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Database: PDB
Entry: 5UK8
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HEADER    TRANSFERASE/SIGNALING PROTEIN/INHIBITOR 20-JAN-17   5UK8              
TITLE     THE CO-STRUCTURE OF (R)-4-(6-(1-(CYCLOPROPYLSULFONYL)CYCLOPROPYL)-2-  
TITLE    2 (1H-INDOL-4-YL)PYRIMIDIN-4-YL)-3-METHYLMORPHOLINE AND A RATIONALLY   
TITLE    3 DESIGNED PI3K-ALPHA MUTANT THAT MIMICS ATR                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT ALPHA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PTDINS-3-KINASE SUBUNIT ALPHA,PHOSPHATIDYLINOSITOL 4,5-     
COMPND   6 BISPHOSPHATE 3-KINASE 110 KDA CATALYTIC SUBUNIT ALPHA,P110ALPHA,     
COMPND   7 PHOSPHOINOSITIDE-3-KINASE CATALYTIC ALPHA POLYPEPTIDE,               
COMPND   8 SERINE/THREONINE PROTEIN KINASE PIK3CA;                              
COMPND   9 EC: 2.7.1.153,2.7.11.1;                                              
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES;                                                       
COMPND  12 OTHER_DETAILS: POINT MUTATION TO THE BINDING POCKET OF P110 PI3K     
COMPND  13 ALPHA DESIGNED TO MIMIC ATR LIGAND BINDING PROPERTIES.;              
COMPND  14 MOL_ID: 2;                                                           
COMPND  15 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT ALPHA;    
COMPND  16 CHAIN: B;                                                            
COMPND  17 SYNONYM: PTDINS-3-KINASE REGULATORY SUBUNIT ALPHA,                   
COMPND  18 PHOSPHATIDYLINOSITOL 3-KINASE 85 KDA REGULATORY SUBUNIT ALPHA,PTDINS-
COMPND  19 3-KINASE REGULATORY SUBUNIT P85-ALPHA;                               
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MUTATION: YES;                                                       
COMPND  22 OTHER_DETAILS: FRAGMENT OF WILD TYPE P85                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PIK3CA;                                                        
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PIK3R1, GRB1;                                                  
SOURCE  13 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10469                                       
KEYWDS    INHIBITOR, LIPID KINASE, MUTATION, ATR, TRANSFERASE-SIGNALING         
KEYWDS   2 PROTEIN-INHIBITOR COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.KNAPP,M.MAMO,R.A.ELLING                                           
REVDAT   1   14-JUN-17 5UK8    0                                                
JRNL        AUTH   Y.LU,M.KNAPP,K.CRAWFORD,R.WARNE,R.ELLING,K.YAN,M.DOYLE,      
JRNL        AUTH 2 G.PARDEE,L.ZHANG,S.MA,M.MAMO,E.ORNELAS,Y.PAN,D.BUSSIERE,     
JRNL        AUTH 3 J.JANSEN,I.ZAROR,A.LAI,P.BARSANTI,J.SIM                      
JRNL        TITL   RATIONALLY DESIGNED PI3K ALPHA MUTANTS TO MIMIC ATR AND      
JRNL        TITL 2 THEIR USE TO UNDERSTAND BINDING SPECIFICITY OF ATR           
JRNL        TITL 3 INHIBITORS.                                                  
JRNL        REF    J. MOL. BIOL.                 V. 429  1684 2017              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   28433539                                                     
JRNL        DOI    10.1016/J.JMB.2017.04.006                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 52530                          
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)  : 0.200                          
REMARK   3   R VALUE            (WORKING SET)  : 0.198                          
REMARK   3   FREE R VALUE                      : 0.240                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.060                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2657                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.56                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.92                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3828                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2270                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3636                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2250                   
REMARK   3   BIN FREE R VALUE                        : 0.2560                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.02                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 192                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10120                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 185                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.43210                                              
REMARK   3    B22 (A**2) : 2.04240                                              
REMARK   3    B33 (A**2) : -6.47450                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.360               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.472               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.262               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.478               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.266               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : NULL   ; NULL   ; NULL                
REMARK   3    BOND ANGLES               : NULL   ; NULL   ; NULL                
