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Database: PDB
Entry: 4OVV
LinkDB: 4OVV
Original site: 4OVV 
HEADER    TRANSFERASE/TRANSFERASE REGULATOR       14-JAN-14   4OVV              
TITLE     CRYSTAL STRUCTURE OF PI3KALPHA IN COMPLEX WITH DIC4-PIP2              
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;                                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT ALPHA;    
COMPND  13 CHAIN: B;                                                            
COMPND  14 FRAGMENT: UNP RESIDUES 322-600;                                      
COMPND  15 SYNONYM: PTDINS-3-KINASE REGULATORY SUBUNIT ALPHA,                   
COMPND  16 PHOSPHATIDYLINOSITOL 3-KINASE 85 KDA REGULATORY SUBUNIT ALPHA,       
COMPND  17 PTDINS-3-KINASE REGULATORY SUBUNIT P85-ALPHA;                        
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 GENE: PIK3CA;                                                        
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HT-A;                            
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: GRB1,PI3KR1,PIK3R1;                                            
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HT-A                             
KEYWDS    P110, P85, PI3KCA, PI3K, PIK3R1, PHOSPHATIDILYNOSITOL 3, 4, 5         
KEYWDS   2 TRIPHOSPHATE, PIP2, PHOSPHATIDYLINOSITOL 4, 5 BISPHOSPHATE, LIPID    
KEYWDS   3 KINASE, PHOSPHOINOSITIDE, 3-KINASE, SIGNALING, PHOSPHATIDYLINOSITOL  
KEYWDS   4 3-KINASE, TRANSFERASE-TRANSFERASE REGULATOR COMPLEX                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.B.GABELLI,B.VOGELSTEIN,M.MILLER,L.M.AMZEL                           
REVDAT   4   27-SEP-17 4OVV    1       REMARK                                   
REVDAT   3   31-AUG-16 4OVV    1       REMARK                                   
REVDAT   2   10-SEP-14 4OVV    1       TITLE                                    
REVDAT   1   03-SEP-14 4OVV    0                                                
JRNL        AUTH   M.S.MILLER,O.SCHMIDT-KITTLER,D.M.BOLDUC,E.T.BROWER,          
JRNL        AUTH 2 D.CHAVES-MOREIRA,M.ALLAIRE,K.W.KINZLER,I.G.JENNINGS,         
JRNL        AUTH 3 P.E.THOMPSON,P.A.COLE,L.M.AMZEL,B.VOGELSTEIN,S.B.GABELLI     
JRNL        TITL   STRUCTURAL BASIS OF NSH2 REGULATION AND LIPID BINDING IN     
JRNL        TITL 2 PI3K ALPHA.                                                  
JRNL        REF    ONCOTARGET                    V.   5  5198 2014              
JRNL        REFN                   ESSN 1949-2553                               
JRNL        PMID   25105564                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 91.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25582                          
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) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.339                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1316                            
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) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1585                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 105                          
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10584                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 83                                      
REMARK   3   SOLVENT ATOMS            : 4                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 94.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.60000                                              
REMARK   3    B22 (A**2) : -1.86000                                             
REMARK   3    B33 (A**2) : -1.73000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.801         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.643         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 90.419        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.821                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10893 ; 0.015 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14704 ; 1.865 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1270 ; 8.020 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   545 ;39.596 ;24.294       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2026 ;23.914 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    73 ;21.072 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1592 ; 0.121 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8140 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   -28        A  1053                          
REMARK   3    RESIDUE RANGE :   A  1101        A  1101                          
