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Database: PDB
Entry: 5SWO
LinkDB: 5SWO
Original site: 5SWO 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       08-AUG-16   5SWO              
TITLE     CRYSTAL STRUCTURE OF PI3KALPHA IN COMPLEX WITH FRAGMENTS 4 AND 19     
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 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT ALPHA;    
COMPND  13 CHAIN: B;                                                            
COMPND  14 SYNONYM: PTDINS-3-KINASE REGULATORY SUBUNIT ALPHA,                   
COMPND  15 PHOSPHATIDYLINOSITOL 3-KINASE 85 KDA REGULATORY SUBUNIT ALPHA,PTDINS-
COMPND  16 3-KINASE REGULATORY SUBUNIT P85-ALPHA;                               
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PIK3CA;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HT-A;                            
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: PIK3R1, GRB1;                                                  
SOURCE  17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  18 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  20 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HT-A                             
KEYWDS    LIPID KINASE, PHOSPHOINOSITIDE, 3-KINASE, SIGNALING, TRANSFERASE-     
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.B.GABELLI,B.VOGELSTEIN,M.S.MILLER,L.M.AMZEL                         
REVDAT   2   20-SEP-17 5SWO    1       REMARK                                   
REVDAT   1   15-FEB-17 5SWO    0                                                
JRNL        AUTH   M.S.MILLER,S.MAHESHWARI,F.M.MCROBB,K.W.KINZLER,L.M.AMZEL,    
JRNL        AUTH 2 B.VOGELSTEIN,S.B.GABELLI                                     
JRNL        TITL   IDENTIFICATION OF ALLOSTERIC BINDING SITES FOR PI3K ALPHA    
JRNL        TITL 2 ONCOGENIC MUTANT SPECIFIC INHIBITOR DESIGN.                  
JRNL        REF    BIOORG. MED. CHEM.            V.  25  1481 2017              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   28129991                                                     
JRNL        DOI    10.1016/J.BMC.2017.01.012                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 91.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24324                          
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1322                            
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) : 3.60                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1655                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 99                           
REMARK   3   BIN FREE R VALUE                    : 0.2860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10874                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 116.1                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.47000                                              
REMARK   3    B22 (A**2) : -1.52000                                             
REMARK   3    B33 (A**2) : -1.96000                                             
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): 0.656         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.463         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.192        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.867                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11138 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 10664 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15027 ; 1.537 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24561 ; 1.010 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1311 ; 7.386 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   561 ;37.815 ;24.242       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2085 ;18.986 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    77 ;14.814 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1612 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12428 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2610 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5265 ; 7.319 ;11.325       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5264 ; 7.309 ;11.324       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6569 ;11.591 ;16.965       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5SWO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223264.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25700                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 91.810                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60100                            
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 4OVU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NAFORMATE, PH 7.0, 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       57.41300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.72100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.18000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.72100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.41300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.18000            
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: 7610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 60190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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   -27                                                      
