GenomeNet

Database: PDB
Entry: 5UBR
LinkDB: 5UBR
Original site: 5UBR 
HEADER    TRANSFERASE/TRANSFERASE REGULATOR       21-DEC-16   5UBR              
TITLE     CRYSTAL STRUCTURE OF PI3K ALPHA IN COMPLEX WITH A 7-(3-(PIPERAZIN-1-  
TITLE    2 YL)PHENYL)PYRROLO[2,1-F][1,2,4] TRIAZIN-4-AMINE DERIVIATINE          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT ALPHA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PTDINS-3-KINASE SUBUNIT ALPHA,PHOSPHATIDYLINOSITOL 4,5-     
COMPND   6 BISPHOSPHATE 3-KINASE 110 KDA CATALYTIC SUBUNIT ALPHA,P110ALPHA,     
COMPND   7 PHOSPHOINOSITIDE-3-KINASE CATALYTIC ALPHA POLYPEPTIDE,               
COMPND   8 SERINE/THREONINE PROTEIN KINASE PIK3CA;                              
COMPND   9 EC: 2.7.1.153;                                                       
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PIK3CA;                                                        
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469                                       
KEYWDS    LIPID KINASE, INHIBITOR, PI3K ALPHA, TRANSFERASE-TRANSFERASE          
KEYWDS   2 INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE REGULATOR COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.SACK                                                              
REVDAT   2   22-FEB-17 5UBR    1       JRNL                                     
REVDAT   1   08-FEB-17 5UBR    0                                                
JRNL        AUTH   L.Y.QIN,Z.RUAN,R.J.CHERNEY,T.G.DHAR,J.NEELS,C.A.WEIGELT,     
JRNL        AUTH 2 J.S.SACK,A.S.SRIVASTAVA,L.A.CORNELIUS,J.A.TINO,K.STEFANSKI,  
JRNL        AUTH 3 X.GU,J.XIE,V.SUSULIC,X.YANG,M.YARDE-CHINN,S.SKALA,R.BOSNIUS, 
JRNL        AUTH 4 C.GOLDSTEIN,P.DAVIES,S.RUEPP,L.SALTER-CID,R.S.BHIDE,M.A.POSS 
JRNL        TITL   DISCOVERY OF                                                 
JRNL        TITL 2 7-(3-(PIPERAZIN-1-YL)PHENYL)PYRROLO[2,1-F][1,2,              
JRNL        TITL 3 4]TRIAZIN-4-AMINE DERIVATIVES AS HIGHLY POTENT AND SELECTIVE 
JRNL        TITL 4 PI3K DELTA INHIBITORS.                                       
JRNL        REF    BIOORG. MED. CHEM. LETT.      V.  27   855 2017              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   28108251                                                     
JRNL        DOI    10.1016/J.BMCL.2017.01.016                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 44406                          
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)  : 0.201                          
REMARK   3   R VALUE            (WORKING SET)  : 0.200                          
REMARK   3   FREE R VALUE                      : 0.246                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 2.600                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1156                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.40                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.46                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.33                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3277                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2320                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3197                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2301                   
REMARK   3   BIN FREE R VALUE                        : 0.3078                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 2.44                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : NULL                     
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6942                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 158                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 65.91                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.59990                                             
REMARK   3    B22 (A**2) : -11.38160                                            
