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Database: PDB
Entry: 4L23
LinkDB: 4L23
Original site: 4L23 
HEADER    SIGNALING PROTEIN/TRANSFERASE/INHIBITOR 04-JUN-13   4L23              
TITLE     CRYSTAL STRUCTURE OF P110ALPHA COMPLEXED WITH NISH2 OF P85ALPHA AND   
TITLE    2 PI-103                                                               
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: PI3-KINASE SUBUNIT ALPHA, PI3K-ALPHA, PI3KALPHA, PTDINS-3-  
COMPND   6 KINASE SUBUNIT ALPHA, PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE 
COMPND   7 110 KDA CATALYTIC SUBUNIT ALPHA, PTDINS-3-KINASE SUBUNIT P110-ALPHA, 
COMPND   8 P110ALPHA, PHOSPHOINOSITIDE-3-KINASE CATALYTIC ALPHA POLYPEPTIDE,    
COMPND   9 SERINE/THREONINE PROTEIN KINASE PIK3CA;                              
COMPND  10 EC: 2.7.1.153, 2.7.11.1;                                             
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 2;                                                           
COMPND  13 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT ALPHA;    
COMPND  14 CHAIN: B;                                                            
COMPND  15 FRAGMENT: NISH2 OF P85ALPHA, UNP RESIDUES 318-615;                   
COMPND  16 SYNONYM: PI3-KINASE REGULATORY SUBUNIT ALPHA, PI3K REGULATORY SUBUNIT
COMPND  17 ALPHA, PTDINS-3-KINASE REGULATORY SUBUNIT ALPHA, PHOSPHATIDYLINOSITOL
COMPND  18 3-KINASE 85 KDA REGULATORY SUBUNIT ALPHA, PI3-KINASE SUBUNIT P85-    
COMPND  19 ALPHA, PTDINS-3-KINASE REGULATORY SUBUNIT P85-ALPHA;                 
COMPND  20 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_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HTB;                             
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: GRB1, PIK3R1;                                                  
SOURCE  16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HTB                              
KEYWDS    ATP BINDING, PI-103, SIGNALING PROTEIN-TRANSFERASE-INHIBITOR COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ZHANG,Y.L.ZHAO,Y.Y.CHEN,M.HUANG,F.JIANG                             
REVDAT   3   15-NOV-17 4L23    1       REMARK                                   
REVDAT   2   01-APR-15 4L23    1       JRNL                                     
REVDAT   1   01-JAN-14 4L23    0                                                
JRNL        AUTH   Y.ZHAO,X.ZHANG,Y.CHEN,S.LU,Y.PENG,X.WANG,C.GUO,A.ZHOU,       
JRNL        AUTH 2 J.ZHANG,Y.LUO,Q.SHEN,J.DING,L.MENG,J.ZHANG                   
JRNL        TITL   CRYSTAL STRUCTURES OF PI3K ALPHA COMPLEXED WITH PI103 AND    
JRNL        TITL 2 ITS DERIVATIVES: NEW DIRECTIONS FOR INHIBITORS DESIGN.       