REMARK 465     THR A   -11                                                      
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     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     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     THR A  1053                                                      
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   337                                                      
REMARK 465     ILE B   338                                                      
REMARK 465     SER B   339                                                      
REMARK 465     ALA B   360                                                      
REMARK 465     SER B   361                                                      
REMARK 465     GLY B   599                                                      
REMARK 465     ASN B   600                                                      
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     ARG A 765    CG   CD   NE   CZ   NH1  NH2                        
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    HIS A -22       41.08     33.10                                   
REMARK 500    MET A   1       37.00     88.16                                   
REMARK 500    PRO A   3       19.05   -145.63                                   
REMARK 500    ARG A  54      -34.87    -38.97                                   
REMARK 500    SER A  67       37.85    -91.80                                   
REMARK 500    ILE A 112       32.43    -88.77                                   
REMARK 500    LEU A 113       61.11   -105.86                                   
REMARK 500    ASP A 133      122.78    -30.96                                   
REMARK 500    ASP A 155       33.86    -82.17                                   
REMARK 500    LYS A 187       56.59     38.37                                   
REMARK 500    SER A 199      140.32   -171.83                                   
REMARK 500    ASN A 201     -147.82   -151.02                                   
REMARK 500    ASN A 202       -3.78     60.46                                   
REMARK 500    LYS A 264       97.88    -50.06                                   
REMARK 500    CYS A 301       72.91     46.98                                   
REMARK 500    THR A 322     -166.06    162.68                                   
REMARK 500    SER A 323       88.45    -63.53                                   
REMARK 500    ASN A 331       67.76   -112.69                                   
REMARK 500    LEU A 339      -71.20   -126.82                                   
REMARK 500    ASP A 352      -72.22    -65.46                                   
REMARK 500    VAL A 371     -163.42   -111.08                                   
REMARK 500    GLN A 374       41.18    -79.55                                   
REMARK 500    VAL A 376       69.80     38.94                                   
REMARK 500    CYS A 378     -120.67   -144.40                                   
REMARK 500    SER A 379     -113.31     56.98                                   
REMARK 500    ASN A 384       65.93   -109.14                                   
REMARK 500    ASP A 390       76.21    -69.74                                   
REMARK 500    ARG A 398      -39.59    -37.52                                   
REMARK 500    SER A 405      124.86   -170.28                                   
REMARK 500    CYS A 420      118.64   -164.32                                   
REMARK 500    ASP A 434       12.76     81.11                                   
REMARK 500    ASN A 457       77.27     58.07                                   
REMARK 500    ASN A 467      109.21    -58.53                                   
REMARK 500    PRO A 471      103.59    -37.74                                   
REMARK 500    PHE A 480       51.16   -107.67                                   
REMARK 500    SER A 481        8.48     50.37                                   
REMARK 500    ALA A 511       -4.01    -53.72                                   
REMARK 500    LEU A 513       86.38   -152.22                                   
REMARK 500    ARG A 516      -94.93     59.75                                   
REMARK 500    LEU A 517      178.13     89.94                                   
REMARK 500    ARG A 519      -54.26    -22.91                                   
REMARK 500    ASP A 520     -123.65     58.63                                   
REMARK 500    LEU A 523     -172.01     67.96                                   
REMARK 500    ILE A 561       70.70   -110.28                                   
REMARK 500    ASP A 589       51.39   -143.35                                   
REMARK 500    LYS A 621      -70.57    -74.23                                   
REMARK 500    GLN A 749      -60.34    -96.57                                   
REMARK 500    ASN A 756      109.33   -169.16                                   
REMARK 500    LEU A 793      -61.91   -124.16                                   
REMARK 500    ASP A 805      -49.69     89.93                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      94 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                  148.54                    