REMARK   3    RESIDUE RANGE :   B  2001        B  2001                          
REMARK   3    RESIDUE RANGE :   A  1201        A  1204                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.4330  62.3510  91.9500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1129 T22:   0.0472                                     
REMARK   3      T33:   0.1132 T12:   0.0379                                     
REMARK   3      T13:   0.0907 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0062 L22:   0.8486                                     
REMARK   3      L33:   1.4592 L12:  -0.0079                                     
REMARK   3      L13:  -0.0521 L23:   0.1955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0642 S12:   0.1694 S13:   0.0107                       
REMARK   3      S21:   0.1111 S22:  -0.0659 S23:   0.2450                       
REMARK   3      S31:   0.0931 S32:  -0.0356 S33:   0.0017                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   327        B   598                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.9180  37.6810  88.4110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2982 T22:   0.2465                                     
REMARK   3      T33:   0.3019 T12:   0.0109                                     
REMARK   3      T13:   0.0340 T23:  -0.0964                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5338 L22:   1.8517                                     
REMARK   3      L33:   0.7955 L12:   0.7304                                     
REMARK   3      L13:   0.3825 L23:   0.2263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1052 S12:   0.2317 S13:  -0.1539                       
REMARK   3      S21:  -0.0507 S22:   0.1480 S23:   0.1011                       
REMARK   3      S31:   0.3180 S32:   0.0088 S33:  -0.2532                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 4OVV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200039.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9788                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28636                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.360                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.000                              
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.36                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NAFORMATE, PH 6.8, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
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       57.12950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.37150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.04150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.37150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.12950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.04150            
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: 7670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 58870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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     GLU A   -10                                                      
REMARK 465     ASN A    -9                                                      
REMARK 465     LEU A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     PHE A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ARG A   309                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     ILE A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     THR A   313                                                      
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     LYS A   410                                                      
REMARK 465     GLY A   411                                                      
REMARK 465     ARG A   412                                                      
REMARK 465     LYS A   413                                                      
REMARK 465     GLY A   414                                                      
REMARK 465     ALA A   415                                                      
REMARK 465     LYS A   416                                                      
REMARK 465     GLU A   417                                                      
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     LYS A  1054                                                      
REMARK 465     MET A  1055                                                      
REMARK 465     ASP A  1056                                                      
REMARK 465     TRP A  1057                                                      
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     MET B   322                                                      