JRNL        REF    ACS MED CHEM LETT             V.   5   138 2014              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   24900786                                                     
JRNL        DOI    10.1021/ML400378E                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 51022                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2605                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.9780 -  6.7783    0.98     2608   152  0.1876 0.2293        
REMARK   3     2  6.7783 -  5.3847    1.00     2525   149  0.2227 0.2671        
REMARK   3     3  5.3847 -  4.7053    1.00     2500   123  0.1815 0.2073        
REMARK   3     4  4.7053 -  4.2757    1.00     2495   140  0.1783 0.2451        
REMARK   3     5  4.2757 -  3.9696    1.00     2483   128  0.1814 0.2247        
REMARK   3     6  3.9696 -  3.7357    1.00     2457   130  0.1909 0.2668        
REMARK   3     7  3.7357 -  3.5488    1.00     2475   126  0.2063 0.2963        
REMARK   3     8  3.5488 -  3.3944    1.00     2455   131  0.2102 0.2745        
REMARK   3     9  3.3944 -  3.2638    1.00     2435   127  0.2322 0.2813        
REMARK   3    10  3.2638 -  3.1512    0.99     2443   135  0.2392 0.3265        
REMARK   3    11  3.1512 -  3.0527    1.00     2468   114  0.2538 0.3110        
REMARK   3    12  3.0527 -  2.9655    1.00     2388   144  0.2470 0.3312        
REMARK   3    13  2.9655 -  2.8874    1.00     2468   118  0.2468 0.3465        
REMARK   3    14  2.8874 -  2.8170    1.00     2457   120  0.2499 0.3048        
REMARK   3    15  2.8170 -  2.7530    0.99     2412   135  0.2657 0.3182        
REMARK   3    16  2.7530 -  2.6944    0.99     2422   144  0.2878 0.3639        
REMARK   3    17  2.6944 -  2.6405    0.98     2360   149  0.2702 0.3221        
REMARK   3    18  2.6405 -  2.5907    0.96     2364   119  0.2775 0.3589        
REMARK   3    19  2.5907 -  2.5445    0.90     2177   110  0.2885 0.3401        
REMARK   3    20  2.5445 -  2.5010    0.83     2025   111  0.2931 0.3202        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          10901                                  
REMARK   3   ANGLE     :  0.846          14708                                  
REMARK   3   CHIRALITY :  0.055           1586                                  
REMARK   3   PLANARITY :  0.003           1884                                  
REMARK   3   DIHEDRAL  : 17.993           4173                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4L23 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080083.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51267                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : 0.07700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.50500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M LITHIUM SULFATE, 0.1 M TRIS PH    
REMARK 280  8.5, 30%(W/V) PEG 1000MME, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 291K                                                    
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       35.81400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.74350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.18850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.74350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.81400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       68.18850            
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: 7420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 57360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     THR A   229                                                      
REMARK 465     ARG A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     MET A   232                                                      
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   411                                                      
REMARK 465     ARG A   412                                                      
REMARK 465     LYS A   413                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     PHE A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     TYR A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     HIS A   510                                                      
REMARK 465     ALA A   511                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     GLY A   864                                                      
