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Database: PDB
Entry: 3PYY
LinkDB: 3PYY
Original site: 3PYY 
HEADER    TRANSFERASE                             13-DEC-10   3PYY              
TITLE     DISCOVERY AND CHARACTERIZATION OF A CELL-PERMEABLE, SMALL-MOLECULE C- 
TITLE    2 ABL KINASE ACTIVATOR THAT BINDS TO THE MYRISTOYL BINDING SITE        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: V-ABL ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG 1     
COMPND   3 ISOFORM B VARIANT;                                                   
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 266-549;                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    TYROSINE KINASE, TRANSFERASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.YANG,N.CAMPOBASSO,M.P.BIJU,K.FISHER,X.Q.PAN,J.COTTOM,S.GALBRAITH,   
AUTHOR   2 T.HO,H.ZHANG,X.HONG,P.WARD,G.HOFMANN,B.SIEGFRIED                     
REVDAT   2   24-JAN-18 3PYY    1       AUTHOR                                   
REVDAT   1   09-MAR-11 3PYY    0                                                
JRNL        AUTH   J.YANG,N.CAMPOBASSO,M.P.BIJU,K.FISHER,X.Q.PAN,J.COTTOM,      
JRNL        AUTH 2 S.GALBRAITH,T.HO,H.ZHANG,X.HONG,P.WARD,G.HOFMANN,            
JRNL        AUTH 3 B.SIEGFRIED,F.ZAPPACOSTA,Y.WASHIO,P.CAO,J.QU,S.BERTRAND,     
JRNL        AUTH 4 D.Y.WANG,M.S.HEAD,H.LI,S.MOORES,Z.LAI,K.JOHANSON,G.BURTON,   
JRNL        AUTH 5 C.ERICKSON-MILLER,G.SIMPSON,P.TUMMINO,R.A.COPELAND,A.OLIFF   
JRNL        TITL   DISCOVERY AND CHARACTERIZATION OF A CELL-PERMEABLE,          
JRNL        TITL 2 SMALL-MOLECULE C-ABL KINASE ACTIVATOR THAT BINDS TO THE      
JRNL        TITL 3 MYRISTOYL BINDING SITE.                                      
JRNL        REF    CHEM.BIOL.                    V.  18   177 2011              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   21338916                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2010.12.013                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6_289)                      
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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.030                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 66950                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1922                            
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 29.9672 -  4.4596    0.99     5110   151  0.1848 0.1932        
REMARK   3     2  4.4596 -  3.5416    0.99     4940   146  0.1655 0.1848        
REMARK   3     3  3.5416 -  3.0944    0.99     4900   144  0.1927 0.1797        
REMARK   3     4  3.0944 -  2.8117    0.99     4873   146  0.2036 0.2369        
REMARK   3     5  2.8117 -  2.6103    0.98     4808   142  0.1900 0.1908        
REMARK   3     6  2.6103 -  2.4565    0.98     4772   140  0.1910 0.2200        
REMARK   3     7  2.4565 -  2.3335    0.97     4728   140  0.1871 0.2139        
REMARK   3     8  2.3335 -  2.2320    0.96     4692   137  0.1882 0.2200        
REMARK   3     9  2.2320 -  2.1461    0.95     4604   134  0.1817 0.2206        
REMARK   3    10  2.1461 -  2.0720    0.95     4598   138  0.1890 0.2053        
REMARK   3    11  2.0720 -  2.0073    0.93     4482   132  0.1976 0.2200        
REMARK   3    12  2.0073 -  1.9499    0.91     4400   131  0.2040 0.2441        
REMARK   3    13  1.9499 -  1.8986    0.86     4149   122  0.2215 0.2460        
REMARK   3    14  1.8986 -  1.8500    0.82     3972   119  0.2349 0.2445        
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              : 0.40                                          
REMARK   3   B_SOL              : 60.01                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.37800                                              
REMARK   3    B22 (A**2) : 3.61700                                              
REMARK   3    B33 (A**2) : -5.99500                                             
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  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      :  0.007           4528                                  
REMARK   3   ANGLE     :  1.076           6125                                  
REMARK   3   CHIRALITY :  0.071            631                                  
REMARK   3   PLANARITY :  0.004            803                                  
REMARK   3   DIHEDRAL  : 15.836           1620                                  