REMARK 465     ASN B   323                                                      
REMARK 465     ASN B   324                                                      
REMARK 465     ASN B   325                                                      
REMARK 465     MET B   326                                                      
REMARK 465     ASP B   359                                                      
REMARK 465     ALA B   360                                                      
REMARK 465     SER B   361                                                      
REMARK 465     LYS B   374                                                      
REMARK 465     GLY B   375                                                      
REMARK 465     GLY B   376                                                      
REMARK 465     ILE B   383                                                      
REMARK 465     PHE B   384                                                      
REMARK 465     HIS B   385                                                      
REMARK 465     ARG B   386                                                      
REMARK 465     ASP B   387                                                      
REMARK 465     GLY B   388                                                      
REMARK 465     LYS B   389                                                      
REMARK 465     TYR B   390                                                      
REMARK 465     GLU B   411                                                      
REMARK 465     LYS B   419                                                      
REMARK 465     LEU B   420                                                      
REMARK 465     ASP B   421                                                      
REMARK 465     VAL B   422                                                      
REMARK 465     LYS B   423                                                      
REMARK 465     LEU B   424                                                      
REMARK 465     LEU B   425                                                      
REMARK 465     PHE B   512                                                      
REMARK 465     LYS B   513                                                      
REMARK 465     ARG B   514                                                      
REMARK 465     GLU B   515                                                      
REMARK 465     GLY B   516                                                      
REMARK 465     VAL B   589                                                      
REMARK 465     ARG B   590                                                      
REMARK 465     GLN B   591                                                      
REMARK 465     LYS B   592                                                      
REMARK 465     GLY B   599                                                      
REMARK 465     ASN B   600                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER A   965     N    GLY A   967              2.10            
REMARK 500   O    ASP B   330     N    GLU B   332              2.10            
REMARK 500   O    GLN A   825     N    GLN A   827              2.18            
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    HIS A -24   CG    HIS A -24   CD2     0.067                       
REMARK 500    HIS A  59   CG    HIS A  59   CD2     0.070                       
REMARK 500    HIS A 419   CG    HIS A 419   CD2     0.054                       
REMARK 500    HIS A 450   CG    HIS A 450   CD2     0.073                       
REMARK 500    HIS A 917   CG    HIS A 917   CD2     0.065                       
REMARK 500    HIS A 936   CG    HIS A 936   CD2     0.073                       
REMARK 500    HIS A1048   CG    HIS A1048   CD2     0.065                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 200   C   -  N   -  CA  ANGL. DEV. =  19.3 DEGREES          
REMARK 500    PRO A 200   C   -  N   -  CD  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    CYS A 215   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES          
REMARK 500    PRO A 487   C   -  N   -  CA  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    LEU A 513   CA  -  CB  -  CG  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    PRO A 591   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO A 595   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A -27      -25.26     52.42                                   
REMARK 500    TYR A -17      108.21    -51.06                                   
REMARK 500    PRO A -14      -82.23    -43.17                                   