REMARK 465     GLY A   865                                                      
REMARK 465     LEU A   866                                                      
REMARK 465     LYS A   867                                                      
REMARK 465     GLY A   868                                                      
REMARK 465     ALA A   869                                                      
REMARK 465     LEU A   870                                                      
REMARK 465     GLN A   871                                                      
REMARK 465     PHE A   872                                                      
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   292                                                      
REMARK 465     SER B   293                                                      
REMARK 465     TYR B   294                                                      
REMARK 465     TYR B   295                                                      
REMARK 465     HIS B   296                                                      
REMARK 465     HIS B   297                                                      
REMARK 465     HIS B   298                                                      
REMARK 465     HIS B   299                                                      
REMARK 465     HIS B   300                                                      
REMARK 465     HIS B   301                                                      
REMARK 465     ASP B   302                                                      
REMARK 465     TYR B   303                                                      
REMARK 465     ASP B   304                                                      
REMARK 465     ILE B   305                                                      
REMARK 465     PRO B   306                                                      
REMARK 465     THR B   307                                                      
REMARK 465     THR B   308                                                      
REMARK 465     GLU B   309                                                      
REMARK 465     ASN B   310                                                      
REMARK 465     LEU B   311                                                      
REMARK 465     TYR B   312                                                      
REMARK 465     PHE B   313                                                      
REMARK 465     GLN B   314                                                      
REMARK 465     SER B   315                                                      
REMARK 465     ILE B   316                                                      
REMARK 465     ALA B   317                                                      
REMARK 465     ALA B   318                                                      
REMARK 465     ASN B   319                                                      
REMARK 465     ASN B   320                                                      
REMARK 465     GLY B   321                                                      
REMARK 465     GLY B   599                                                      
REMARK 465     ASN B   600                                                      
REMARK 465     GLU B   601                                                      
REMARK 465     ASN B   602                                                      
REMARK 465     THR B   603                                                      
REMARK 465     GLU B   604                                                      
REMARK 465     ASP B   605                                                      
REMARK 465     GLN B   606                                                      
REMARK 465     TYR B   607                                                      
REMARK 465     SER B   608                                                      
REMARK 465     LEU B   609                                                      
REMARK 465     VAL B   610                                                      
REMARK 465     GLU B   611                                                      
REMARK 465     ASP B   612                                                      
REMARK 465     ASP B   613                                                      
REMARK 465     GLU B   614                                                      
REMARK 465     ASP B   615                                                      