REMARK   3    TORSION ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : NULL   ; NULL   ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : NULL   ; NULL   ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : NULL                     
REMARK   3    BOND ANGLES                  (DEGREES) : NULL                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|2 - A|121 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   24.2930  -34.5182   38.7639           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|122 - A|323 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -4.8986  -39.8567    9.2957           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|324 - A|395 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -23.9425  -28.3372   60.0952           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|396 - A|525 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -21.3056  -32.0815   52.2069           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { A|526 - A|695 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -23.9521  -35.6779   30.8728           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { A|696 - A|807 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    9.9280  -18.9978   20.9401           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { A|808 - A|875 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -10.1358  -13.4216   15.7297           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { A|876 - A|1057 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.1872   -7.9493   16.1516           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { B|326 - B|441 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -45.2475  -13.0670   44.5400           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { B|442 - B|514 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    7.2802  -19.2537   50.4927           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: { B|515 - B|591 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    3.9320  -15.1369   52.3352           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0000 T22:    0.0000                                    
REMARK   3     T33:    0.0000 T12:    0.0000                                    
REMARK   3     T13:    0.0000 T23:    0.0000                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0000 L12:    0.0000                                    
REMARK   3     L13:    0.0000 L23:    0.0000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:    0.0000 S13:    0.0000                     
REMARK   3     S21:    0.0000 S22:    0.0000 S23:    0.0000                     
REMARK   3     S31:    0.0000 S32:    0.0000 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000225876.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.29                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52602                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.520                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.14600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.49800                            
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: PHASER                                                
REMARK 200 STARTING MODEL: IN-HOUSE                                             
REMARK 200                                                                      
REMARK 200 REMARK: LONG RECTANGULAR RODS                                        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3 UL OF PROTEIN WAS MIXED WITH 5 UL OF   
REMARK 280  WELL SOLUTION CONTAINING 12% PEG 3350 AND 120 MM POTASSIUM          
REMARK 280  THIOCYANATE, PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  303.15K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       52.01400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.35300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.54850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.35300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       52.01400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.54850            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 54800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     1                                                      
REMARK 465     SER A   231                                                      
REMARK 465     LYS A   232                                                      
REMARK 465     LYS A   233                                                      
REMARK 465     LEU A   234                                                      
REMARK 465     SER A   235                                                      
REMARK 465     SER A   236                                                      
REMARK 465     GLU A   237                                                      
REMARK 465     ALA A   314                                                      
REMARK 465     THR A   315                                                      
REMARK 465     PRO A   316                                                      
REMARK 465     TYR A   317                                                      
REMARK 465     MET A   318                                                      
REMARK 465     ASN A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     THR A   322                                                      
REMARK 465     VAL A   500                                                      
