E2 2-AZANYL-~{N}-[7-METHOXY-8-(3-MORPHOLIN-4-                       
HETNAM   2 6E2  YLPROPOXY)-2,3-DIHYDROIMIDAZO[1,2-C]QUINAZOLIN-                 
HETNAM   3 6E2  5-YL]PYRIMIDINE-5-CARBOXAMIDE                                   
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  6E2    C23 H28 N8 O4                                                
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *11(H2 O)                                                     
HELIX    1   1 GLU A  145  GLY A  159  1                                  15    
HELIX    2   2 ASP A  171  LEU A  180  1                                  10    
HELIX    3   3 LEU A  180  ALA A  189  1                                  10    
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 LYS A  214  ALA A  216  5                                   3    
HELIX    7   7 THR A  240  THR A  250  1                                  11    
HELIX    8   8 PRO A  286  ASN A  289  5                                   4    
HELIX    9   9 PHE A  290  ASN A  299  1                                  10    
HELIX   10  10 ASP A  312  GLU A  317  5                                   6    
HELIX   11  11 LYS A  421  LEU A  423  5                                   3    
HELIX   12  12 ASN A  498  THR A  503  5                                   6    
HELIX   13  13 PRO A  548  THR A  561  1                                  14    
HELIX   14  14 THR A  568  PHE A  578  1                                  11    
HELIX   15  15 PHE A  578  LYS A  584  1                                   7    
HELIX   16  16 HIS A  585  LYS A  587  5                                   3    
HELIX   17  17 ALA A  588  SER A  594  1                                   7    
HELIX   18  18 GLN A  600  ALA A  612  1                                  13    
HELIX   19  19 ARG A  614  SER A  620  1                                   7    
HELIX   20  20 ASP A  623  LEU A  630  1                                   8    
HELIX   21  21 ASP A  637  GLU A  649  1                                  13    
HELIX   22  22 GLU A  652  ALA A  666  1                                  15    
HELIX   23  23 VAL A  667  GLU A  670  5                                   4    
HELIX   24  24 SER A  675  ASN A  688  1                                  14    
HELIX   25  25 ASN A  688  ALA A  704  1                                  17    
HELIX   26  26 TYR A  709  GLY A  725  1                                  17    
HELIX   27  27 GLY A  725  SER A  751  1                                  27    
HELIX   28  28 SER A  760  SER A  777  1                                  18    
HELIX   29  29 ILE A  798  CYS A  801  5                                   4    
HELIX   30  30 ASP A  837  THR A  857  1                                  21    
HELIX   31  31 ILE A  888  GLN A  892  1                                   5    
HELIX   32  32 GLU A  905  GLU A  913  1                                   9    
HELIX   33  33 THR A  917  GLY A  943  1                                  27    
HELIX   34  34 HIS A  948  ASP A  950  5                                   3    
HELIX   35  35 THR A  988  MET A  995  1                                   8    
HELIX   36  36 SER A 1003  HIS A 1022  1                                  20    
HELIX   37  37 HIS A 1023  MET A 1039  1                                  17    
HELIX   38  38 ILE A 1048  LEU A 1055  1                                   8    
HELIX   39  39 ASN A 1060  GLY A 1079  1                                  20    
HELIX   40  40 GLY A 1079  VAL A 1091  1                                  13    
SHEET    1  AA 5 SER A 230  VAL A 235  0                                        