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  54    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A  59    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 321    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 729    CG   CD   CE   NZ                                   
REMARK 470     LYS A 863    CG   CD   CE   NZ                                   
REMARK 470     ILE A1058    CG1  CG2  CD1                                       
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    ASP A    64     O    HOH A  1347              2.08            
REMARK 500   O    HIS A   940     NZ   LYS A   943              2.16            
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    LEU A  49      -63.88    -93.90                                   
REMARK 500    PRO A 159       32.87    -97.11                                   
REMARK 500    LYS A 187       34.31     37.71                                   
REMARK 500    LEU A 234     -168.56   -128.28                                   
REMARK 500    LEU A 239      -10.73    -43.34                                   
REMARK 500    GLN A 247      -53.73   -135.37                                   
REMARK 500    LEU A 293      -60.81    -94.52                                   
REMARK 500    SER A 323       83.09     54.22                                   
REMARK 500    LEU A 339      -79.17    -89.85                                   
REMARK 500    SER A 481       -1.46     77.63                                   
REMARK 500    ARG A 516      -11.90     90.26                                   
REMARK 500    LEU A 793      -71.18   -126.74                                   
REMARK 500    ASP A 939       72.35     55.95                                   
REMARK 500    LYS A 944       -5.84     67.46                                   
REMARK 500    THR A1052     -147.55     55.01                                   
REMARK 500    THR A1053     -175.09   -176.14                                   
REMARK 500    LYS B 587       -2.89     71.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X6K A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 702                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4L1B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF P110ALPHA COMPLEXED WITH NISH2 OF P85ALPHA      
REMARK 900 RELATED ID: 4L2Y   RELATED DB: PDB                                   
DBREF  4L23 A    1  1068  UNP    P42336   PK3CA_HUMAN      1   1068             
DBREF  4L23 B  318   615  UNP    P27986   P85A_HUMAN     318    615             
SEQADV 4L23 MET B  292  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 SER B  293  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 TYR B  294  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 TYR B  295  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 HIS B  296  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 HIS B  297  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 HIS B  298  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 HIS B  299  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 HIS B  300  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 HIS B  301  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 ASP B  302  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 TYR B  303  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 ASP B  304  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 ILE B  305  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 PRO B  306  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 THR B  307  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 THR B  308  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 GLU B  309  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 ASN B  310  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 LEU B  311  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 TYR B  312  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 PHE B  313  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 GLN B  314  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 SER B  315  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 ILE B  316  UNP  P27986              EXPRESSION TAG                 
SEQADV 4L23 ALA B  317  UNP  P27986              EXPRESSION TAG                 
SEQRES   1 A 1068  MET PRO PRO ARG PRO SER SER GLY GLU LEU TRP GLY ILE          
SEQRES   2 A 1068  HIS LEU MET PRO PRO ARG ILE LEU VAL GLU CYS LEU LEU          