REMARK 465     SER A   501                                                      
REMARK 465     ARG A   502                                                      
REMARK 465     GLU A   503                                                      
REMARK 465     ALA A   504                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     PHE A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     TYR A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     HIS A   510                                                      
REMARK 465     ALA A   511                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     ASN A   515                                                      
REMARK 465     ARG A   516                                                      
REMARK 465     LEU A   517                                                      
REMARK 465     ALA A   518                                                      
REMARK 465     ARG A   519                                                      
REMARK 465     ASP A   520                                                      
REMARK 465     ASN A   521                                                      
REMARK 465     GLU A   522                                                      
REMARK 465     LEU A   523                                                      
REMARK 465     GLY A   864                                                      
REMARK 465     GLY A   865                                                      
REMARK 465     LEU A   866                                                      
REMARK 465     LYS A   867                                                      
REMARK 465     GLY A   868                                                      
REMARK 465     ALA A   869                                                      
REMARK 465     LEU A   870                                                      
REMARK 465     GLN A   871                                                      
REMARK 465     ILE A  1058                                                      
REMARK 465     PHE A  1059                                                      
REMARK 465     HIS A  1060                                                      
REMARK 465     THR A  1061                                                      
REMARK 465     ILE A  1062                                                      
REMARK 465     LYS A  1063                                                      
REMARK 465     GLN A  1064                                                      
REMARK 465     HIS A  1065                                                      
REMARK 465     ALA A  1066                                                      
REMARK 465     LEU A  1067                                                      
REMARK 465     ASN A  1068                                                      
REMARK 465     HIS A  1069                                                      
REMARK 465     HIS A  1070                                                      
REMARK 465     HIS A  1071                                                      
REMARK 465     HIS A  1072                                                      
REMARK 465     HIS A  1073                                                      
REMARK 465     HIS A  1074                                                      
REMARK 465     MET B   301                                                      
REMARK 465     HIS B   302                                                      
REMARK 465     ASN B   303                                                      
REMARK 465     LEU B   304                                                      
REMARK 465     GLN B   305                                                      
REMARK 465     TYR B   306                                                      
REMARK 465     LEU B   307                                                      
REMARK 465     PRO B   308                                                      
REMARK 465     PRO B   309                                                      
REMARK 465     LYS B   310                                                      
REMARK 465     PRO B   311                                                      
REMARK 465     PRO B   312                                                      
REMARK 465     LYS B   313                                                      
REMARK 465     PRO B   314                                                      
REMARK 465     THR B   315                                                      
REMARK 465     THR B   316                                                      
REMARK 465     VAL B   317                                                      
REMARK 465     ALA B   318                                                      
REMARK 465     ASN B   319                                                      
REMARK 465     ASN B   320                                                      
REMARK 465     GLY B   321                                                      
REMARK 465     MET B   322                                                      
REMARK 465     ASN B   323                                                      
REMARK 465     ASN B   324                                                      
REMARK 465     ASN B   325                                                      