REMARK 500    SER A   6        8.72     45.23                                   
REMARK 500    GLU A   9      -32.93    -33.60                                   
REMARK 500    ILE A  13      -60.36    -26.10                                   
REMARK 500    HIS A  14      -80.11    111.23                                   
REMARK 500    ARG A  38      -40.03    -23.74                                   
REMARK 500    LEU A  42       -9.82    -54.43                                   
REMARK 500    ARG A  54      -21.59    -38.42                                   
REMARK 500    LEU A  58       66.98     68.63                                   
REMARK 500    ASP A  64      130.71    -39.28                                   
REMARK 500    SER A  66      -39.86    -20.02                                   
REMARK 500    SER A  67       32.31    -92.63                                   
REMARK 500    GLN A  75      -72.46    -50.48                                   
REMARK 500    PHE A  82       79.44   -109.09                                   
REMARK 500    ASP A  84      106.53    -57.79                                   
REMARK 500    ARG A  93       73.69     66.52                                   
REMARK 500    PHE A  95      -87.22     73.12                                   
REMARK 500    ASN A 107      -45.05      5.76                                   
REMARK 500    ARG A 108       54.92    -69.72                                   
REMARK 500    GLU A 109      -15.45    -46.40                                   
REMARK 500    ASN A 114      -10.18    161.47                                   
REMARK 500    GLU A 116      -73.66    -48.55                                   
REMARK 500    ILE A 117      -37.82    -34.86                                   
REMARK 500    ASP A 133      130.35    -33.12                                   
REMARK 500    ASP A 155       12.55    -65.00                                   
REMARK 500    TYR A 167       59.69   -117.91                                   
REMARK 500    LYS A 184       32.84    -96.52                                   
REMARK 500    ASP A 186       52.84     37.91                                   
REMARK 500    VAL A 198      -74.33   -108.06                                   
REMARK 500    ASN A 212      133.31    -33.79                                   
REMARK 500    ALA A 222      -86.70    -48.46                                   
REMARK 500    GLU A 223      -19.96    -48.49                                   
REMARK 500    THR A 229      -64.64    -90.24                                   
REMARK 500    ARG A 230      101.90    -16.61                                   
REMARK 500    SER A 235      152.43    -36.11                                   
REMARK 500    GLU A 245      -78.51    -61.38                                   
REMARK 500    GLN A 247      -68.59    -20.26                                   
REMARK 500    PHE A 261       74.01   -109.36                                   
REMARK 500    CYS A 276      -37.47    -34.25                                   
REMARK 500    TYR A 294       -1.47    -52.23                                   
REMARK 500    TYR A 307       36.62    -68.61                                   
REMARK 500    SER A 323       -3.17     64.72                                   
REMARK 500    THR A 324     -106.45     54.87                                   
REMARK 500    LYS A 325      120.39   -177.42                                   
REMARK 500    ASN A 331       48.58    -91.97                                   
REMARK 500    ALA A 333     -174.49    -66.06                                   
REMARK 500    LEU A 339     -118.48    -80.05                                   
REMARK 500    THR A 342      -65.19    -91.97                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     170 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  113     ASN A  114                 -148.94                    
REMARK 500 ASN A  201     ASN A  202                  148.35                    
REMARK 500 ARG A  375     VAL A  376                 -147.57                    
REMARK 500 PRO A  377     CYS A  378                  148.06                    
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 PBU A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PBU B 2001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OVU   RELATED DB: PDB                                   
DBREF  4OVV A    1  1068  UNP    P42336   PK3CA_HUMAN      1   1068             
DBREF  4OVV B  322   600  UNP    P27986   P85A_HUMAN     322    600             