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 3PYY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000062984.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69872                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MGS/ML PROTEIN IN 20 MM TRIS-HCL,     
REMARK 280  PH 8.0, 100 MM NACL, 3 MM DTT AND 5% (V/V) GLYCEROL. RESERVOIR      
REMARK 280  WITH 0.4 M AMMONIUM PHOSPHATE. CRYO W/ 15%-30% GLYCEROL, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
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       37.19550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.75100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.71600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.75100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.19550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.71600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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   234                                                      
REMARK 465     HIS A   235                                                      
REMARK 465     HIS A   236                                                      
REMARK 465     HIS A   237                                                      
REMARK 465     HIS A   238                                                      
REMARK 465     HIS A   239                                                      
REMARK 465     HIS A   240                                                      
REMARK 465     GLU A   241                                                      
REMARK 465     ASN A   242                                                      
REMARK 465     LEU A   243                                                      
REMARK 465     TYR A   244                                                      
REMARK 465     PHE A   245                                                      
REMARK 465     GLN A   246                                                      
REMARK 465     GLY A   247                                                      
REMARK 465     SER A   248                                                      
REMARK 465     PRO A   249                                                      
REMARK 465     ASN A   250                                                      
REMARK 465     GLU A   294                                                      
REMARK 465     ASP A   295                                                      
REMARK 465     THR A   296                                                      
REMARK 465     MET A   297                                                      
REMARK 465     SER A   520                                                      
REMARK 465     ILE A   521                                                      
REMARK 465     SER A   522                                                      
REMARK 465     ASP A   523                                                      
REMARK 465     GLU A   524                                                      
REMARK 465     VAL A   525                                                      
REMARK 465     GLU A   526                                                      
REMARK 465     LYS A   527                                                      
REMARK 465     GLU A   528                                                      
REMARK 465     LEU A   529                                                      
REMARK 465     GLY A   530                                                      
REMARK 465     LYS A   531                                                      
REMARK 465     MET B   234                                                      
REMARK 465     HIS B   235                                                      
REMARK 465     HIS B   236                                                      
REMARK 465     HIS B   237                                                      
REMARK 465     HIS B   238                                                      
REMARK 465     HIS B   239                                                      
REMARK 465     HIS B   240                                                      
REMARK 465     GLU B   241                                                      
REMARK 465     ASN B   242                                                      
REMARK 465     LEU B   243                                                      
REMARK 465     TYR B   244                                                      
REMARK 465     PHE B   245                                                      
REMARK 465     GLN B   246                                                      