REMARK 465     LYS B   363                                                      
REMARK 465     MET B   364                                                      
REMARK 465     HIS B   365                                                      
REMARK 465     GLY B   388                                                      
REMARK 465     LYS B   389                                                      
REMARK 465     TYR B   390                                                      
REMARK 465     GLY B   391                                                      
REMARK 465     ASN B   410                                                      
REMARK 465     GLU B   411                                                      
REMARK 465     SER B   412                                                      
REMARK 465     LEU B   413                                                      
REMARK 465     ALA B   414                                                      
REMARK 465     GLN B   415                                                      
REMARK 465     TYR B   416                                                      
REMARK 465     ASN B   417                                                      
REMARK 465     PRO B   418                                                      
REMARK 465     LYS B   419                                                      
REMARK 465     LEU B   420                                                      
REMARK 465     ASP B   421                                                      
REMARK 465     ASP B   434                                                      
REMARK 465     GLN B   435                                                      
REMARK 465     VAL B   436                                                      
REMARK 465     VAL B   437                                                      
REMARK 465     LYS B   593                                                      
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 109    CG   CD   OE1  OE2                                  
REMARK 470     MET A 130    CG   SD   CE                                        
REMARK 470     ASP A 186    CG   OD1  OD2                                       
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     LYS A 228    CG   CD   CE   NZ                                   
REMARK 470     ARG A 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 238    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 240    CG   CD   CE   NZ                                   
REMARK 470     LEU A 241    CG   CD1  CD2                                       
REMARK 470     CYS A 242    SG                                                  
REMARK 470     GLU A 245    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 246    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A 247    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 264    CG   CD   CE   NZ                                   
REMARK 470     GLU A 291    CG   CD   OE1  OE2                                  
REMARK 470     MET A 299    CG   SD   CE                                        
REMARK 470     SER A 306    OG                                                  
REMARK 470     ARG A 309    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 348    CG1  CG2  CD1                                       
REMARK 470     LYS A 413    CG   CD   CE   NZ                                   
REMARK 470     LYS A 416    CG   CD   CE   NZ                                   
REMARK 470     ARG A 524    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 526    CG   OD1  ND2                                       
REMARK 470     LYS A 573    CG   CD   CE   NZ                                   
REMARK 470     ARG A 577    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 882    CG   CD   CE   NZ                                   
REMARK 470     LYS A 886    CG   CD   CE   NZ                                   
REMARK 470     LYS A 942    CG   CD   CE   NZ                                   
REMARK 470     LYS A 948    CG   CD   CE   NZ                                   
REMARK 470     ARG A 975    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1054    CG   CD   CE   NZ                                   
REMARK 470     TRP A1057    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A1057    CZ3  CH2                                            
REMARK 470     MET B 326    CG   SD   CE                                        
REMARK 470     LEU B 328    CG   CD1  CD2                                       
REMARK 470     GLU B 345    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 386    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 387    CG   OD1  OD2                                       
REMARK 470     ASP B 394    CG   OD1  OD2                                       
REMARK 470     LEU B 396    CG   CD1  CD2                                       
REMARK 470     PHE B 398    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE B 405    CG1  CG2  CD1                                       
REMARK 470     LYS B 423    CG   CD   CE   NZ                                   
REMARK 470     LEU B 424    CG   CD1  CD2                                       
REMARK 470     LYS B 430    CG   CD   CE   NZ                                   
REMARK 470     TYR B 431    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B 433    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 438    CG   CD   CE   NZ                                   