SEQADV 4OVV MET A  -28  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV SER A  -27  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV TYR A  -26  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV TYR A  -25  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV HIS A  -24  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV HIS A  -23  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV HIS A  -22  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV HIS A  -21  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV HIS A  -20  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV HIS A  -19  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV ASP A  -18  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV TYR A  -17  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV ASP A  -16  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV ILE A  -15  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV PRO A  -14  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV THR A  -13  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV THR A  -12  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV GLU A  -10  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV ASN A   -9  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV LEU A   -8  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV TYR A   -7  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV PHE A   -6  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV GLN A   -5  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV GLY A   -4  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV ALA A   -3  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV MET A   -2  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV GLY A   -1  UNP  P42336              EXPRESSION TAG                 
SEQADV 4OVV SER A    0  UNP  P42336              EXPRESSION TAG                 
SEQRES   1 A 1096  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 A 1096  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET          
SEQRES   3 A 1096  GLY SER MET PRO PRO ARG PRO SER SER GLY GLU LEU TRP          
SEQRES   4 A 1096  GLY ILE HIS LEU MET PRO PRO ARG ILE LEU VAL GLU CYS          
SEQRES   5 A 1096  LEU LEU PRO ASN GLY MET ILE VAL THR LEU GLU CYS LEU          
SEQRES   6 A 1096  ARG GLU ALA THR LEU ILE THR ILE LYS HIS GLU LEU PHE          
SEQRES   7 A 1096  LYS GLU ALA ARG LYS TYR PRO LEU HIS GLN LEU LEU GLN          
SEQRES   8 A 1096  ASP GLU SER SER TYR ILE PHE VAL SER VAL THR GLN GLU          
SEQRES   9 A 1096  ALA GLU ARG GLU GLU PHE PHE ASP GLU THR ARG ARG LEU          
SEQRES  10 A 1096  CYS ASP LEU ARG LEU PHE GLN PRO PHE LEU LYS VAL ILE          
SEQRES  11 A 1096  GLU PRO VAL GLY ASN ARG GLU GLU LYS ILE LEU ASN ARG          
SEQRES  12 A 1096  GLU ILE GLY PHE ALA ILE GLY MET PRO VAL CYS GLU PHE          
SEQRES  13 A 1096  ASP MET VAL LYS ASP PRO GLU VAL GLN ASP PHE ARG ARG          
SEQRES  14 A 1096  ASN ILE LEU ASN VAL CYS LYS GLU ALA VAL ASP LEU ARG          
SEQRES  15 A 1096  ASP LEU ASN SER PRO HIS SER ARG ALA MET TYR VAL TYR          
SEQRES  16 A 1096  PRO PRO ASN VAL GLU SER SER PRO GLU LEU PRO LYS HIS          
SEQRES  17 A 1096  ILE TYR ASN LYS LEU ASP LYS GLY GLN ILE ILE VAL VAL          
SEQRES  18 A 1096  ILE TRP VAL ILE VAL SER PRO ASN ASN ASP LYS GLN LYS          
SEQRES  19 A 1096  TYR THR LEU LYS ILE ASN HIS ASP CYS VAL PRO GLU GLN          
SEQRES  20 A 1096  VAL ILE ALA GLU ALA ILE ARG LYS LYS THR ARG SER MET          
SEQRES  21 A 1096  LEU LEU SER SER GLU GLN LEU LYS LEU CYS VAL LEU GLU          
SEQRES  22 A 1096  TYR GLN GLY LYS TYR ILE LEU LYS VAL CYS GLY CYS ASP          
SEQRES  23 A 1096  GLU TYR PHE LEU GLU LYS TYR PRO LEU SER GLN TYR LYS          
SEQRES  24 A 1096  TYR ILE ARG SER CYS ILE MET LEU GLY ARG MET PRO ASN          
SEQRES  25 A 1096  LEU MET LEU MET ALA LYS GLU SER LEU TYR SER GLN LEU          
SEQRES  26 A 1096  PRO MET ASP CYS PHE THR MET PRO SER TYR SER ARG ARG          
SEQRES  27 A 1096  ILE SER THR ALA THR PRO TYR MET ASN GLY GLU THR SER          
SEQRES  28 A 1096  THR LYS SER LEU TRP VAL ILE ASN SER ALA LEU ARG ILE          
SEQRES  29 A 1096  LYS ILE LEU CYS ALA THR TYR VAL ASN VAL ASN ILE ARG          
SEQRES  30 A 1096  ASP ILE ASP LYS ILE TYR VAL ARG THR GLY ILE TYR HIS          
SEQRES  31 A 1096  GLY GLY GLU PRO LEU CYS ASP ASN VAL ASN THR GLN ARG          
SEQRES  32 A 1096  VAL PRO CYS SER ASN PRO ARG TRP ASN GLU TRP LEU ASN          
SEQRES  33 A 1096  TYR ASP ILE TYR ILE PRO ASP LEU PRO ARG ALA ALA ARG          
SEQRES  34 A 1096  LEU CYS LEU SER ILE CYS SER VAL LYS GLY ARG LYS GLY          
SEQRES  35 A 1096  ALA LYS GLU GLU HIS CYS PRO LEU ALA TRP GLY ASN ILE          
SEQRES  36 A 1096  ASN LEU PHE ASP TYR THR ASP THR LEU VAL SER GLY LYS          