REMARK 465     GLY B   247                                                      
REMARK 465     SER B   248                                                      
REMARK 465     PRO B   249                                                      
REMARK 465     ASN B   250                                                      
REMARK 465     TYR B   251                                                      
REMARK 465     LYS B   293                                                      
REMARK 465     GLU B   294                                                      
REMARK 465     ASP B   295                                                      
REMARK 465     THR B   296                                                      
REMARK 465     MET B   297                                                      
REMARK 465     GLU B   298                                                      
REMARK 465     LEU B   403                                                      
REMARK 465     SER B   404                                                      
REMARK 465     ARG B   405                                                      
REMARK 465     LEU B   406                                                      
REMARK 465     MET B   407                                                      
REMARK 465     THR B   408                                                      
REMARK 465     GLY B   409                                                      
REMARK 465     ASP B   410                                                      
REMARK 465     THR B   411                                                      
REMARK 465     TYR B   412                                                      
REMARK 465     THR B   413                                                      
REMARK 465     ALA B   414                                                      
REMARK 465     HIS B   415                                                      
REMARK 465     ALA B   416                                                      
REMARK 465     GLY B   417                                                      
REMARK 465     GLY B   530                                                      
REMARK 465     LYS B   531                                                      
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     TYR A 251    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 298    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 326    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 405    CD   NE   CZ   NH1  NH2                             
REMARK 470     THR A 408    OG1  CG2                                            
REMARK 470     ASP A 410    CG   OD1  OD2                                       
REMARK 470     LYS A 434    CD   CE   NZ                                        
REMARK 470     ARG B 258    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 327    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 375    CD   CE   NZ                                        
REMARK 470     GLU B 526    CD   OE1  OE2                                       
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    LYS A 264     -140.88   -109.74                                   
REMARK 500    ARG A 381      -13.02     91.69                                   
REMARK 500    ASP A 382       51.13   -148.94                                   
REMARK 500    HIS A 415      129.13   -171.72                                   
REMARK 500    ALA A 418     -167.89   -119.91                                   
REMARK 500    LYS B 264     -142.29   -121.37                                   
REMARK 500    ARG B 326      -98.22    -95.71                                   
REMARK 500    ARG B 381      -14.20     86.30                                   
REMARK 500    ASP B 382       46.33   -146.61                                   
REMARK 500    ASP B 474       31.91     72.52                                   
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 SO4 A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STI A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3YY A 538                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STI B 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PE B 170                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 60                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3YY B 532                 
DBREF  3PYY A  248   531  UNP    Q59FK4   Q59FK4_HUMAN   266    549             
DBREF  3PYY B  248   531  UNP    Q59FK4   Q59FK4_HUMAN   266    549             