REMARK   3    B33 (A**2) : 14.98150                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.330               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.336               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.238               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.335               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.240               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7339   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9938   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2581   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 195    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1069   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7339   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 936    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 8326   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.08                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.70                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.33                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UBR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000225613.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45019                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 97.880                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL, VAPOR DIFFUSION, TEMPERATURE       
REMARK 280  293K                                                                
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       29.32250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.17100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.40250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.17100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.32250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.40250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 39390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A   233                                                      
REMARK 465     LEU A   234                                                      
REMARK 465     SER A   235                                                      
REMARK 465     SER A   236                                                      
REMARK 465     GLU A   237                                                      
REMARK 465     GLN A   238                                                      
REMARK 465     LEU A   239                                                      
REMARK 465     LYS A   240                                                      
REMARK 465     LEU A   241                                                      
REMARK 465     CYS A   242                                                      
REMARK 465     VAL A   243                                                      
REMARK 465     LEU A   244                                                      
REMARK 465     GLU A   245                                                      
REMARK 465     TYR A   246                                                      
REMARK 465     GLN A   247                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     ILE A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     THR A   313                                                      
REMARK 465     ALA A   314                                                      
REMARK 465     THR A   315                                                      
REMARK 465     PRO A   316                                                      
REMARK 465     TYR A   317                                                      
REMARK 465     MET A   318                                                      
REMARK 465     ASN A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     THR A   322                                                      
REMARK 465     SER A   323                                                      
REMARK 465     THR A   324                                                      
REMARK 465     ASN A   347                                                      
REMARK 465     ILE A   348                                                      
REMARK 465     ARG A   349                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     ILE A   351                                                      
REMARK 465     ASP A   352                                                      
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     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     LYS A   943                                                      
REMARK 465     LYS A   944                                                      