SEQRES  37 A 1096  MET ALA LEU ASN LEU TRP PRO VAL PRO HIS GLY LEU GLU          
SEQRES  38 A 1096  ASP LEU LEU ASN PRO ILE GLY VAL THR GLY SER ASN PRO          
SEQRES  39 A 1096  ASN LYS GLU THR PRO CYS LEU GLU LEU GLU PHE ASP TRP          
SEQRES  40 A 1096  PHE SER SER VAL VAL LYS PHE PRO ASP MET SER VAL ILE          
SEQRES  41 A 1096  GLU GLU HIS ALA ASN TRP SER VAL SER ARG GLU ALA GLY          
SEQRES  42 A 1096  PHE SER TYR SER HIS ALA GLY LEU SER ASN ARG LEU ALA          
SEQRES  43 A 1096  ARG ASP ASN GLU LEU ARG GLU ASN ASP LYS GLU GLN LEU          
SEQRES  44 A 1096  LYS ALA ILE SER THR ARG ASP PRO LEU SER GLU ILE THR          
SEQRES  45 A 1096  GLU GLN GLU LYS ASP PHE LEU TRP SER HIS ARG HIS TYR          
SEQRES  46 A 1096  CYS VAL THR ILE PRO GLU ILE LEU PRO LYS LEU LEU LEU          
SEQRES  47 A 1096  SER VAL LYS TRP ASN SER ARG ASP GLU VAL ALA GLN MET          
SEQRES  48 A 1096  TYR CYS LEU VAL LYS ASP TRP PRO PRO ILE LYS PRO GLU          
SEQRES  49 A 1096  GLN ALA MET GLU LEU LEU ASP CYS ASN TYR PRO ASP PRO          
SEQRES  50 A 1096  MET VAL ARG GLY PHE ALA VAL ARG CYS LEU GLU LYS TYR          
SEQRES  51 A 1096  LEU THR ASP ASP LYS LEU SER GLN TYR LEU ILE GLN LEU          
SEQRES  52 A 1096  VAL GLN VAL LEU LYS TYR GLU GLN TYR LEU ASP ASN LEU          
SEQRES  53 A 1096  LEU VAL ARG PHE LEU LEU LYS LYS ALA LEU THR ASN GLN          
SEQRES  54 A 1096  ARG ILE GLY HIS PHE PHE PHE TRP HIS LEU LYS SER GLU          
SEQRES  55 A 1096  MET HIS ASN LYS THR VAL SER GLN ARG PHE GLY LEU LEU          
SEQRES  56 A 1096  LEU GLU SER TYR CYS ARG ALA CYS GLY MET TYR LEU LYS          
SEQRES  57 A 1096  HIS LEU ASN ARG GLN VAL GLU ALA MET GLU LYS LEU ILE          
SEQRES  58 A 1096  ASN LEU THR ASP ILE LEU LYS GLN GLU LYS LYS ASP GLU          
SEQRES  59 A 1096  THR GLN LYS VAL GLN MET LYS PHE LEU VAL GLU GLN MET          
SEQRES  60 A 1096  ARG ARG PRO ASP PHE MET ASP ALA LEU GLN GLY PHE LEU          
SEQRES  61 A 1096  SER PRO LEU ASN PRO ALA HIS GLN LEU GLY ASN LEU ARG          
SEQRES  62 A 1096  LEU GLU GLU CYS ARG ILE MET SER SER ALA LYS ARG PRO          
SEQRES  63 A 1096  LEU TRP LEU ASN TRP GLU ASN PRO ASP ILE MET SER GLU          
SEQRES  64 A 1096  LEU LEU PHE GLN ASN ASN GLU ILE ILE PHE LYS ASN GLY          
SEQRES  65 A 1096  ASP ASP LEU ARG GLN ASP MET LEU THR LEU GLN ILE ILE          
SEQRES  66 A 1096  ARG ILE MET GLU ASN ILE TRP GLN ASN GLN GLY LEU ASP          
SEQRES  67 A 1096  LEU ARG MET LEU PRO TYR GLY CYS LEU SER ILE GLY ASP          
SEQRES  68 A 1096  CYS VAL GLY LEU ILE GLU VAL VAL ARG ASN SER HIS THR          
SEQRES  69 A 1096  ILE MET GLN ILE GLN CYS LYS GLY GLY LEU LYS GLY ALA          
SEQRES  70 A 1096  LEU GLN PHE ASN SER HIS THR LEU HIS GLN TRP LEU LYS          
SEQRES  71 A 1096  ASP LYS ASN LYS GLY GLU ILE TYR ASP ALA ALA ILE ASP          
SEQRES  72 A 1096  LEU PHE THR ARG SER CYS ALA GLY TYR CYS VAL ALA THR          
SEQRES  73 A 1096  PHE ILE LEU GLY ILE GLY ASP ARG HIS ASN SER ASN ILE          
SEQRES  74 A 1096  MET VAL LYS ASP ASP GLY GLN LEU PHE HIS ILE ASP PHE          
SEQRES  75 A 1096  GLY HIS PHE LEU ASP HIS LYS LYS LYS LYS PHE GLY TYR          
SEQRES  76 A 1096  LYS ARG GLU ARG VAL PRO PHE VAL LEU THR GLN ASP PHE          
SEQRES  77 A 1096  LEU ILE VAL ILE SER LYS GLY ALA GLN GLU CYS THR LYS          
SEQRES  78 A 1096  THR ARG GLU PHE GLU ARG PHE GLN GLU MET CYS TYR LYS          
SEQRES  79 A 1096  ALA TYR LEU ALA ILE ARG GLN HIS ALA ASN LEU PHE ILE          
SEQRES  80 A 1096  ASN LEU PHE SER MET MET LEU GLY SER GLY MET PRO GLU          
SEQRES  81 A 1096  LEU GLN SER PHE ASP ASP ILE ALA TYR ILE ARG LYS THR          
SEQRES  82 A 1096  LEU ALA LEU ASP LYS THR GLU GLN GLU ALA LEU GLU TYR          
SEQRES  83 A 1096  PHE MET LYS GLN MET ASN ASP ALA HIS HIS GLY GLY TRP          
SEQRES  84 A 1096  THR THR LYS MET ASP TRP ILE PHE HIS THR ILE LYS GLN          
SEQRES  85 A 1096  HIS ALA LEU ASN                                              
SEQRES   1 B  279  MET ASN ASN ASN MET SER LEU GLN ASP ALA GLU TRP TYR          
SEQRES   2 B  279  TRP GLY ASP ILE SER ARG GLU GLU VAL ASN GLU LYS LEU          
SEQRES   3 B  279  ARG ASP THR ALA ASP GLY THR PHE LEU VAL ARG ASP ALA          
SEQRES   4 B  279  SER THR LYS MET HIS GLY ASP TYR THR LEU THR LEU ARG          
SEQRES   5 B  279  LYS GLY GLY ASN ASN LYS LEU ILE LYS ILE PHE HIS ARG          
SEQRES   6 B  279  ASP GLY LYS TYR GLY PHE SER ASP PRO LEU THR PHE SER          
SEQRES   7 B  279  SER VAL VAL GLU LEU ILE ASN HIS TYR ARG ASN GLU SER          
SEQRES   8 B  279  LEU ALA GLN TYR ASN PRO LYS LEU ASP VAL LYS LEU LEU          
SEQRES   9 B  279  TYR PRO VAL SER LYS TYR GLN GLN ASP GLN VAL VAL LYS          