REMARK 470     GLU B 443    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 511    CG   CD   CE   NZ                                   
REMARK 470     GLU B 518    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 519    CG   CD   CE   NZ                                   
REMARK 470     LYS B 587    CG   CD   CE   NZ                                   
REMARK 470     GLN B 591    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 592    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A 167       74.05   -115.36                                   
REMARK 500    LEU A 239       96.04    -64.56                                   
REMARK 500    LEU A 241       84.78   -156.58                                   
REMARK 500    ASP A 258       49.41    -91.52                                   
REMARK 500    PHE A 261       75.32   -111.32                                   
REMARK 500    LEU A 339      -80.91    -78.19                                   
REMARK 500    ASP A 434       16.80     80.33                                   
REMARK 500    GLU A 469       48.48    -93.10                                   
REMARK 500    SER A 481       -5.89     63.09                                   
REMARK 500    LEU A 601        3.00    -69.71                                   
REMARK 500    GLN A 721      -81.67   -116.00                                   
REMARK 500    ASP A 725       50.55    -92.38                                   
REMARK 500    LEU A 793      -73.28   -137.54                                   
REMARK 500    ASN A 873     -162.52   -112.14                                   
REMARK 500    ASP A 933       72.11     46.59                                   
REMARK 500    LEU A 938     -136.11     55.68                                   
REMARK 500    ASP A 939       72.44   -110.24                                   
REMARK 500    LEU B 328       -5.70     72.95                                   
REMARK 500    ARG B 386      -19.46   -146.89                                   
REMARK 500    LEU B 396       96.29    -68.00                                   
REMARK 500    LEU B 424       78.60    -66.10                                   
REMARK 500    LYS B 587       47.01    -89.49                                   
REMARK 500    GLN B 591     -179.01   -173.64                                   
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 8DV A 1101                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UKJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UL1   RELATED DB: PDB                                   
DBREF  5UK8 A    1  1068  UNP    P42336   PK3CA_HUMAN      1   1068             
DBREF  5UK8 B  301   593  UNP    P27986   P85A_HUMAN       1    293             
SEQADV 5UK8 LYS A  232  UNP  P42336    MET   232 ENGINEERED MUTATION            
SEQADV 5UK8 LYS A  233  UNP  P42336    LEU   233 ENGINEERED MUTATION            
SEQADV 5UK8 GLU A  770  UNP  P42336    ARG   770 ENGINEERED MUTATION            
SEQADV 5UK8 LYS A  780  UNP  P42336    TRP   780 ENGINEERED MUTATION            
SEQADV 5UK8 ILE A  798  UNP  P42336    GLU   798 ENGINEERED MUTATION            
SEQADV 5UK8 MET A  800  UNP  P42336    ILE   800 ENGINEERED MUTATION            
SEQADV 5UK8 TRP A  850  UNP  P42336    VAL   850 ENGINEERED MUTATION            
SEQADV 5UK8 VAL A  930  UNP  P42336    PHE   930 ENGINEERED MUTATION            
SEQADV 5UK8 HIS A 1069  UNP  P42336              EXPRESSION TAG                 
SEQADV 5UK8 HIS A 1070  UNP  P42336              EXPRESSION TAG                 
SEQADV 5UK8 HIS A 1071  UNP  P42336              EXPRESSION TAG                 
SEQADV 5UK8 HIS A 1072  UNP  P42336              EXPRESSION TAG                 
SEQADV 5UK8 HIS A 1073  UNP  P42336              EXPRESSION TAG                 
SEQADV 5UK8 HIS A 1074  UNP  P42336              EXPRESSION TAG                 
SEQADV 5UK8 TYR B  306  UNP  P27986    THR     6 ENGINEERED MUTATION            
SEQRES   1 A 1074  MET PRO PRO ARG PRO SER SER GLY GLU LEU TRP GLY ILE          
SEQRES   2 A 1074  HIS LEU MET PRO PRO ARG ILE LEU VAL GLU CYS LEU LEU          
SEQRES   3 A 1074  PRO ASN GLY MET ILE VAL THR LEU GLU CYS LEU ARG GLU          
SEQRES   4 A 1074  ALA THR LEU ILE THR ILE LYS HIS GLU LEU PHE LYS GLU          
SEQRES   5 A 1074  ALA ARG LYS TYR PRO LEU HIS GLN LEU LEU GLN ASP GLU          
SEQRES   6 A 1074  SER SER TYR ILE PHE VAL SER VAL THR GLN GLU ALA GLU          
SEQRES   7 A 1074  ARG GLU GLU PHE PHE ASP GLU THR ARG ARG LEU CYS ASP          
SEQRES   8 A 1074  LEU ARG LEU PHE GLN PRO PHE LEU LYS VAL ILE GLU PRO          
SEQRES   9 A 1074  VAL GLY ASN ARG GLU GLU LYS ILE LEU ASN ARG GLU ILE          
SEQRES  10 A 1074  GLY PHE ALA ILE GLY MET PRO VAL CYS GLU PHE ASP MET          
SEQRES  11 A 1074  VAL LYS ASP PRO GLU VAL GLN ASP PHE ARG ARG ASN ILE          
SEQRES  12 A 1074  LEU ASN VAL CYS LYS GLU ALA VAL ASP LEU ARG ASP LEU          
SEQRES  13 A 1074  ASN SER PRO HIS SER ARG ALA MET TYR VAL TYR PRO PRO          
SEQRES  14 A 1074  ASN VAL GLU SER SER PRO GLU LEU PRO LYS HIS ILE TYR          
SEQRES  15 A 1074  ASN LYS LEU ASP LYS GLY GLN ILE ILE VAL VAL ILE TRP          
SEQRES  16 A 1074  VAL ILE VAL SER PRO ASN ASN ASP LYS GLN LYS TYR THR          
SEQRES  17 A 1074  LEU LYS ILE ASN HIS ASP CYS VAL PRO GLU GLN VAL ILE          