REMARK 465     PHE A   945                                                      
REMARK 465     GLY A   946                                                      
REMARK 465     TYR A   947                                                      
REMARK 465     LYS A   948                                                      
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     ASN A 107    CG   OD1  ND2                                       
REMARK 470     ARG A 108    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 111    CG   CD   CE   NZ                                   
REMARK 470     ILE A 112    CD1                                                 
REMARK 470     LYS A 132    CG   CD   CE   NZ                                   
REMARK 470     ASN A 157    CG   OD1  ND2                                       
REMARK 470     GLU A 176    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 177    CG   CD1  CD2                                       
REMARK 470     LYS A 179    CG   CD   CE   NZ                                   
REMARK 470     ASN A 183    CG   OD1  ND2                                       
REMARK 470     LYS A 184    CG   CD   CE   NZ                                   
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     ILE A 194    CD1                                                 
REMARK 470     PRO A 200    CG   CD                                             
REMARK 470     ASN A 202    CG   OD1  ND2                                       
REMARK 470     LYS A 204    CE   NZ                                             
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     ILE A 211    CD1                                                 
REMARK 470     ARG A 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 249    CG   CD   CE   NZ                                   
REMARK 470     LYS A 264    CG   CD   CE   NZ                                   
REMARK 470     MET A 278    SD   CE                                             
REMARK 470     ARG A 281    NE   CZ   NH1  NH2                                  
REMARK 470     GLN A 296    CG   CD   OE1  NE2                                  
REMARK 470     MET A 299    CG   SD   CE                                        
REMARK 470     ARG A 309    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 325    CG   CD   CE   NZ                                   
REMARK 470     SER A 326    OG                                                  
REMARK 470     LEU A 327    CG   CD1  CD2                                       
REMARK 470     LYS A 337    NZ                                                  
REMARK 470     LYS A 353    CG   CD   CE   NZ                                   
REMARK 470     THR A 373    OG1  CG2                                            
REMARK 470     ARG A 382    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 384    CG   OD1  ND2                                       
REMARK 470     ILE A 406    CD1                                                 
REMARK 470     GLU A 418    CG   CD   OE1  OE2                                  
REMARK 470     CYS A 420    SG                                                  
REMARK 470     LYS A 440    CG   CD   CE   NZ                                   
REMARK 470     HIS A 450    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 452    CG   CD1  CD2                                       
REMARK 470     GLU A 453    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 459    CD1                                                 
REMARK 470     VAL A 461    CG1  CG2                                            
REMARK 470     LEU A 473    CG   CD1  CD2                                       
REMARK 470     VAL A 484    CG1  CG2                                            
REMARK 470     GLU A 494    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 502    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 519    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 523    CG   CD1  CD2                                       
REMARK 470     ARG A 524    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 528    CE   NZ                                             
REMARK 470     GLU A 529    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 532    CG   CD   CE   NZ                                   
REMARK 470     LEU A 540    CG   CD1  CD2                                       