SEQADV 3PYY MET A  234  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS A  235  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS A  236  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS A  237  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS A  238  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS A  239  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS A  240  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY GLU A  241  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY ASN A  242  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY LEU A  243  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY TYR A  244  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY PHE A  245  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY GLN A  246  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY GLY A  247  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY MET B  234  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS B  235  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS B  236  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS B  237  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS B  238  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS B  239  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY HIS B  240  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY GLU B  241  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY ASN B  242  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY LEU B  243  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY TYR B  244  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY PHE B  245  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY GLN B  246  UNP  Q59FK4              EXPRESSION TAG                 
SEQADV 3PYY GLY B  247  UNP  Q59FK4              EXPRESSION TAG                 
SEQRES   1 A  298  MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN          
SEQRES   2 A  298  GLY SER PRO ASN TYR ASP LYS TRP GLU MET GLU ARG THR          
SEQRES   3 A  298  ASP ILE THR MET LYS HIS LYS LEU GLY GLY GLY GLN TYR          
SEQRES   4 A  298  GLY GLU VAL TYR GLU GLY VAL TRP LYS LYS TYR SER LEU          
SEQRES   5 A  298  THR VAL ALA VAL LYS THR LEU LYS GLU ASP THR MET GLU          
SEQRES   6 A  298  VAL GLU GLU PHE LEU LYS GLU ALA ALA VAL MET LYS GLU          
SEQRES   7 A  298  ILE LYS HIS PRO ASN LEU VAL GLN LEU LEU GLY VAL CYS          
SEQRES   8 A  298  THR ARG GLU PRO PRO PHE TYR ILE ILE THR GLU PHE MET          
SEQRES   9 A  298  THR TYR GLY ASN LEU LEU ASP TYR LEU ARG GLU CYS ASN          
SEQRES  10 A  298  ARG GLN GLU VAL ASN ALA VAL VAL LEU LEU TYR MET ALA          
SEQRES  11 A  298  THR GLN ILE SER SER ALA MET GLU TYR LEU GLU LYS LYS          
SEQRES  12 A  298  ASN PHE ILE HIS ARG ASP LEU ALA ALA ARG ASN CYS LEU          
SEQRES  13 A  298  VAL GLY GLU ASN HIS LEU VAL LYS VAL ALA ASP PHE GLY          
SEQRES  14 A  298  LEU SER ARG LEU MET THR GLY ASP THR TYR THR ALA HIS          
SEQRES  15 A  298  ALA GLY ALA LYS PHE PRO ILE LYS TRP THR ALA PRO GLU          
SEQRES  16 A  298  SER LEU ALA TYR ASN LYS PHE SER ILE LYS SER ASP VAL          
SEQRES  17 A  298  TRP ALA PHE GLY VAL LEU LEU TRP GLU ILE ALA THR TYR          
SEQRES  18 A  298  GLY MET SER PRO TYR PRO GLY ILE ASP LEU SER GLN VAL          
SEQRES  19 A  298  TYR GLU LEU LEU GLU LYS ASP TYR ARG MET GLU ARG PRO          
SEQRES  20 A  298  GLU GLY CYS PRO GLU LYS VAL TYR GLU LEU MET ARG ALA          
SEQRES  21 A  298  CYS TRP GLN TRP ASN PRO SER ASP ARG PRO SER PHE ALA          
SEQRES  22 A  298  GLU ILE HIS GLN ALA PHE GLU THR MET PHE GLN GLU SER          
SEQRES  23 A  298  SER ILE SER ASP GLU VAL GLU LYS GLU LEU GLY LYS              
SEQRES   1 B  298  MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN          
SEQRES   2 B  298  GLY SER PRO ASN TYR ASP LYS TRP GLU MET GLU ARG THR          
SEQRES   3 B  298  ASP ILE THR MET LYS HIS LYS LEU GLY GLY GLY GLN TYR          
SEQRES   4 B  298  GLY GLU VAL TYR GLU GLY VAL TRP LYS LYS TYR SER LEU          
SEQRES   5 B  298  THR VAL ALA VAL LYS THR LEU LYS GLU ASP THR MET GLU          
SEQRES   6 B  298  VAL GLU GLU PHE LEU LYS GLU ALA ALA VAL MET LYS GLU          
SEQRES   7 B  298  ILE LYS HIS PRO ASN LEU VAL GLN LEU LEU GLY VAL CYS          
SEQRES   8 B  298  THR ARG GLU PRO PRO PHE TYR ILE ILE THR GLU PHE MET          
SEQRES   9 B  298  THR TYR GLY ASN LEU LEU ASP TYR LEU ARG GLU CYS ASN          
SEQRES  10 B  298  ARG GLN GLU VAL ASN ALA VAL VAL LEU LEU TYR MET ALA          