SEQRES  10 B  279  GLU ASP ASN ILE GLU ALA VAL GLY LYS LYS LEU HIS GLU          
SEQRES  11 B  279  TYR ASN THR GLN PHE GLN GLU LYS SER ARG GLU TYR ASP          
SEQRES  12 B  279  ARG LEU TYR GLU GLU TYR THR ARG THR SER GLN GLU ILE          
SEQRES  13 B  279  GLN MET LYS ARG THR ALA ILE GLU ALA PHE ASN GLU THR          
SEQRES  14 B  279  ILE LYS ILE PHE GLU GLU GLN CYS GLN THR GLN GLU ARG          
SEQRES  15 B  279  TYR SER LYS GLU TYR ILE GLU LYS PHE LYS ARG GLU GLY          
SEQRES  16 B  279  ASN GLU LYS GLU ILE GLN ARG ILE MET HIS ASN TYR ASP          
SEQRES  17 B  279  LYS LEU LYS SER ARG ILE SER GLU ILE ILE ASP SER ARG          
SEQRES  18 B  279  ARG ARG LEU GLU GLU ASP LEU LYS LYS GLN ALA ALA GLU          
SEQRES  19 B  279  TYR ARG GLU ILE ASP LYS ARG MET ASN SER ILE LYS PRO          
SEQRES  20 B  279  ASP LEU ILE GLN LEU ARG LYS THR ARG ASP GLN TYR LEU          
SEQRES  21 B  279  MET TRP LEU THR GLN LYS GLY VAL ARG GLN LYS LYS LEU          
SEQRES  22 B  279  ASN GLU TRP LEU GLY ASN                                      
HET    PBU  A1101      39                                                       
HET    PO4  A1102       5                                                       
HET    PBU  B2001      39                                                       
HETNAM     PBU (2R)-3-{[(R)-HYDROXY{[(1R,2R,3S,4R,5R,6S)-2,3,6-                 
HETNAM   2 PBU  TRIHYDROXY-4,5-BIS(PHOSPHONOOXY)                                
HETNAM   3 PBU  CYCLOHEXYL]OXY}PHOSPHORYL]OXY}PROPANE-1,2-DIYL                  
HETNAM   4 PBU  DIBUTANOATE                                                     
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     PBU DI-BUTANOYL L-ALPHA-PHOSPHATIDYL-D-MYO-INOSITOL 4,5-             
HETSYN   2 PBU  BISPHOSPHATE; DI-C4-PIP2                                        
FORMUL   3  PBU    2(C17 H33 O19 P3)                                            
FORMUL   4  PO4    O4 P 3-                                                      
FORMUL   6  HOH   *4(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 ASP A   64  TYR A   68  5                                   5    
HELIX    4 AA4 ASN A  114  GLY A  122  1                                   9    
HELIX    5 AA5 VAL A  125  MET A  130  1                                   6    
HELIX    6 AA6 GLU A  135  ILE A  143  1                                   9    
HELIX    7 AA7 ILE A  143  ASP A  155  1                                  13    
HELIX    8 AA8 LEU A  156  SER A  158  5                                   3    
HELIX    9 AA9 PRO A  159  TYR A  167  1                                   9    
HELIX   10 AB1 PRO A  178  ASN A  183  1                                   6    
HELIX   11 AB2 VAL A  216  ARG A  230  1                                  15    
HELIX   12 AB3 SER A  235  TYR A  246  1                                  12    
HELIX   13 AB4 PRO A  266  GLN A  269  5                                   4    
HELIX   14 AB5 TYR A  270  LEU A  279  1                                  10    
HELIX   15 AB6 LYS A  290  LEU A  297  1                                   8    
HELIX   16 AB7 SER A  326  ILE A  330  5                                   5    
HELIX   17 AB8 PRO A  394  LEU A  396  5                                   3    
HELIX   18 AB9 ASP A  488  ALA A  504  1                                  17    
HELIX   19 AC1 GLU A  525  GLU A  529  5                                   5    
HELIX   20 AC2 GLN A  530  ARG A  537  1                                   8    
HELIX   21 AC3 THR A  544  HIS A  554  1                                  11    
HELIX   22 AC4 HIS A  554  VAL A  559  1                                   6    
HELIX   23 AC5 ILE A  561  GLU A  563  5                                   3    
HELIX   24 AC6 ILE A  564  VAL A  572  1                                   9    
HELIX   25 AC7 SER A  576  ASP A  589  1                                  14    
HELIX   26 AC8 LYS A  594  MET A  599  1                                   6    
HELIX   27 AC9 GLU A  600  ASP A  603  5                                   4    
HELIX   28 AD1 ASP A  608  TYR A  622  1                                  15    
HELIX   29 AD2 ASP A  626  TYR A  631  1                                   6    
HELIX   30 AD3 TYR A  631  LEU A  639  1                                   9    
HELIX   31 AD4 LYS A  640  GLU A  642  5                                   3    
HELIX   32 AD5 ASN A  647  ASN A  660  1                                  14    
HELIX   33 AD6 ASN A  660  GLU A  674  1                                  15    
HELIX   34 AD7 MET A  675  ASN A  677  5                                   3    
HELIX   35 AD8 VAL A  680  CYS A  695  1                                  16    