SEQRES  18 A 1074  ALA GLU ALA ILE ARG LYS LYS THR ARG SER LYS LYS LEU          
SEQRES  19 A 1074  SER SER GLU GLN LEU LYS LEU CYS VAL LEU GLU TYR GLN          
SEQRES  20 A 1074  GLY LYS TYR ILE LEU LYS VAL CYS GLY CYS ASP GLU TYR          
SEQRES  21 A 1074  PHE LEU GLU LYS TYR PRO LEU SER GLN TYR LYS TYR ILE          
SEQRES  22 A 1074  ARG SER CYS ILE MET LEU GLY ARG MET PRO ASN LEU MET          
SEQRES  23 A 1074  LEU MET ALA LYS GLU SER LEU TYR SER GLN LEU PRO MET          
SEQRES  24 A 1074  ASP CYS PHE THR MET PRO SER TYR SER ARG ARG ILE SER          
SEQRES  25 A 1074  THR ALA THR PRO TYR MET ASN GLY GLU THR SER THR LYS          
SEQRES  26 A 1074  SER LEU TRP VAL ILE ASN SER ALA LEU ARG ILE LYS ILE          
SEQRES  27 A 1074  LEU CYS ALA THR TYR VAL ASN VAL ASN ILE ARG ASP ILE          
SEQRES  28 A 1074  ASP LYS ILE TYR VAL ARG THR GLY ILE TYR HIS GLY GLY          
SEQRES  29 A 1074  GLU PRO LEU CYS ASP ASN VAL ASN THR GLN ARG VAL PRO          
SEQRES  30 A 1074  CYS SER ASN PRO ARG TRP ASN GLU TRP LEU ASN TYR ASP          
SEQRES  31 A 1074  ILE TYR ILE PRO ASP LEU PRO ARG ALA ALA ARG LEU CYS          
SEQRES  32 A 1074  LEU SER ILE CYS SER VAL LYS GLY ARG LYS GLY ALA LYS          
SEQRES  33 A 1074  GLU GLU HIS CYS PRO LEU ALA TRP GLY ASN ILE ASN LEU          
SEQRES  34 A 1074  PHE ASP TYR THR ASP THR LEU VAL SER GLY LYS MET ALA          
SEQRES  35 A 1074  LEU ASN LEU TRP PRO VAL PRO HIS GLY LEU GLU ASP LEU          
SEQRES  36 A 1074  LEU ASN PRO ILE GLY VAL THR GLY SER ASN PRO ASN LYS          
SEQRES  37 A 1074  GLU THR PRO CYS LEU GLU LEU GLU PHE ASP TRP PHE SER          
SEQRES  38 A 1074  SER VAL VAL LYS PHE PRO ASP MET SER VAL ILE GLU GLU          
SEQRES  39 A 1074  HIS ALA ASN TRP SER VAL SER ARG GLU ALA GLY PHE SER          
SEQRES  40 A 1074  TYR SER HIS ALA GLY LEU SER ASN ARG LEU ALA ARG ASP          
SEQRES  41 A 1074  ASN GLU LEU ARG GLU ASN ASP LYS GLU GLN LEU LYS ALA          
SEQRES  42 A 1074  ILE SER THR ARG ASP PRO LEU SER GLU ILE THR GLU GLN          
SEQRES  43 A 1074  GLU LYS ASP PHE LEU TRP SER HIS ARG HIS TYR CYS VAL          
SEQRES  44 A 1074  THR ILE PRO GLU ILE LEU PRO LYS LEU LEU LEU SER VAL          
SEQRES  45 A 1074  LYS TRP ASN SER ARG ASP GLU VAL ALA GLN MET TYR CYS          
SEQRES  46 A 1074  LEU VAL LYS ASP TRP PRO PRO ILE LYS PRO GLU GLN ALA          
SEQRES  47 A 1074  MET GLU LEU LEU ASP CYS ASN TYR PRO ASP PRO MET VAL          
SEQRES  48 A 1074  ARG GLY PHE ALA VAL ARG CYS LEU GLU LYS TYR LEU THR          
SEQRES  49 A 1074  ASP ASP LYS LEU SER GLN TYR LEU ILE GLN LEU VAL GLN          
SEQRES  50 A 1074  VAL LEU LYS TYR GLU GLN TYR LEU ASP ASN LEU LEU VAL          
SEQRES  51 A 1074  ARG PHE LEU LEU LYS LYS ALA LEU THR ASN GLN ARG ILE          
SEQRES  52 A 1074  GLY HIS PHE PHE PHE TRP HIS LEU LYS SER GLU MET HIS          
SEQRES  53 A 1074  ASN LYS THR VAL SER GLN ARG PHE GLY LEU LEU LEU GLU          
SEQRES  54 A 1074  SER TYR CYS ARG ALA CYS GLY MET TYR LEU LYS HIS LEU          
SEQRES  55 A 1074  ASN ARG GLN VAL GLU ALA MET GLU LYS LEU ILE ASN LEU          
SEQRES  56 A 1074  THR ASP ILE LEU LYS GLN GLU LYS LYS ASP GLU THR GLN          
SEQRES  57 A 1074  LYS VAL GLN MET LYS PHE LEU VAL GLU GLN MET ARG ARG          
SEQRES  58 A 1074  PRO ASP PHE MET ASP ALA LEU GLN GLY PHE LEU SER PRO          
SEQRES  59 A 1074  LEU ASN PRO ALA HIS GLN LEU GLY ASN LEU ARG LEU GLU          
SEQRES  60 A 1074  GLU CYS GLU ILE MET SER SER ALA LYS ARG PRO LEU LYS          
SEQRES  61 A 1074  LEU ASN TRP GLU ASN PRO ASP ILE MET SER GLU LEU LEU          
SEQRES  62 A 1074  PHE GLN ASN ASN ILE ILE MET PHE LYS ASN GLY ASP ASP          
SEQRES  63 A 1074  LEU ARG GLN ASP MET LEU THR LEU GLN ILE ILE ARG ILE          
SEQRES  64 A 1074  MET GLU ASN ILE TRP GLN ASN GLN GLY LEU ASP LEU ARG          
SEQRES  65 A 1074  MET LEU PRO TYR GLY CYS LEU SER ILE GLY ASP CYS VAL          
SEQRES  66 A 1074  GLY LEU ILE GLU TRP VAL ARG ASN SER HIS THR ILE MET          
SEQRES  67 A 1074  GLN ILE GLN CYS LYS GLY GLY LEU LYS GLY ALA LEU GLN          
SEQRES  68 A 1074  PHE ASN SER HIS THR LEU HIS GLN TRP LEU LYS ASP LYS          
SEQRES  69 A 1074  ASN LYS GLY GLU ILE TYR ASP ALA ALA ILE ASP LEU PHE          
SEQRES  70 A 1074  THR ARG SER CYS ALA GLY TYR CYS VAL ALA THR PHE ILE          
SEQRES  71 A 1074  LEU GLY ILE GLY ASP ARG HIS ASN SER ASN ILE MET VAL          
SEQRES  72 A 1074  LYS ASP ASP GLY GLN LEU VAL HIS ILE ASP PHE GLY HIS          
SEQRES  73 A 1074  PHE LEU ASP HIS LYS LYS LYS LYS PHE GLY TYR LYS ARG          
SEQRES  74 A 1074  GLU ARG VAL PRO PHE VAL LEU THR GLN ASP PHE LEU ILE          
SEQRES  75 A 1074  VAL ILE SER LYS GLY ALA GLN GLU CYS THR LYS THR ARG          
SEQRES  76 A 1074  GLU PHE GLU ARG PHE GLN GLU MET CYS TYR LYS ALA TYR          
SEQRES  77 A 1074  LEU ALA ILE ARG GLN HIS ALA ASN LEU PHE ILE ASN LEU          
SEQRES  78 A 1074  PHE SER MET MET LEU GLY SER GLY MET PRO GLU LEU GLN          
SEQRES  79 A 1074  SER PHE ASP ASP ILE ALA TYR ILE ARG LYS THR LEU ALA          
SEQRES  80 A 1074  LEU ASP LYS THR GLU GLN GLU ALA LEU GLU TYR PHE MET          
SEQRES  81 A 1074  LYS GLN MET ASN ASP ALA HIS HIS GLY GLY TRP THR THR          
SEQRES  82 A 1074  LYS MET ASP TRP ILE PHE HIS THR ILE LYS GLN HIS ALA          
SEQRES  83 A 1074  LEU ASN HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  293  MET HIS ASN LEU GLN TYR LEU PRO PRO LYS PRO PRO LYS          