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 CL A 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 70T A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2ZV B 701                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5SW8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SWG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SWP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SWR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SWT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SX8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SX9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SXA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SXB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SXC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SXD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SXE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SXF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SXI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SXJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5SXK   RELATED DB: PDB                                   
DBREF  5SWO A    1  1068  UNP    P42336   PK3CA_HUMAN      1   1068             
DBREF  5SWO B  322   600  UNP    P27986   P85A_HUMAN     322    600             
SEQADV 5SWO MET A  -27  UNP  P42336              INITIATING METHIONINE          
SEQADV 5SWO SER A  -26  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO TYR A  -25  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO TYR A  -24  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO HIS A  -23  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO HIS A  -22  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO HIS A  -21  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO HIS A  -20  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO HIS A  -19  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO HIS A  -18  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO ASP A  -17  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO TYR A  -16  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO ASP A  -15  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO ILE A  -14  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO PRO A  -13  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO THR A  -12  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO THR A  -11  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO GLU A  -10  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO ASN A   -9  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO LEU A   -8  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO TYR A   -7  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO PHE A   -6  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO GLN A   -5  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO GLY A   -4  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO ALA A   -3  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO MET A   -2  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO GLY A   -1  UNP  P42336              EXPRESSION TAG                 
SEQADV 5SWO 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 SEP 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                                      
MODRES 5SWO SEP A  790  SER  MODIFIED RESIDUE                                   
HET    SEP  A 790      10                                                       
HET     CL  A1101       1                                                       
HET    70T  A1102      13                                                       
HET    2ZV  B 701      11                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     70T 2-METHYL-5-NITRO-1H-INDOLE                                       
HETNAM     2ZV 4-METHYL-3-NITROPYRIDIN-2-AMINE                                  
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  70T    C9 H8 N2 O2                                                  
FORMUL   5  2ZV    C6 H7 N3 O2                                                  
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 GLU A  109  LEU A  113  5                                   5    
HELIX    7 AA7 ASN A  114  GLY A  122  1                                   9    
HELIX    8 AA8 VAL A  125  MET A  130  1                                   6    
HELIX    9 AA9 ASP A  133  ASP A  155  1                                  23    
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  THR A  229  1                                  14    
HELIX   13 AB4 SER A  235  GLY A  248  1                                  14    
HELIX   14 AB5 PRO A  266  GLN A  269  5                                   4    
HELIX   15 AB6 TYR A  270  LEU A  279  1                                  10    
HELIX   16 AB7 LYS A  290  GLN A  296  1                                   7    
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  GLY A  505  1                                  18    
HELIX   20 AC2 SER A  507  GLY A  512  1                                   6    
HELIX   21 AC3 ARG A  524  THR A  536  1                                  13    
HELIX   22 AC4 THR A  544  HIS A  554  1                                  11    
HELIX   23 AC5 HIS A  556  THR A  560  5                                   5    
HELIX   24 AC6 ILE A  561  GLU A  563  5                                   3    
HELIX   25 AC7 ILE A  564  LEU A  570  1                                   7    
HELIX   26 AC8 SER A  576  ASP A  589  1                                  14    
HELIX   27 AC9 LYS A  594  MET A  599  1                                   6    
HELIX   28 AD1 GLU A  600  ASP A  603  5                                   4    