REMARK 470     GLU A 542    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 543    CD1                                                 
REMARK 470     LYS A 573    CD   CE   NZ                                        
REMARK 470     LYS A 588    CE   NZ                                             
REMARK 470     LYS A 594    CE   NZ                                             
REMARK 470     LYS A 621    CG   CD   CE   NZ                                   
REMARK 470     GLU A 710    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 714    CG   OD1  ND2                                       
REMARK 470     LYS A 724    CG   CD   CE   NZ                                   
REMARK 470     LYS A 729    CD   CE   NZ                                        
REMARK 470     LYS A 733    CG   CD   CE   NZ                                   
REMARK 470     ASP A 743    CG   OD1  OD2                                       
REMARK 470     MET A 745    SD   CE                                             
REMARK 470     ARG A 777    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 852    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 863    CG   CD   CE   NZ                                   
REMARK 470     ASN A 873    CG   OD1  ND2                                       
REMARK 470     GLN A 879    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 882    CE   NZ                                             
REMARK 470     ASP A 883    CG   OD1  OD2                                       
REMARK 470     LYS A 886    CG   CD   CE   NZ                                   
REMARK 470     GLU A 888    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 949    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 966    CD   CE   NZ                                        
REMARK 470     GLN A 969    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 970    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 973    CG   CD   CE   NZ                                   
REMARK 470     ARG A 975    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 978    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 982    CD   OE1  OE2                                       
REMARK 470     LYS A 986    CG   CD   CE   NZ                                   
REMARK 470     LYS A1030    CE   NZ                                             
REMARK 470     GLU A1034    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1037    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1041    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 133      109.00   -167.26                                   
REMARK 500    ASN A 157       61.62   -118.98                                   
REMARK 500    SER A 199      150.48     60.17                                   
REMARK 500    PHE A 261       65.72   -109.63                                   
REMARK 500    LYS A 264       43.45    -64.86                                   
REMARK 500    LEU A 327     -138.09   -155.91                                   
REMARK 500    ASN A 331       82.47    -66.30                                   
REMARK 500    LEU A 339      -78.64    -75.07                                   
REMARK 500    TRP A 383      -50.60   -139.21                                   
REMARK 500    ASN A 384       17.13     47.43                                   
REMARK 500    GLU A 418       62.83   -101.90                                   
REMARK 500    LEU A 422      -62.62    -90.63                                   
REMARK 500    ASP A 434       14.82     80.36                                   
REMARK 500    GLU A 469       51.53   -108.36                                   
REMARK 500    PHE A 480     -163.62   -111.32                                   
REMARK 500    SER A 482     -155.74   -138.24                                   
REMARK 500    PHE A 744      -46.53   -148.51                                   
REMARK 500    ASN A 756       97.84   -162.41                                   
REMARK 500    PRO A 757        0.37    -65.97                                   
REMARK 500    SER A 774      154.21    -48.11                                   
REMARK 500    LEU A 793      -77.55   -111.03                                   
REMARK 500    ASP A 933       91.58     58.86                                   