HELIX   36 AD9 MET A  697  GLN A  721  1                                  25    
HELIX   37 AE1 THR A  727  ARG A  741  1                                  15    
HELIX   38 AE2 ARG A  741  LEU A  748  1                                   8    
HELIX   39 AE3 MET A  789  LEU A  793  5                                   5    
HELIX   40 AE4 LEU A  807  ASN A  826  1                                  20    
HELIX   41 AE5 ILE A  857  GLY A  864  1                                   8    
HELIX   42 AE6 HIS A  875  ASN A  885  1                                  11    
HELIX   43 AE7 GLY A  887  LEU A  911  1                                  25    
HELIX   44 AE8 THR A  957  SER A  965  1                                   9    
HELIX   45 AE9 THR A  974  GLN A  993  1                                  20    
HELIX   46 AF1 HIS A  994  LEU A 1006  1                                  13    
HELIX   47 AF2 ASP A 1018  ALA A 1020  5                                   3    
HELIX   48 AF3 TYR A 1021  LEU A 1026  1                                   6    
HELIX   49 AF4 THR A 1031  HIS A 1047  1                                  17    
HELIX   50 AF5 SER B  339  GLU B  345  1                                   7    
HELIX   51 AF6 VAL B  401  ASN B  406  1                                   6    
HELIX   52 AF7 GLN B  435  GLU B  439  5                                   5    
HELIX   53 AF8 GLU B  443  LYS B  506  1                                  64    
HELIX   54 AF9 GLU B  518  SER B  565  1                                  48    
HELIX   55 AG1 ILE B  566  GLY B  588  1                                  23    
SHEET    1 AA1 5 ILE A  31  LEU A  37  0                                        
SHEET    2 AA1 5 ARG A  19  LEU A  25 -1  N  VAL A  22   O  LEU A  34           
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 4 GLN A 205  ASN A 212  0                                        
SHEET    2 AA2 4 GLN A 189  VAL A 196 -1  N  ILE A 194   O  TYR A 207           
SHEET    3 AA2 4 ASN A 284  ALA A 289  1  O  LEU A 287   N  TRP A 195           
SHEET    4 AA2 4 TYR A 250  VAL A 254 -1  N  LYS A 253   O  MET A 286           
SHEET    1 AA3 4 TRP A 386  TYR A 392  0                                        
SHEET    2 AA3 4 ALA A 333  ALA A 341 -1  N  ILE A 336   O  LEU A 387           
SHEET    3 AA3 4 CYS A 472  PHE A 477 -1  O  GLU A 476   N  LYS A 337           
SHEET    4 AA3 4 GLY A 439  ASN A 444 -1  N  MET A 441   O  LEU A 475           
SHEET    1 AA4 4 LYS A 353  TYR A 361  0                                        
SHEET    2 AA4 4 ARG A 401  VAL A 409 -1  O  SER A 405   N  ARG A 357           
SHEET    3 AA4 4 CYS A 420  ASN A 428 -1  O  LEU A 422   N  ILE A 406           
SHEET    4 AA4 4 TRP A 446  PRO A 447 -1  O  TRP A 446   N  TRP A 424           
SHEET    1 AA5 2 PHE A 751  LEU A 752  0                                        
SHEET    2 AA5 2 GLN A 760  LEU A 761 -1  O  LEU A 761   N  PHE A 751           
SHEET    1 AA6 5 ARG A 770  ILE A 771  0                                        
SHEET    2 AA6 5 LEU A 779  GLU A 784 -1  O  TRP A 780   N  ARG A 770           
SHEET    3 AA6 5 ASN A 796  ASN A 803 -1  O  ASN A 797   N  TRP A 783           
SHEET    4 AA6 5 VAL A 845  GLU A 849 -1  O  ILE A 848   N  ILE A 800           
SHEET    5 AA6 5 CYS A 838  SER A 840 -1  N  LEU A 839   O  LEU A 847           
SHEET    1 AA7 3 SER A 854  THR A 856  0                                        
SHEET    2 AA7 3 ILE A 921  LYS A 924 -1  O  VAL A 923   N  HIS A 855           
SHEET    3 AA7 3 LEU A 929  HIS A 931 -1  O  PHE A 930   N  MET A 922           
SHEET    1 AA8 2 LEU B 370  THR B 371  0                                        
SHEET    2 AA8 2 LEU B 380  ILE B 381 -1  O  ILE B 381   N  LEU B 370           
CISPEP   1 SER A  158    PRO A  159          0        12.47                     
CISPEP   2 SER A  199    PRO A  200          0        17.26                     
CISPEP   3 PRO A  200    ASN A  201          0         6.15                     
CISPEP   4 PHE B  398    SER B  399          0       -14.64                     
SITE     1 AC1  3 GLY A  12  PRO A  17  GLU A 722                               
SITE     1 AC2  6 GLN A 205  LYS A 206  TYR A 207  THR A 208                    
SITE     2 AC2  6 LYS A 227  ARG B 461                                          
CRYST1  114.259  116.083  148.743  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      0.008752  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008615  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006723        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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