SEQRES   2 B  293  PRO THR THR VAL ALA ASN ASN GLY MET ASN ASN ASN MET          
SEQRES   3 B  293  SER LEU GLN ASP ALA GLU TRP TYR TRP GLY ASP ILE SER          
SEQRES   4 B  293  ARG GLU GLU VAL ASN GLU LYS LEU ARG ASP THR ALA ASP          
SEQRES   5 B  293  GLY THR PHE LEU VAL ARG ASP ALA SER THR LYS MET HIS          
SEQRES   6 B  293  GLY ASP TYR THR LEU THR LEU ARG LYS GLY GLY ASN ASN          
SEQRES   7 B  293  LYS LEU ILE LYS ILE PHE HIS ARG ASP GLY LYS TYR GLY          
SEQRES   8 B  293  PHE SER ASP PRO LEU THR PHE SER SER VAL VAL GLU LEU          
SEQRES   9 B  293  ILE ASN HIS TYR ARG ASN GLU SER LEU ALA GLN TYR ASN          
SEQRES  10 B  293  PRO LYS LEU ASP VAL LYS LEU LEU TYR PRO VAL SER LYS          
SEQRES  11 B  293  TYR GLN GLN ASP GLN VAL VAL LYS GLU ASP ASN ILE GLU          
SEQRES  12 B  293  ALA VAL GLY LYS LYS LEU HIS GLU TYR ASN THR GLN PHE          
SEQRES  13 B  293  GLN GLU LYS SER ARG GLU TYR ASP ARG LEU TYR GLU GLU          
SEQRES  14 B  293  TYR THR ARG THR SER GLN GLU ILE GLN MET LYS ARG THR          
SEQRES  15 B  293  ALA ILE GLU ALA PHE ASN GLU THR ILE LYS ILE PHE GLU          
SEQRES  16 B  293  GLU GLN CYS GLN THR GLN GLU ARG TYR SER LYS GLU TYR          
SEQRES  17 B  293  ILE GLU LYS PHE LYS ARG GLU GLY ASN GLU LYS GLU ILE          
SEQRES  18 B  293  GLN ARG ILE MET HIS ASN TYR ASP LYS LEU LYS SER ARG          
SEQRES  19 B  293  ILE SER GLU ILE ILE ASP SER ARG ARG ARG LEU GLU GLU          
SEQRES  20 B  293  ASP LEU LYS LYS GLN ALA ALA GLU TYR ARG GLU ILE ASP          
SEQRES  21 B  293  LYS ARG MET ASN SER ILE LYS PRO ASP LEU ILE GLN LEU          
SEQRES  22 B  293  ARG LYS THR ARG ASP GLN TYR LEU MET TRP LEU THR GLN          
SEQRES  23 B  293  LYS GLY VAL ARG GLN LYS LYS                                  
HET    8DV  A1101      31                                                       
HETNAM     8DV (R)-4-(6-(1-(CYCLOPROPYLSULFONYL)CYCLOPROPYL)-2-(1H-             
HETNAM   2 8DV  INDOL-4-YL)PYRIMIDIN-4-YL)-3-METHYLMORPHOLINE                   
HETSYN     8DV 4-{4-[1-(CYCLOPROPYLSULFONYL)CYCLOPROPYL]-6-[(3R)-3-             
HETSYN   2 8DV  METHYLMORPHOLIN-4-YL]PYRIMIDIN-2-YL}-1H-INDOLE                  
FORMUL   3  8DV    C23 H26 N4 O3 S                                              
FORMUL   4  HOH   *185(H2 O)                                                    
HELIX    1 AA1 THR A   41  ALA A   53  1                                  13    
HELIX    2 AA2 ARG A   54  TYR A   56  5                                   3    
HELIX    3 AA3 LEU A   58  LEU A   62  5                                   5    
HELIX    4 AA4 ASP A   64  TYR A   68  5                                   5    
HELIX    5 AA5 ARG A   88  ARG A   93  5                                   6    
HELIX    6 AA6 ASN A  107  GLY A  122  1                                  16    
HELIX    7 AA7 VAL A  125  VAL A  131  1                                   7    
HELIX    8 AA8 ASP A  133  ILE A  143  1                                  11    
HELIX    9 AA9 ILE A  143  ASP A  155  1                                  13    
HELIX   10 AB1 PRO A  159  TYR A  167  1                                   9    
HELIX   11 AB2 PRO A  178  ASN A  183  1                                   6    
HELIX   12 AB3 VAL A  216  LYS A  227  1                                  12    
HELIX   13 AB4 PRO A  266  GLN A  269  5                                   4    
HELIX   14 AB5 TYR A  270  GLY A  280  1                                  11    
HELIX   15 AB6 ALA A  289  SER A  295  1                                   7    
HELIX   16 AB7 PRO A  305  ARG A  309  5                                   5    
HELIX   17 AB8 TRP A  328  ILE A  330  5                                   3    
HELIX   18 AB9 PRO A  394  LEU A  396  5                                   3    
HELIX   19 AC1 ASP A  488  ASN A  497  1                                  10    
HELIX   20 AC2 GLU A  525  ARG A  537  1                                  13    
HELIX   21 AC3 THR A  544  HIS A  554  1                                  11    
HELIX   22 AC4 HIS A  556  GLU A  563  5                                   8    
HELIX   23 AC5 ILE A  564  LEU A  570  1                                   7    
HELIX   24 AC6 SER A  576  TRP A  590  1                                  15    
HELIX   25 AC7 LYS A  594  MET A  599  1                                   6    
HELIX   26 AC8 GLU A  600  ASP A  603  5                                   4    
HELIX   27 AC9 ASP A  608  LEU A  623  1                                  16    
HELIX   28 AD1 THR A  624  TYR A  631  1                                   8    
HELIX   29 AD2 TYR A  631  VAL A  638  1                                   8    
HELIX   30 AD3 LEU A  639  GLU A  642  5                                   4    
HELIX   31 AD4 ASN A  647  LEU A  658  1                                  12    
HELIX   32 AD5 ASN A  660  GLU A  674  1                                  15    
HELIX   33 AD6 VAL A  680  CYS A  695  1                                  16    
HELIX   34 AD7 MET A  697  GLN A  721  1                                  25    
HELIX   35 AD8 THR A  727  ARG A  740  1                                  14    
HELIX   36 AD9 ARG A  741  LEU A  748  1                                   8    
HELIX   37 AE1 ARG A  765  CYS A  769  5                                   5    
HELIX   38 AE2 MET A  789  LEU A  793  5                                   5    