SEQRES   3 A 1068  PRO ASN GLY MET ILE VAL THR LEU GLU CYS LEU ARG GLU          
SEQRES   4 A 1068  ALA THR LEU ILE THR ILE LYS HIS GLU LEU PHE LYS GLU          
SEQRES   5 A 1068  ALA ARG LYS TYR PRO LEU HIS GLN LEU LEU GLN ASP GLU          
SEQRES   6 A 1068  SER SER TYR ILE PHE VAL SER VAL THR GLN GLU ALA GLU          
SEQRES   7 A 1068  ARG GLU GLU PHE PHE ASP GLU THR ARG ARG LEU CYS ASP          
SEQRES   8 A 1068  LEU ARG LEU PHE GLN PRO PHE LEU LYS VAL ILE GLU PRO          
SEQRES   9 A 1068  VAL GLY ASN ARG GLU GLU LYS ILE LEU ASN ARG GLU ILE          
SEQRES  10 A 1068  GLY PHE ALA ILE GLY MET PRO VAL CYS GLU PHE ASP MET          
SEQRES  11 A 1068  VAL LYS ASP PRO GLU VAL GLN ASP PHE ARG ARG ASN ILE          
SEQRES  12 A 1068  LEU ASN VAL CYS LYS GLU ALA VAL ASP LEU ARG ASP LEU          
SEQRES  13 A 1068  ASN SER PRO HIS SER ARG ALA MET TYR VAL TYR PRO PRO          
SEQRES  14 A 1068  ASN VAL GLU SER SER PRO GLU LEU PRO LYS HIS ILE TYR          
SEQRES  15 A 1068  ASN LYS LEU ASP LYS GLY GLN ILE ILE VAL VAL ILE TRP          
SEQRES  16 A 1068  VAL ILE VAL SER PRO ASN ASN ASP LYS GLN LYS TYR THR          
SEQRES  17 A 1068  LEU LYS ILE ASN HIS ASP CYS VAL PRO GLU GLN VAL ILE          
SEQRES  18 A 1068  ALA GLU ALA ILE ARG LYS LYS THR ARG SER MET LEU LEU          
SEQRES  19 A 1068  SER SER GLU GLN LEU LYS LEU CYS VAL LEU GLU TYR GLN          
SEQRES  20 A 1068  GLY LYS TYR ILE LEU LYS VAL CYS GLY CYS ASP GLU TYR          
SEQRES  21 A 1068  PHE LEU GLU LYS TYR PRO LEU SER GLN TYR LYS TYR ILE          
SEQRES  22 A 1068  ARG SER CYS ILE MET LEU GLY ARG MET PRO ASN LEU MET          
SEQRES  23 A 1068  LEU MET ALA LYS GLU SER LEU TYR SER GLN LEU PRO MET          
SEQRES  24 A 1068  ASP CYS PHE THR MET PRO SER TYR SER ARG ARG ILE SER          
SEQRES  25 A 1068  THR ALA THR PRO TYR MET ASN GLY GLU THR SER THR LYS          
SEQRES  26 A 1068  SER LEU TRP VAL ILE ASN SER ALA LEU ARG ILE LYS ILE          
SEQRES  27 A 1068  LEU CYS ALA THR TYR VAL ASN VAL ASN ILE ARG ASP ILE          
SEQRES  28 A 1068  ASP LYS ILE TYR VAL ARG THR GLY ILE TYR HIS GLY GLY          
SEQRES  29 A 1068  GLU PRO LEU CYS ASP ASN VAL ASN THR GLN ARG VAL PRO          
SEQRES  30 A 1068  CYS SER ASN PRO ARG TRP ASN GLU TRP LEU ASN TYR ASP          
SEQRES  31 A 1068  ILE TYR ILE PRO ASP LEU PRO ARG ALA ALA ARG LEU CYS          
SEQRES  32 A 1068  LEU SER ILE CYS SER VAL LYS GLY ARG LYS GLY ALA LYS          
SEQRES  33 A 1068  GLU GLU HIS CYS PRO LEU ALA TRP GLY ASN ILE ASN LEU          
SEQRES  34 A 1068  PHE ASP TYR THR ASP THR LEU VAL SER GLY LYS MET ALA          
SEQRES  35 A 1068  LEU ASN LEU TRP PRO VAL PRO HIS GLY LEU GLU ASP LEU          
SEQRES  36 A 1068  LEU ASN PRO ILE GLY VAL THR GLY SER ASN PRO ASN LYS          
SEQRES  37 A 1068  GLU THR PRO CYS LEU GLU LEU GLU PHE ASP TRP PHE SER          
SEQRES  38 A 1068  SER VAL VAL LYS PHE PRO ASP MET SER VAL ILE GLU GLU          
SEQRES  39 A 1068  HIS ALA ASN TRP SER VAL SER ARG GLU ALA GLY PHE SER          
SEQRES  40 A 1068  TYR SER HIS ALA GLY LEU SER ASN ARG LEU ALA ARG ASP          
SEQRES  41 A 1068  ASN GLU LEU ARG GLU ASN ASP LYS GLU GLN LEU LYS ALA          
SEQRES  42 A 1068  ILE SER THR ARG ASP PRO LEU SER GLU ILE THR GLU GLN          
SEQRES  43 A 1068  GLU LYS ASP PHE LEU TRP SER HIS ARG HIS TYR CYS VAL          
SEQRES  44 A 1068  THR ILE PRO GLU ILE LEU PRO LYS LEU LEU LEU SER VAL          
SEQRES  45 A 1068  LYS TRP ASN SER ARG ASP GLU VAL ALA GLN MET TYR CYS          
SEQRES  46 A 1068  LEU VAL LYS ASP TRP PRO PRO ILE LYS PRO GLU GLN ALA          
SEQRES  47 A 1068  MET GLU LEU LEU ASP CYS ASN TYR PRO ASP PRO MET VAL          
SEQRES  48 A 1068  ARG GLY PHE ALA VAL ARG CYS LEU GLU LYS TYR LEU THR          
SEQRES  49 A 1068  ASP ASP LYS LEU SER GLN TYR LEU ILE GLN LEU VAL GLN          
SEQRES  50 A 1068  VAL LEU LYS TYR GLU GLN TYR LEU ASP ASN LEU LEU VAL          
SEQRES  51 A 1068  ARG PHE LEU LEU LYS LYS ALA LEU THR ASN GLN ARG ILE          
SEQRES  52 A 1068  GLY HIS PHE PHE PHE TRP HIS LEU LYS SER GLU MET HIS          
SEQRES  53 A 1068  ASN LYS THR VAL SER GLN ARG PHE GLY LEU LEU LEU GLU          
SEQRES  54 A 1068  SER TYR CYS ARG ALA CYS GLY MET TYR LEU LYS HIS LEU          
SEQRES  55 A 1068  ASN ARG GLN VAL GLU ALA MET GLU LYS LEU ILE ASN LEU          
SEQRES  56 A 1068  THR ASP ILE LEU LYS GLN GLU LYS LYS ASP GLU THR GLN          
SEQRES  57 A 1068  LYS VAL GLN MET LYS PHE LEU VAL GLU GLN MET ARG ARG          