REMARK 500    LEU A 938     -149.66     57.40                                   
REMARK 500    ASP A 939       37.19    -73.85                                   
REMARK 500    ALA A1027       57.66     38.60                                   
REMARK 500    HIS A1048        2.24     57.74                                   
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 85S A 4000                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UBT   RELATED DB: PDB                                   
DBREF  5UBR A  107  1050  UNP    P42336   PK3CA_HUMAN    107   1050             
SEQRES   1 A  944  ASN ARG GLU GLU LYS ILE LEU ASN ARG GLU ILE GLY PHE          
SEQRES   2 A  944  ALA ILE GLY MET PRO VAL CYS GLU PHE ASP MET VAL LYS          
SEQRES   3 A  944  ASP PRO GLU VAL GLN ASP PHE ARG ARG ASN ILE LEU ASN          
SEQRES   4 A  944  VAL CYS LYS GLU ALA VAL ASP LEU ARG ASP LEU ASN SER          
SEQRES   5 A  944  PRO HIS SER ARG ALA MET TYR VAL TYR PRO PRO ASN VAL          
SEQRES   6 A  944  GLU SER SER PRO GLU LEU PRO LYS HIS ILE TYR ASN LYS          
SEQRES   7 A  944  LEU ASP LYS GLY GLN ILE ILE VAL VAL ILE TRP VAL ILE          
SEQRES   8 A  944  VAL SER PRO ASN ASN ASP LYS GLN LYS TYR THR LEU LYS          
SEQRES   9 A  944  ILE ASN HIS ASP CYS VAL PRO GLU GLN VAL ILE ALA GLU          
SEQRES  10 A  944  ALA ILE ARG LYS LYS THR ARG SER MET LEU LEU SER SER          
SEQRES  11 A  944  GLU GLN LEU LYS LEU CYS VAL LEU GLU TYR GLN GLY LYS          
SEQRES  12 A  944  TYR ILE LEU LYS VAL CYS GLY CYS ASP GLU TYR PHE LEU          
SEQRES  13 A  944  GLU LYS TYR PRO LEU SER GLN TYR LYS TYR ILE ARG SER          
SEQRES  14 A  944  CYS ILE MET LEU GLY ARG MET PRO ASN LEU MET LEU MET          
SEQRES  15 A  944  ALA LYS GLU SER LEU TYR SER GLN LEU PRO MET ASP CYS          
SEQRES  16 A  944  PHE THR MET PRO SER TYR SER ARG ARG ILE SER THR ALA          
SEQRES  17 A  944  THR PRO TYR MET ASN GLY GLU THR SER THR LYS SER LEU          
SEQRES  18 A  944  TRP VAL ILE ASN SER ALA LEU ARG ILE LYS ILE LEU CYS          
SEQRES  19 A  944  ALA THR TYR VAL ASN VAL ASN ILE ARG ASP ILE ASP LYS          
SEQRES  20 A  944  ILE TYR VAL ARG THR GLY ILE TYR HIS GLY GLY GLU PRO          
SEQRES  21 A  944  LEU CYS ASP ASN VAL ASN THR GLN ARG VAL PRO CYS SER          
SEQRES  22 A  944  ASN PRO ARG TRP ASN GLU TRP LEU ASN TYR ASP ILE TYR          
SEQRES  23 A  944  ILE PRO ASP LEU PRO ARG ALA ALA ARG LEU CYS LEU SER          
SEQRES  24 A  944  ILE CYS SER VAL LYS GLY ARG LYS GLY ALA LYS GLU GLU          
SEQRES  25 A  944  HIS CYS PRO LEU ALA TRP GLY ASN ILE ASN LEU PHE ASP          
SEQRES  26 A  944  TYR THR ASP THR LEU VAL SER GLY LYS MET ALA LEU ASN          
SEQRES  27 A  944  LEU TRP PRO VAL PRO HIS GLY LEU GLU ASP LEU LEU ASN          
SEQRES  28 A  944  PRO ILE GLY VAL THR GLY SER ASN PRO ASN LYS GLU THR          
SEQRES  29 A  944  PRO CYS LEU GLU LEU GLU PHE ASP TRP PHE SER SER VAL          
SEQRES  30 A  944  VAL LYS PHE PRO ASP MET SER VAL ILE GLU GLU HIS ALA          
SEQRES  31 A  944  ASN TRP SER VAL SER ARG GLU ALA GLY PHE SER TYR SER          
SEQRES  32 A  944  HIS ALA GLY LEU SER ASN ARG LEU ALA ARG ASP ASN GLU          
SEQRES  33 A  944  LEU ARG GLU ASN ASP LYS GLU GLN LEU LYS ALA ILE SER          
SEQRES  34 A  944  THR ARG ASP PRO LEU SER GLU ILE THR GLU GLN GLU LYS          
SEQRES  35 A  944  ASP PHE LEU TRP SER HIS ARG HIS TYR CYS VAL THR ILE          
SEQRES  36 A  944  PRO GLU ILE LEU PRO LYS LEU LEU LEU SER VAL LYS TRP          
SEQRES  37 A  944  ASN SER ARG ASP GLU VAL ALA GLN MET TYR CYS LEU VAL          
SEQRES  38 A  944  LYS ASP TRP PRO PRO ILE LYS PRO GLU GLN ALA MET GLU          
SEQRES  39 A  944  LEU LEU ASP CYS ASN TYR PRO ASP PRO MET VAL ARG GLY          
SEQRES  40 A  944  PHE ALA VAL ARG CYS LEU GLU LYS TYR LEU THR ASP ASP          
SEQRES  41 A  944  LYS LEU SER GLN TYR LEU ILE GLN LEU VAL GLN VAL LEU          
SEQRES  42 A  944  LYS TYR GLU GLN TYR LEU ASP ASN LEU LEU VAL ARG PHE          
SEQRES  43 A  944  LEU LEU LYS LYS ALA LEU THR ASN GLN ARG ILE GLY HIS          
SEQRES  44 A  944  PHE PHE PHE TRP HIS LEU LYS SER GLU MET HIS ASN LYS          
SEQRES  45 A  944  THR VAL SER GLN ARG PHE GLY LEU LEU LEU GLU SER TYR          
SEQRES  46 A  944  CYS ARG ALA CYS GLY MET TYR LEU LYS HIS LEU ASN ARG          
SEQRES  47 A  944  GLN VAL GLU ALA MET GLU LYS LEU ILE ASN LEU THR ASP          