HELIX   29 AD2 ASP A  608  TYR A  622  1                                  15    
HELIX   30 AD3 THR A  624  TYR A  631  1                                   8    
HELIX   31 AD4 TYR A  631  VAL A  638  1                                   8    
HELIX   32 AD5 LEU A  639  GLU A  642  5                                   4    
HELIX   33 AD6 ASN A  647  ASN A  660  1                                  14    
HELIX   34 AD7 ASN A  660  GLU A  674  1                                  15    
HELIX   35 AD8 VAL A  680  CYS A  695  1                                  16    
HELIX   36 AD9 MET A  697  GLU A  722  1                                  26    
HELIX   37 AE1 THR A  727  ARG A  741  1                                  15    
HELIX   38 AE2 ARG A  741  GLY A  750  1                                  10    
HELIX   39 AE3 MET A  789  PHE A  794  1                                   6    
HELIX   40 AE4 LEU A  807  ASN A  826  1                                  20    
HELIX   41 AE5 ILE A  857  GLY A  865  1                                   9    
HELIX   42 AE6 HIS A  875  ASN A  885  1                                  11    
HELIX   43 AE7 GLY A  887  GLY A  912  1                                  26    
HELIX   44 AE8 HIS A  917  SER A  919  5                                   3    
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  LEU A 1006  1                                  13    
HELIX   49 AF4 SER A 1015  ALA A 1020  1                                   6    
HELIX   50 AF5 ALA A 1020  ALA A 1027  1                                   8    
HELIX   51 AF6 THR A 1031  HIS A 1048  1                                  18    
HELIX   52 AF7 GLU B  341  ARG B  348  1                                   8    
HELIX   53 AF8 SER B  400  GLU B  411  1                                  12    
HELIX   54 AF9 GLN B  435  GLU B  439  5                                   5    
HELIX   55 AG1 ILE B  442  LYS B  511  1                                  70    
HELIX   56 AG2 ASN B  517  GLY B  588  1                                  72    
HELIX   57 AG3 LYS B  592  TRP B  597  5                                   6    
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  LEU A  25           
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 VAL A 193  TRP A 195  0                                        
SHEET    2 AA2 4 ASN A 284  ALA A 289  1  O  LEU A 287   N  TRP A 195           
SHEET    3 AA2 4 TYR A 250  VAL A 254 -1  N  ILE A 251   O  MET A 288           
SHEET    4 AA2 4 CYS A 257  PHE A 261 -1  O  PHE A 261   N  LEU A 252           
SHEET    1 AA3 2 LYS A 325  SER A 326  0                                        
SHEET    2 AA3 2 VAL A 484  LYS A 485  1  O  LYS A 485   N  LYS A 325           
SHEET    1 AA4 4 TRP A 386  TYR A 392  0                                        
SHEET    2 AA4 4 ALA A 333  ALA A 341 -1  N  LEU A 334   O  TYR A 389           
SHEET    3 AA4 4 CYS A 472  PHE A 477 -1  O  GLU A 476   N  LYS A 337           
SHEET    4 AA4 4 GLY A 439  ASN A 444 -1  N  GLY A 439   O  PHE A 477           
SHEET    1 AA5 3 ILE A 360  TYR A 361  0                                        
SHEET    2 AA5 3 ARG A 401  SER A 408 -1  O  ARG A 401   N  TYR A 361           
SHEET    3 AA5 3 CYS A 420  PRO A 421 -1  O  CYS A 420   N  SER A 408           
SHEET    1 AA6 5 ASN A 370  VAL A 371  0                                        
SHEET    2 AA6 5 ILE A 354  THR A 358 -1  N  THR A 358   O  ASN A 370           
SHEET    3 AA6 5 ARG A 401  SER A 408 -1  O  SER A 405   N  ARG A 357           
SHEET    4 AA6 5 ALA A 423  ASN A 428 -1  O  ILE A 427   N  LEU A 402           
SHEET    5 AA6 5 TRP A 446  PRO A 447 -1  O  TRP A 446   N  TRP A 424           
SHEET    1 AA7 2 PHE A 751  LEU A 752  0                                        
SHEET    2 AA7 2 GLN A 760  LEU A 761 -1  O  LEU A 761   N  PHE A 751           
SHEET    1 AA8 5 ARG A 770  ILE A 771  0                                        
SHEET    2 AA8 5 LEU A 779  GLU A 784 -1  O  TRP A 780   N  ARG A 770           
SHEET    3 AA8 5 ASN A 796  LYS A 802 -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  ILE 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  PHE A 930   N  MET A 922           
SHEET    1 AB1 4 PHE B 355  ARG B 358  0                                        
SHEET    2 AB1 4 TYR B 368  ARG B 373 -1  O  THR B 371   N  LEU B 356           
SHEET    3 AB1 4 ASN B 378  HIS B 385 -1  O  LYS B 379   N  LEU B 372           
SHEET    4 AB1 4 TYR B 390  GLY B 391 -1  O  GLY B 391   N  PHE B 384           
LINK         C   MET A 789                 N   SEP A 790     1555   1555  1.34  
LINK         C   SEP A 790                 N   GLU A 791     1555   1555  1.33  
CISPEP   1 ARG A    4    PRO A    5          0         0.29                     
CISPEP   2 SER A  158    PRO A  159          0        13.17                     
CISPEP   3 SER A  199    PRO A  200          0       -11.87                     
SITE     1 AC1  2 LEU A 233  GLU A 849                                          
SITE     1 AC2  2 LYS A 271  CYS A 838                                          
SITE     1 AC3  3 ASN B 344  ASN B 377  ASN B 378                               
CRYST1  114.826  116.360  149.442  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      0.008709  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008594  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006692        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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