SEQRES  58 A 1068  PRO ASP PHE MET ASP ALA LEU GLN GLY PHE LEU SER PRO          
SEQRES  59 A 1068  LEU ASN PRO ALA HIS GLN LEU GLY ASN LEU ARG LEU GLU          
SEQRES  60 A 1068  GLU CYS ARG ILE MET SER SER ALA LYS ARG PRO LEU TRP          
SEQRES  61 A 1068  LEU ASN TRP GLU ASN PRO ASP ILE MET SER GLU LEU LEU          
SEQRES  62 A 1068  PHE GLN ASN ASN GLU ILE ILE PHE LYS ASN GLY ASP ASP          
SEQRES  63 A 1068  LEU ARG GLN ASP MET LEU THR LEU GLN ILE ILE ARG ILE          
SEQRES  64 A 1068  MET GLU ASN ILE TRP GLN ASN GLN GLY LEU ASP LEU ARG          
SEQRES  65 A 1068  MET LEU PRO TYR GLY CYS LEU SER ILE GLY ASP CYS VAL          
SEQRES  66 A 1068  GLY LEU ILE GLU VAL VAL ARG ASN SER HIS THR ILE MET          
SEQRES  67 A 1068  GLN ILE GLN CYS LYS GLY GLY LEU LYS GLY ALA LEU GLN          
SEQRES  68 A 1068  PHE ASN SER HIS THR LEU HIS GLN TRP LEU LYS ASP LYS          
SEQRES  69 A 1068  ASN LYS GLY GLU ILE TYR ASP ALA ALA ILE ASP LEU PHE          
SEQRES  70 A 1068  THR ARG SER CYS ALA GLY TYR CYS VAL ALA THR PHE ILE          
SEQRES  71 A 1068  LEU GLY ILE GLY ASP ARG HIS ASN SER ASN ILE MET VAL          
SEQRES  72 A 1068  LYS ASP ASP GLY GLN LEU PHE HIS ILE ASP PHE GLY HIS          
SEQRES  73 A 1068  PHE LEU ASP HIS LYS LYS LYS LYS PHE GLY TYR LYS ARG          
SEQRES  74 A 1068  GLU ARG VAL PRO PHE VAL LEU THR GLN ASP PHE LEU ILE          
SEQRES  75 A 1068  VAL ILE SER LYS GLY ALA GLN GLU CYS THR LYS THR ARG          
SEQRES  76 A 1068  GLU PHE GLU ARG PHE GLN GLU MET CYS TYR LYS ALA TYR          
SEQRES  77 A 1068  LEU ALA ILE ARG GLN HIS ALA ASN LEU PHE ILE ASN LEU          
SEQRES  78 A 1068  PHE SER MET MET LEU GLY SER GLY MET PRO GLU LEU GLN          
SEQRES  79 A 1068  SER PHE ASP ASP ILE ALA TYR ILE ARG LYS THR LEU ALA          
SEQRES  80 A 1068  LEU ASP LYS THR GLU GLN GLU ALA LEU GLU TYR PHE MET          
SEQRES  81 A 1068  LYS GLN MET ASN ASP ALA HIS HIS GLY GLY TRP THR THR          
SEQRES  82 A 1068  LYS MET ASP TRP ILE PHE HIS THR ILE LYS GLN HIS ALA          
SEQRES  83 A 1068  LEU ASN                                                      
SEQRES   1 B  324  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 B  324  ILE PRO THR THR GLU ASN LEU TYR PHE GLN SER ILE ALA          
SEQRES   3 B  324  ALA ASN ASN GLY MET ASN ASN ASN MET SER LEU GLN ASP          
SEQRES   4 B  324  ALA GLU TRP TYR TRP GLY ASP ILE SER ARG GLU GLU VAL          
SEQRES   5 B  324  ASN GLU LYS LEU ARG ASP THR ALA ASP GLY THR PHE LEU          
SEQRES   6 B  324  VAL ARG ASP ALA SER THR LYS MET HIS GLY ASP TYR THR          
SEQRES   7 B  324  LEU THR LEU ARG LYS GLY GLY ASN ASN LYS LEU ILE LYS          
SEQRES   8 B  324  ILE PHE HIS ARG ASP GLY LYS TYR GLY PHE SER ASP PRO          
SEQRES   9 B  324  LEU THR PHE SER SER VAL VAL GLU LEU ILE ASN HIS TYR          
SEQRES  10 B  324  ARG ASN GLU SER LEU ALA GLN TYR ASN PRO LYS LEU ASP          
SEQRES  11 B  324  VAL LYS LEU LEU TYR PRO VAL SER LYS TYR GLN GLN ASP          
SEQRES  12 B  324  GLN VAL VAL LYS GLU ASP ASN ILE GLU ALA VAL GLY LYS          
SEQRES  13 B  324  LYS LEU HIS GLU TYR ASN THR GLN PHE GLN GLU LYS SER          
SEQRES  14 B  324  ARG GLU TYR ASP ARG LEU TYR GLU GLU TYR THR ARG THR          
SEQRES  15 B  324  SER GLN GLU ILE GLN MET LYS ARG THR ALA ILE GLU ALA          
SEQRES  16 B  324  PHE ASN GLU THR ILE LYS ILE PHE GLU GLU GLN CYS GLN          
SEQRES  17 B  324  THR GLN GLU ARG TYR SER LYS GLU TYR ILE GLU LYS PHE          
SEQRES  18 B  324  LYS ARG GLU GLY ASN GLU LYS GLU ILE GLN ARG ILE MET          
SEQRES  19 B  324  HIS ASN TYR ASP LYS LEU LYS SER ARG ILE SER GLU ILE          
SEQRES  20 B  324  ILE ASP SER ARG ARG ARG LEU GLU GLU ASP LEU LYS LYS          
SEQRES  21 B  324  GLN ALA ALA GLU TYR ARG GLU ILE ASP LYS ARG MET ASN          
SEQRES  22 B  324  SER ILE LYS PRO ASP LEU ILE GLN LEU ARG LYS THR ARG          
SEQRES  23 B  324  ASP GLN TYR LEU MET TRP LEU THR GLN LYS GLY VAL ARG          
SEQRES  24 B  324  GLN LYS LYS LEU ASN GLU TRP LEU GLY ASN GLU ASN THR          
SEQRES  25 B  324  GLU ASP GLN TYR SER LEU VAL GLU ASP ASP GLU ASP              
HET    X6K  A1101      26                                                       
HET    SO4  A1102       5                                                       
HET    SO4  B 701       5                                                       
HET    GOL  B 702       6                                                       
HETNAM     X6K 3-(4-MORPHOLIN-4-YLPYRIDO[3',2':4,5]FURO[3,2-                    