SEQRES  11 B  298  THR GLN ILE SER SER ALA MET GLU TYR LEU GLU LYS LYS          
SEQRES  12 B  298  ASN PHE ILE HIS ARG ASP LEU ALA ALA ARG ASN CYS LEU          
SEQRES  13 B  298  VAL GLY GLU ASN HIS LEU VAL LYS VAL ALA ASP PHE GLY          
SEQRES  14 B  298  LEU SER ARG LEU MET THR GLY ASP THR TYR THR ALA HIS          
SEQRES  15 B  298  ALA GLY ALA LYS PHE PRO ILE LYS TRP THR ALA PRO GLU          
SEQRES  16 B  298  SER LEU ALA TYR ASN LYS PHE SER ILE LYS SER ASP VAL          
SEQRES  17 B  298  TRP ALA PHE GLY VAL LEU LEU TRP GLU ILE ALA THR TYR          
SEQRES  18 B  298  GLY MET SER PRO TYR PRO GLY ILE ASP LEU SER GLN VAL          
SEQRES  19 B  298  TYR GLU LEU LEU GLU LYS ASP TYR ARG MET GLU ARG PRO          
SEQRES  20 B  298  GLU GLY CYS PRO GLU LYS VAL TYR GLU LEU MET ARG ALA          
SEQRES  21 B  298  CYS TRP GLN TRP ASN PRO SER ASP ARG PRO SER PHE ALA          
SEQRES  22 B  298  GLU ILE HIS GLN ALA PHE GLU THR MET PHE GLN GLU SER          
SEQRES  23 B  298  SER ILE SER ASP GLU VAL GLU LYS GLU LEU GLY LYS              
HET    SO4  A   4       5                                                       
HET    SO4  A   5       5                                                       
HET    STI  A   3      37                                                       
HET    3YY  A 538      25                                                       
HET    SO4  B   3       5                                                       
HET    STI  B   4      37                                                       
HET    2PE  B 170      28                                                       
HET    GOL  B  60       6                                                       
HET    3YY  B 532      25                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     STI 4-(4-METHYL-PIPERAZIN-1-YLMETHYL)-N-[4-METHYL-3-(4-              
HETNAM   2 STI  PYRIDIN-3-YL-PYRIMIDIN-2-YLAMINO)-PHENYL]-BENZAMIDE             
HETNAM     3YY (5R)-5-[3-(4-FLUOROPHENYL)-1-PHENYL-1H-PYRAZOL-4-                
HETNAM   2 3YY  YL]IMIDAZOLIDINE-2,4-DIONE                                      
HETNAM     2PE NONAETHYLENE GLYCOL                                              
HETNAM     GOL GLYCEROL                                                         
HETSYN     STI STI-571;IMATINIB                                                 
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   5  STI    2(C29 H31 N7 O)                                              
FORMUL   6  3YY    2(C18 H13 F N4 O2)                                           
FORMUL   9  2PE    C18 H38 O10                                                  
FORMUL  10  GOL    C3 H8 O3                                                     
FORMUL  12  HOH   *215(H2 O)                                                    
HELIX    1   1 GLU A  257  THR A  259  5                                   3    
HELIX    2   2 GLY A  268  GLN A  271  5                                   4    
HELIX    3   3 LYS A  282  SER A  284  5                                   3    
HELIX    4   4 GLU A  298  GLU A  311  1                                  14    
HELIX    5   5 LEU A  342  CYS A  349  1                                   8    
HELIX    6   6 ASN A  355  LYS A  376  1                                  22    
HELIX    7   7 ALA A  384  ARG A  386  5                                   3    
HELIX    8   8 GLU A  392  HIS A  394  5                                   3    
HELIX    9   9 GLY A  402  LEU A  406  5                                   5    
HELIX   10  10 PRO A  421  THR A  425  5                                   5    
HELIX   11  11 ALA A  426  ASN A  433  1                                   8    
HELIX   12  12 SER A  436  THR A  453  1                                  18    
HELIX   13  13 ASP A  463  SER A  465  5                                   3    
HELIX   14  14 GLN A  466  LYS A  473  1                                   8    
HELIX   15  15 PRO A  484  TRP A  495  1                                  12    
HELIX   16  16 ASN A  498  ARG A  502  5                                   5    
HELIX   17  17 SER A  504  SER A  519  1                                  16    
HELIX   18  18 GLU B  257  THR B  259  5                                   3    
HELIX   19  19 GLY B  268  GLN B  271  5                                   4    
HELIX   20  20 LYS B  282  SER B  284  5                                   3    
HELIX   21  21 GLU B  300  GLU B  311  1                                  12    
HELIX   22  22 ASN B  341  CYS B  349  1                                   9    