SEQRES  48 A  944  ILE LEU LYS GLN GLU LYS LYS ASP GLU THR GLN LYS VAL          
SEQRES  49 A  944  GLN MET LYS PHE LEU VAL GLU GLN MET ARG ARG PRO ASP          
SEQRES  50 A  944  PHE MET ASP ALA LEU GLN GLY PHE LEU SER PRO LEU ASN          
SEQRES  51 A  944  PRO ALA HIS GLN LEU GLY ASN LEU ARG LEU GLU GLU CYS          
SEQRES  52 A  944  ARG ILE MET SER SER ALA LYS ARG PRO LEU TRP LEU ASN          
SEQRES  53 A  944  TRP GLU ASN PRO ASP ILE MET SER GLU LEU LEU PHE GLN          
SEQRES  54 A  944  ASN ASN GLU ILE ILE PHE LYS ASN GLY ASP ASP LEU ARG          
SEQRES  55 A  944  GLN ASP MET LEU THR LEU GLN ILE ILE ARG ILE MET GLU          
SEQRES  56 A  944  ASN ILE TRP GLN ASN GLN GLY LEU ASP LEU ARG MET LEU          
SEQRES  57 A  944  PRO TYR GLY CYS LEU SER ILE GLY ASP CYS VAL GLY LEU          
SEQRES  58 A  944  ILE GLU VAL VAL ARG ASN SER HIS THR ILE MET GLN ILE          
SEQRES  59 A  944  GLN CYS LYS GLY GLY LEU LYS GLY ALA LEU GLN PHE ASN          
SEQRES  60 A  944  SER HIS THR LEU HIS GLN TRP LEU LYS ASP LYS ASN LYS          
SEQRES  61 A  944  GLY GLU ILE TYR ASP ALA ALA ILE ASP LEU PHE THR ARG          
SEQRES  62 A  944  SER CYS ALA GLY TYR CYS VAL ALA THR PHE ILE LEU GLY          
SEQRES  63 A  944  ILE GLY ASP ARG HIS ASN SER ASN ILE MET VAL LYS ASP          
SEQRES  64 A  944  ASP GLY GLN LEU PHE HIS ILE ASP PHE GLY HIS PHE LEU          
SEQRES  65 A  944  ASP HIS LYS LYS LYS LYS PHE GLY TYR LYS ARG GLU ARG          
SEQRES  66 A  944  VAL PRO PHE VAL LEU THR GLN ASP PHE LEU ILE VAL ILE          
SEQRES  67 A  944  SER LYS GLY ALA GLN GLU CYS THR LYS THR ARG GLU PHE          
SEQRES  68 A  944  GLU ARG PHE GLN GLU MET CYS TYR LYS ALA TYR LEU ALA          
SEQRES  69 A  944  ILE ARG GLN HIS ALA ASN LEU PHE ILE ASN LEU PHE SER          
SEQRES  70 A  944  MET MET LEU GLY SER GLY MET PRO GLU LEU GLN SER PHE          
SEQRES  71 A  944  ASP ASP ILE ALA TYR ILE ARG LYS THR LEU ALA LEU ASP          
SEQRES  72 A  944  LYS THR GLU GLN GLU ALA LEU GLU TYR PHE MET LYS GLN          
SEQRES  73 A  944  MET ASN ASP ALA HIS HIS GLY GLY                              
HET    85S  A4000      36                                                       
HETNAM     85S 1-[4-(3-{4-AMINO-5-[1-(OXAN-4-YL)-1H-PYRAZOL-5-                  
HETNAM   2 85S  YL]PYRROLO[2,1-F][1,2,4]TRIAZIN-7-YL}PHENYL)PIPERAZIN-          
HETNAM   3 85S  1-YL]ETHAN-1-ONE                                                
FORMUL   2  85S    C26 H30 N8 O2                                                
FORMUL   3  HOH   *158(H2 O)                                                    
HELIX    1 AA1 ASN A  107  GLY A  122  1                                  16    
HELIX    2 AA2 VAL A  125  MET A  130  1                                   6    
HELIX    3 AA3 ASP A  133  ASP A  155  1                                  23    
HELIX    4 AA4 PRO A  159  TYR A  167  1                                   9    
HELIX    5 AA5 PRO A  178  ASN A  183  1                                   6    
HELIX    6 AA6 VAL A  216  ARG A  230  1                                  15    
HELIX    7 AA7 PRO A  266  GLN A  269  5                                   4    
HELIX    8 AA8 TYR A  270  GLY A  280  1                                  11    
HELIX    9 AA9 LYS A  290  SER A  295  1                                   6    
HELIX   10 AB1 PRO A  305  ARG A  309  5                                   5    
HELIX   11 AB2 PRO A  394  LEU A  396  5                                   3    
HELIX   12 AB3 ASP A  488  GLY A  505  1                                  18    
HELIX   13 AB4 SER A  507  GLY A  512  1                                   6    
HELIX   14 AB5 ARG A  524  THR A  536  1                                  13    
HELIX   15 AB6 THR A  544  HIS A  554  1                                  11    
HELIX   16 AB7 TYR A  557  GLU A  563  5                                   7    
HELIX   17 AB8 ILE A  564  SER A  571  1                                   8    
HELIX   18 AB9 SER A  576  ASP A  589  1                                  14    
HELIX   19 AC1 LYS A  594  MET A  599  1                                   6    
HELIX   20 AC2 GLU A  600  ASP A  603  5                                   4    
HELIX   21 AC3 ASP A  608  LEU A  623  1                                  16    
HELIX   22 AC4 THR A  624  TYR A  631  1                                   8    