HELIX   39 AE3 LEU A  807  GLN A  827  1                                  21    
HELIX   40 AE4 ILE A  857  LYS A  863  1                                   7    
HELIX   41 AE5 HIS A  875  ASN A  885  1                                  11    
HELIX   42 AE6 LYS A  886  GLU A  888  5                                   3    
HELIX   43 AE7 ILE A  889  GLY A  912  1                                  24    
HELIX   44 AE8 ASP A  939  GLY A  946  1                                   8    
HELIX   45 AE9 THR A  957  SER A  965  1                                   9    
HELIX   46 AF1 GLU A  970  LYS A  973  5                                   4    
HELIX   47 AF2 THR A  974  GLN A  993  1                                  20    
HELIX   48 AF3 HIS A  994  MET A 1004  1                                  11    
HELIX   49 AF4 SER A 1015  LEU A 1026  1                                  12    
HELIX   50 AF5 THR A 1031  HIS A 1048  1                                  18    
HELIX   51 AF6 SER B  339  LEU B  347  1                                   9    
HELIX   52 AF7 SER B  400  ARG B  409  1                                  10    
HELIX   53 AF8 ILE B  442  ARG B  514  1                                  73    
HELIX   54 AF9 ASN B  517  LYS B  587  1                                  71    
SHEET    1 AA1 5 ILE A  31  LEU A  37  0                                        
SHEET    2 AA1 5 ARG A  19  LEU A  25 -1  N  ILE A  20   O  CYS A  36           
SHEET    3 AA1 5 PHE A  98  ILE A 102  1  O  LEU A  99   N  GLU A  23           
SHEET    4 AA1 5 ILE A  69  VAL A  73 -1  N  VAL A  71   O  LYS A 100           
SHEET    5 AA1 5 ARG A  79  PHE A  82 -1  O  PHE A  82   N  PHE A  70           
SHEET    1 AA2 5 ASP A 203  ASN A 212  0                                        
SHEET    2 AA2 5 GLN A 189  VAL A 198 -1  N  VAL A 192   O  LEU A 209           
SHEET    3 AA2 5 ASN A 284  MET A 288  1  O  LEU A 287   N  TRP A 195           
SHEET    4 AA2 5 ILE A 251  VAL A 254 -1  N  LYS A 253   O  MET A 286           
SHEET    5 AA2 5 TYR A 260  PHE A 261 -1  O  PHE A 261   N  LEU A 252           
SHEET    1 AA3 2 THR A 324  SER A 326  0                                        
SHEET    2 AA3 2 VAL A 483  LYS A 485  1  O  LYS A 485   N  LYS A 325           
SHEET    1 AA4 4 ARG A 382  TYR A 392  0                                        
SHEET    2 AA4 4 ALA A 333  ALA A 341 -1  N  ILE A 336   O  LEU A 387           
SHEET    3 AA4 4 CYS A 472  GLU A 476 -1  O  GLU A 474   N  CYS A 340           
SHEET    4 AA4 4 LYS A 440  ASN A 444 -1  N  LEU A 443   O  LEU A 473           
SHEET    1 AA5 3 GLU A 365  PRO A 366  0                                        
SHEET    2 AA5 3 LYS A 353  HIS A 362 -1  N  HIS A 362   O  GLU A 365           
SHEET    3 AA5 3 VAL A 371  ASN A 372 -1  O  VAL A 371   N  THR A 358           
SHEET    1 AA6 4 GLU A 365  PRO A 366  0                                        
SHEET    2 AA6 4 LYS A 353  HIS A 362 -1  N  HIS A 362   O  GLU A 365           
SHEET    3 AA6 4 ARG A 401  LYS A 413 -1  O  CYS A 407   N  TYR A 355           
SHEET    4 AA6 4 LYS A 416  ASN A 428 -1  O  LEU A 422   N  ILE A 406           
SHEET    1 AA7 2 PHE A 751  SER A 753  0                                        
SHEET    2 AA7 2 ASN A 756  LEU A 761 -1  O  LEU A 761   N  PHE A 751           
SHEET    1 AA8 5 GLU A 770  ILE A 771  0                                        
SHEET    2 AA8 5 LEU A 779  GLU A 784 -1  O  LYS A 780   N  GLU A 770           
SHEET    3 AA8 5 ASN A 796  ASN A 803 -1  O  ASN A 797   N  TRP A 783           
SHEET    4 AA8 5 VAL A 845  GLU A 849 -1  O  ILE A 848   N  MET A 800           
SHEET    5 AA8 5 CYS A 838  GLY A 842 -1  N  LEU A 839   O  LEU A 847           
SHEET    1 AA9 3 SER A 854  THR A 856  0                                        
SHEET    2 AA9 3 ILE A 921  LYS A 924 -1  O  VAL A 923   N  HIS A 855           
SHEET    3 AA9 3 LEU A 929  HIS A 931 -1  O  VAL A 930   N  MET A 922           
SHEET    1 AB1 4 TYR B 334  GLY B 336  0                                        
SHEET    2 AB1 4 THR B 354  ASP B 359  1  O  VAL B 357   N  TRP B 335           
SHEET    3 AB1 4 TYR B 368  LYS B 374 -1  O  ARG B 373   N  THR B 354           
SHEET    4 AB1 4 ASN B 377  ILE B 383 -1  O  ILE B 381   N  LEU B 370           
SHEET    1 AB2 3 TYR B 334  GLY B 336  0                                        
SHEET    2 AB2 3 THR B 354  ASP B 359  1  O  VAL B 357   N  TRP B 335           
SHEET    3 AB2 3 TYR B 426  PRO B 427  1  O  TYR B 426   N  PHE B 355           
CISPEP   1 SER A  158    PRO A  159          0         1.92                     
CISPEP   2 SER A  199    PRO A  200          0         0.95                     
SITE     1 AC1 15 ILE A 311  SER A 774  PRO A 778  LYS A 802                    
SITE     2 AC1 15 ASP A 810  TYR A 836  ILE A 848  GLU A 849                    
SITE     3 AC1 15 TRP A 850  VAL A 851  SER A 854  THR A 856                    
SITE     4 AC1 15 MET A 922  ILE A 932  ASP A 933                               
CRYST1  104.028  107.097  134.706  90.00  90.00  90.00 P 21 21 21    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      0.009613  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009337  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007424        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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