HELIX   23  23 ASN B  355  LYS B  376  1                                  22    
HELIX   24  24 ALA B  384  ARG B  386  5                                   3    
HELIX   25  25 GLU B  392  HIS B  394  5                                   3    
HELIX   26  26 PRO B  421  THR B  425  5                                   5    
HELIX   27  27 ALA B  426  ASN B  433  1                                   8    
HELIX   28  28 SER B  436  THR B  453  1                                  18    
HELIX   29  29 ASP B  463  SER B  465  5                                   3    
HELIX   30  30 GLN B  466  LYS B  473  1                                   8    
HELIX   31  31 PRO B  484  TRP B  495  1                                  12    
HELIX   32  32 ASN B  498  ARG B  502  5                                   5    
HELIX   33  33 SER B  504  LEU B  529  1                                  26    
SHEET    1   A 5 ILE A 261  LYS A 266  0                                        
SHEET    2   A 5 VAL A 275  TRP A 280 -1  O  GLU A 277   N  HIS A 265           
SHEET    3   A 5 LEU A 285  THR A 291 -1  O  LEU A 285   N  TRP A 280           
SHEET    4   A 5 TYR A 331  GLU A 335 -1  O  ILE A 332   N  LYS A 290           
SHEET    5   A 5 LEU A 320  CYS A 324 -1  N  LEU A 321   O  ILE A 333           
SHEET    1   B 3 GLY A 340  ASN A 341  0                                        
SHEET    2   B 3 CYS A 388  VAL A 390 -1  O  VAL A 390   N  GLY A 340           
SHEET    3   B 3 VAL A 396  VAL A 398 -1  O  LYS A 397   N  LEU A 389           
SHEET    1   C 2 THR A 413  HIS A 415  0                                        
SHEET    2   C 2 ALA A 418  PHE A 420 -1  O  PHE A 420   N  THR A 413           
SHEET    1   D 5 ILE B 261  LYS B 266  0                                        
SHEET    2   D 5 VAL B 275  TRP B 280 -1  O  GLU B 277   N  LYS B 264           
SHEET    3   D 5 LEU B 285  LEU B 292 -1  O  LEU B 285   N  TRP B 280           
SHEET    4   D 5 PHE B 330  GLU B 335 -1  O  ILE B 332   N  LYS B 290           
SHEET    5   D 5 LEU B 320  CYS B 324 -1  N  LEU B 321   O  ILE B 333           
SHEET    1   E 2 CYS B 388  VAL B 390  0                                        
SHEET    2   E 2 VAL B 396  VAL B 398 -1  O  LYS B 397   N  LEU B 389           
CISPEP   1 PRO A  328    PRO A  329          0        -0.18                     
CISPEP   2 PRO B  328    PRO B  329          0         0.58                     
SITE     1 AC1  3 ARG A 479  GLU A 481  GLY A 482                               
SITE     1 AC2  3 HOH A  21  ARG A 492  GLN A 496                               
SITE     1 AC3 16 HOH A  33  ALA A 288  LYS A 290  GLU A 305                    
SITE     2 AC3 16 MET A 309  ILE A 312  VAL A 318  THR A 334                    
SITE     3 AC3 16 PHE A 336  MET A 337  ILE A 379  HIS A 380                    
SITE     4 AC3 16 ARG A 381  ALA A 399  ASP A 400  PHE A 401                    
SITE     1 AC4 11 HOH A 150  ALA A 356  LEU A 359  ALA A 363                    
SITE     2 AC4 11 LEU A 448  ILE A 451  ALA A 452  GLU A 481                    
SITE     3 AC4 11 GLY A 482  CYS A 483  PRO A 484                               
SITE     1 AC5  3 GLU A 469  LYS A 473  LYS B 313                               
SITE     1 AC6 16 HOH B 177  TYR B 272  LYS B 290  GLU B 305                    
SITE     2 AC6 16 MET B 309  ILE B 312  VAL B 318  ILE B 332                    
SITE     3 AC6 16 THR B 334  PHE B 336  MET B 337  ILE B 379                    
SITE     4 AC6 16 HIS B 380  ALA B 399  ASP B 400  PHE B 401                    
SITE     1 AC7  8 ASN B 355  VAL B 358  TYR B 361  ASN B 393                    
SITE     2 AC7  8 TYR B 432  LYS B 434  PHE B 516  SER B 520                    
SITE     1 AC8  6 HOH B  37  ASP B 474  ARG B 476  ARG B 492                    
SITE     2 AC8  6 TRP B 495  GLN B 496                                          
SITE     1 AC9 13 GLU A 392  ASN A 393  HOH B 152  ALA B 356                    
SITE     2 AC9 13 LEU B 359  ALA B 363  LEU B 448  ILE B 451                    
SITE     3 AC9 13 ALA B 452  GLU B 481  GLY B 482  CYS B 483                    
SITE     4 AC9 13 PRO B 484                                                     
CRYST1   74.391   95.432  115.502  90.00  90.00  90.00 P 21 21 21    8          
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      0.013442  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010479  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008658        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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