HELIX   23 AC5 TYR A  631  VAL A  638  1                                   8    
HELIX   24 AC6 LEU A  639  GLU A  642  5                                   4    
HELIX   25 AC7 ASN A  647  LEU A  658  1                                  12    
HELIX   26 AC8 ASN A  660  SER A  673  1                                  14    
HELIX   27 AC9 VAL A  680  CYS A  695  1                                  16    
HELIX   28 AD1 MET A  697  GLU A  722  1                                  26    
HELIX   29 AD2 THR A  727  ARG A  741  1                                  15    
HELIX   30 AD3 MET A  745  GLN A  749  5                                   5    
HELIX   31 AD4 ARG A  765  CYS A  769  5                                   5    
HELIX   32 AD5 MET A  789  LEU A  793  5                                   5    
HELIX   33 AD6 LEU A  807  GLN A  827  1                                  21    
HELIX   34 AD7 ILE A  857  LYS A  863  1                                   7    
HELIX   35 AD8 HIS A  875  ASN A  885  1                                  11    
HELIX   36 AD9 LYS A  886  GLU A  888  5                                   3    
HELIX   37 AE1 ILE A  889  GLY A  912  1                                  24    
HELIX   38 AE2 THR A  957  SER A  965  1                                   9    
HELIX   39 AE3 GLU A  970  LYS A  973  5                                   4    
HELIX   40 AE4 THR A  974  HIS A  994  1                                  21    
HELIX   41 AE5 HIS A  994  MET A 1005  1                                  12    
HELIX   42 AE6 SER A 1015  LEU A 1026  1                                  12    
HELIX   43 AE7 THR A 1031  HIS A 1048  1                                  18    
SHEET    1 AA1 4 ASP A 203  ASN A 212  0                                        
SHEET    2 AA1 4 GLN A 189  VAL A 198 -1  N  VAL A 192   O  LEU A 209           
SHEET    3 AA1 4 ASN A 284  ALA A 289  1  O  LEU A 287   N  TRP A 195           
SHEET    4 AA1 4 TYR A 250  VAL A 254 -1  N  LYS A 253   O  MET A 286           
SHEET    1 AA2 4 ARG A 382  TYR A 392  0                                        
SHEET    2 AA2 4 ALA A 333  THR A 342 -1  N  LEU A 334   O  TYR A 389           
SHEET    3 AA2 4 CYS A 472  PHE A 477 -1  O  GLU A 474   N  CYS A 340           
SHEET    4 AA2 4 GLY A 439  ASN A 444 -1  N  LEU A 443   O  LEU A 473           
SHEET    1 AA3 3 GLU A 365  PRO A 366  0                                        
SHEET    2 AA3 3 ILE A 354  HIS A 362 -1  N  HIS A 362   O  GLU A 365           
SHEET    3 AA3 3 VAL A 371  ASN A 372 -1  O  VAL A 371   N  THR A 358           
SHEET    1 AA4 5 GLU A 365  PRO A 366  0                                        
SHEET    2 AA4 5 ILE A 354  HIS A 362 -1  N  HIS A 362   O  GLU A 365           
SHEET    3 AA4 5 ALA A 400  SER A 408 -1  O  CYS A 407   N  TYR A 355           
SHEET    4 AA4 5 CYS A 420  ASN A 428 -1  O  LEU A 422   N  ILE A 406           
SHEET    5 AA4 5 TRP A 446  PRO A 447 -1  O  TRP A 446   N  TRP A 424           
SHEET    1 AA5 2 PHE A 751  SER A 753  0                                        
SHEET    2 AA5 2 ASN A 756  LEU A 761 -1  O  LEU A 761   N  PHE A 751           
SHEET    1 AA6 5 ARG A 770  ILE A 771  0                                        
SHEET    2 AA6 5 LEU A 779  GLU A 784 -1  O  TRP A 780   N  ARG A 770           
SHEET    3 AA6 5 ASN A 796  ASN A 803 -1  O  ILE A 799   N  LEU A 781           
SHEET    4 AA6 5 VAL A 845  GLU A 849 -1  O  ILE A 848   N  ILE A 800           
SHEET    5 AA6 5 CYS A 838  GLY A 842 -1  N  LEU A 839   O  LEU A 847           
SHEET    1 AA7 3 SER A 854  THR A 856  0                                        
SHEET    2 AA7 3 ILE A 921  LYS A 924 -1  O  VAL A 923   N  HIS A 855           
SHEET    3 AA7 3 LEU A 929  HIS A 931 -1  O  PHE A 930   N  MET A 922           
CISPEP   1 SER A  158    PRO A  159          0         3.85                     
SITE     1 AC1 12 ARG A 770  MET A 772  SER A 774  PRO A 778                    
SITE     2 AC1 12 TRP A 780  LYS A 802  TYR A 836  GLU A 849                    
SITE     3 AC1 12 VAL A 850  VAL A 851  GLN A 859  ILE A 932                    
CRYST1   58.645  134.805  142.342  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      0.017052  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007418  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007025        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system