HETNAM   2 X6K  D]PYRIMIDIN-2-YL)PHENOL                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     X6K PI-103                                                           
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  X6K    C19 H16 N4 O3                                                
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7  HOH   *252(H2 O)                                                    
HELIX    1   1 THR A   41  ARG A   54  1                                  14    
HELIX    2   2 ASP A   64  TYR A   68  5                                   5    
HELIX    3   3 ARG A   88  LEU A   92  5                                   5    
HELIX    4   4 ASN A  107  GLY A  122  1                                  16    
HELIX    5   5 VAL A  125  VAL A  131  1                                   7    
HELIX    6   6 ASP A  133  ILE A  143  1                                  11    
HELIX    7   7 ILE A  143  ARG A  154  1                                  12    
HELIX    8   8 PRO A  159  TYR A  167  1                                   9    
HELIX    9   9 PRO A  178  ASN A  183  1                                   6    
HELIX   10  10 VAL A  216  LYS A  227  1                                  12    
HELIX   11  11 LEU A  239  TYR A  246  1                                   8    
HELIX   12  12 PRO A  266  GLN A  269  5                                   4    
HELIX   13  13 TYR A  270  LEU A  279  1                                  10    
HELIX   14  14 LYS A  290  SER A  295  1                                   6    
HELIX   15  15 TRP A  328  ILE A  330  5                                   3    
HELIX   16  16 PRO A  394  LEU A  396  5                                   3    
HELIX   17  17 ASP A  488  GLU A  503  1                                  16    
HELIX   18  18 ARG A  516  ASN A  521  1                                   6    
HELIX   19  19 ARG A  524  SER A  535  1                                  12    
HELIX   20  20 THR A  544  HIS A  554  1                                  11    
HELIX   21  21 TYR A  557  GLU A  563  5                                   7    
HELIX   22  22 ILE A  564  VAL A  572  1                                   9    
HELIX   23  23 SER A  576  TRP A  590  1                                  15    
HELIX   24  24 LYS A  594  MET A  599  1                                   6    
HELIX   25  25 GLU A  600  ASP A  603  5                                   4    
HELIX   26  26 ASP A  608  LEU A  623  1                                  16    
HELIX   27  27 THR A  624  LEU A  639  1                                  16    
HELIX   28  28 ASN A  647  ASN A  660  1                                  14    
HELIX   29  29 ASN A  660  SER A  673  1                                  14    
HELIX   30  30 VAL A  680  CYS A  695  1                                  16    
HELIX   31  31 MET A  697  GLU A  722  1                                  26    
HELIX   32  32 THR A  727  ARG A  740  1                                  14    
HELIX   33  33 ARG A  741  GLN A  749  1                                   9    
HELIX   34  34 ARG A  765  CYS A  769  5                                   5    
HELIX   35  35 MET A  789  LEU A  793  5                                   5    
HELIX   36  36 LEU A  807  ASN A  826  1                                  20    
HELIX   37  37 ILE A  857  CYS A  862  1                                   6    
HELIX   38  38 HIS A  875  LYS A  886  1                                  12    
HELIX   39  39 ILE A  889  GLY A  912  1                                  24    
HELIX   40  40 THR A  957  SER A  965  1                                   9    
HELIX   41  41 THR A  974  HIS A  994  1                                  21    
HELIX   42  42 HIS A  994  MET A 1004  1                                  11    
HELIX   43  43 SER A 1015  ALA A 1020  1                                   6    
HELIX   44  44 ALA A 1020  LEU A 1026  1                                   7    
HELIX   45  45 THR A 1031  HIS A 1047  1                                  17    
HELIX   46  46 MET B  322  MET B  326  5                                   5    
HELIX   47  47 SER B  327  ALA B  331  5                                   5    
HELIX   48  48 SER B  339  ARG B  348  1                                  10    
HELIX   49  49 SER B  400  GLU B  411  1                                  12    