SHEET    2  AA 5 ILE A 220  HIS A 225 -1  O  ILE A 220   N  VAL A 235           
SHEET    3  AA 5 ILE A 303  ASP A 308  1  O  ILE A 303   N  VAL A 223           
SHEET    4  AA 5 VAL A 271  VAL A 274 -1  O  VAL A 271   N  ASP A 308           
SHEET    5  AA 5 TYR A 280  LEU A 281 -1  O  LEU A 281   N  LEU A 272           
SHEET    1  AB 4 GLU A 407  LYS A 419  0                                        
SHEET    2  AB 4 LYS A 360  ASP A 369 -1  O  PHE A 361   N  PHE A 416           
SHEET    3  AB 4 SER A 515  LEU A 520 -1  O  SER A 515   N  ASP A 369           
SHEET    4  AB 4 GLY A 478  HIS A 483 -1  O  GLY A 478   N  LEU A 520           
SHEET    1  AC 2 GLN A 392  ARG A 398  0                                        
SHEET    2  AC 2 THR A 380  HIS A 389 -1  O  ALA A 385   N  ARG A 397           
SHEET    1  AD 2 LYS A 402  PRO A 403  0                                        
SHEET    2  AD 2 THR A 380  HIS A 389 -1  O  VAL A 381   N  LYS A 402           
SHEET    1  AE 5 TRP A 485  GLN A 486  0                                        
SHEET    2  AE 5 LEU A 460  LEU A 467 -1  O  TYR A 463   N  TRP A 485           
SHEET    3  AE 5 LEU A 428  TYR A 434 -1  O  LEU A 429   N  LEU A 466           
SHEET    4  AE 5 THR A 380  HIS A 389 -1  O  PHE A 382   N  TYR A 434           
SHEET    5  AE 5 GLN A 392  ARG A 398 -1  O  GLN A 392   N  HIS A 389           
SHEET    1  AF 5 TRP A 485  GLN A 486  0                                        
SHEET    2  AF 5 LEU A 460  LEU A 467 -1  O  TYR A 463   N  TRP A 485           
SHEET    3  AF 5 LEU A 428  TYR A 434 -1  O  LEU A 429   N  LEU A 466           
SHEET    4  AF 5 THR A 380  HIS A 389 -1  O  PHE A 382   N  TYR A 434           
SHEET    5  AF 5 LYS A 402  PRO A 403 -1  O  LYS A 402   N  VAL A 381           
SHEET    1  AG 6 PHE A 783  VAL A 785  0                                        
SHEET    2  AG 6 ASP A 788  LEU A 796 -1  N  ASP A 788   O  VAL A 785           
SHEET    3  AG 6 LEU A 811  CYS A 817 -1  O  LYS A 816   N  GLY A 794           
SHEET    4  AG 6 ILE A 828  HIS A 834 -1  O  ILE A 828   N  PHE A 815           
SHEET    5  AG 6 ILE A 876  GLU A 880 -1  O  GLY A 877   N  LYS A 833           
SHEET    6  AG 6 CYS A 869  GLY A 873 -1  O  ILE A 870   N  MET A 878           
SHEET    1  AH 4 PHE A 783  VAL A 785  0                                        
SHEET    2  AH 4 ASP A 788  LEU A 796 -1  N  ASP A 788   O  VAL A 785           
SHEET    3  AH 4 LEU A 811  CYS A 817 -1  O  LYS A 816   N  GLY A 794           
SHEET    4  AH 4 LYS A 802  VAL A 803  1  O  LYS A 802   N  TRP A 812           
SHEET    1  AI 3 ALA A 885  THR A 887  0                                        
SHEET    2  AI 3 ILE A 952  THR A 955 -1  O  ILE A 954   N  THR A 886           
SHEET    3  AI 3 LEU A 960  HIS A 962 -1  O  PHE A 961   N  MET A 953           
SITE     1 AC1 14 LYS A 802  TRP A 812  ILE A 831  LYS A 833                    
SITE     2 AC1 14 ASP A 836  LEU A 838  ASP A 841  TYR A 867                    
SITE     3 AC1 14 ILE A 879  GLU A 880  VAL A 882  MET A 953                    
SITE     4 AC1 14 ILE A 963  ASP A 964                                          
SITE     1 AC2  4 GLU A 546  TRP A 576  ARG A 579  LYS A 606                    
CRYST1  144.762   68.336  106.472  90.00  95.11  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      0.006908  0.000000  0.000618        0.00000                         
SCALE2      0.000000  0.014634  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009430        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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