HELIX   50  50 TYR B  431  VAL B  437  1                                   7    
HELIX   51  51 ASN B  441  LYS B  513  1                                  73    
HELIX   52  52 GLU B  520  GLN B  586  1                                  67    
HELIX   53  53 ARG B  590  LEU B  598  1                                   9    
SHEET    1   A 2 ARG A  19  LEU A  21  0                                        
SHEET    2   A 2 GLU A  35  LEU A  37 -1  O  CYS A  36   N  ILE A  20           
SHEET    1   B 5 ILE A  31  VAL A  32  0                                        
SHEET    2   B 5 GLU A  23  LEU A  25 -1  N  CYS A  24   O  VAL A  32           
SHEET    3   B 5 PHE A  98  ILE A 102  1  O  LEU A  99   N  LEU A  25           
SHEET    4   B 5 ILE A  69  VAL A  73 -1  N  ILE A  69   O  ILE A 102           
SHEET    5   B 5 ARG A  79  PHE A  82 -1  O  PHE A  82   N  PHE A  70           
SHEET    1   C 5 LYS A 204  ASN A 212  0                                        
SHEET    2   C 5 GLN A 189  ILE A 197 -1  N  ILE A 194   O  TYR A 207           
SHEET    3   C 5 ASN A 284  ALA A 289  1  O  LEU A 285   N  VAL A 193           
SHEET    4   C 5 TYR A 250  VAL A 254 -1  N  LYS A 253   O  MET A 286           
SHEET    5   C 5 TYR A 260  PHE A 261 -1  O  PHE A 261   N  LEU A 252           
SHEET    1   D 2 LYS A 325  SER A 326  0                                        
SHEET    2   D 2 VAL A 484  LYS A 485  1  O  LYS A 485   N  LYS A 325           
SHEET    1   E 4 ARG A 382  TYR A 392  0                                        
SHEET    2   E 4 ALA A 333  ALA A 341 -1  N  ILE A 336   O  LEU A 387           
SHEET    3   E 4 CYS A 472  PHE A 477 -1  O  GLU A 474   N  CYS A 340           
SHEET    4   E 4 GLY A 439  ASN A 444 -1  N  LEU A 443   O  LEU A 473           
SHEET    1   F 4 GLU A 365  PRO A 366  0                                        
SHEET    2   F 4 LYS A 353  HIS A 362 -1  N  HIS A 362   O  GLU A 365           
SHEET    3   F 4 ARG A 401  VAL A 409 -1  O  CYS A 407   N  TYR A 355           
SHEET    4   F 4 HIS A 419  ASN A 428 -1  O  LEU A 422   N  ILE A 406           
SHEET    1   G 2 PHE A 751  LEU A 752  0                                        
SHEET    2   G 2 GLN A 760  LEU A 761 -1  O  LEU A 761   N  PHE A 751           
SHEET    1   H 5 ARG A 770  ILE A 771  0                                        
SHEET    2   H 5 LEU A 779  GLU A 784 -1  O  TRP A 780   N  ARG A 770           
SHEET    3   H 5 ASN A 796  ASN A 803 -1  O  PHE A 801   N  LEU A 779           
SHEET    4   H 5 VAL A 845  GLU A 849 -1  O  ILE A 848   N  ILE A 800           
SHEET    5   H 5 CYS A 838  GLY A 842 -1  N  ILE A 841   O  VAL A 845           
SHEET    1   I 3 SER A 854  THR A 856  0                                        
SHEET    2   I 3 ILE A 921  LYS A 924 -1  O  VAL A 923   N  HIS A 855           
SHEET    3   I 3 LEU A 929  HIS A 931 -1  O  PHE A 930   N  MET A 922           
SHEET    1   J 5 LYS B 389  GLY B 391  0                                        
SHEET    2   J 5 ASN B 377  ARG B 386 -1  N  PHE B 384   O  GLY B 391           
SHEET    3   J 5 TYR B 368  LYS B 374 -1  N  LEU B 370   O  ILE B 381           
SHEET    4   J 5 THR B 354  ASP B 359 -1  N  ARG B 358   O  THR B 369           
SHEET    5   J 5 TYR B 426  PRO B 427  1  O  TYR B 426   N  PHE B 355           
CISPEP   1 SER A  158    PRO A  159          0        -4.82                     
CISPEP   2 ASP B  394    PRO B  395          0        -0.78                     
SITE     1 AC1 13 MET A 772  ASP A 810  TYR A 836  ILE A 848                    
SITE     2 AC1 13 GLU A 849  VAL A 850  VAL A 851  SER A 854                    
SITE     3 AC1 13 MET A 922  ILE A 932  ASP A 933  ASP B 387                    
SITE     4 AC1 13 HOH B 803                                                     
SITE     1 AC2  3 VAL A 131  LYS A 132  ASP A 133                               
SITE     1 AC3  8 ARG A 537  ARG B 340  ARG B 358  ALA B 360                    
SITE     2 AC3  8 SER B 361  MET B 364  THR B 369  LYS B 382                    
SITE     1 AC4  6 ASN A 467  GLU A 469  ARG B 481  TYR B 556                    
SITE     2 AC4  6 HOH B 810  HOH B 819                                          
CRYST1   71.628  136.377  151.487  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      0.013961  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007333  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006601        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system