GenomeNet

Database: PDB
Entry: 1OPL
LinkDB: 1OPL
Original site: 1OPL 
HEADER    TRANSFERASE                             06-MAR-03   1OPL              
TITLE     STRUCTURAL BASIS FOR THE AUTO-INHIBITION OF C-ABL TYROSINE            
TITLE    2 KINASE                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: N-TERMINAL 531 RESIDUES (MYR-SH3-SH2-KINASE                
COMPND   5 DOMAIN);                                                             
COMPND   6 EC: 2.7.1.112;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ABL;                                                           
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.NAGAR,O.HANTSCHEL,M.A.YOUNG,K.SCHEFFZEK,D.VEACH,                    
AUTHOR   2 W.BORNMANN,B.CLARKSON,G.SUPERTI-FURGA,J.KURIYAN                      
REVDAT   2   24-FEB-09 1OPL    1       VERSN                                    
REVDAT   1   08-APR-03 1OPL    0                                                
JRNL        AUTH   B.NAGAR,O.HANTSCHEL,M.A.YOUNG,K.SCHEFFZEK,D.VEACH,           
JRNL        AUTH 2 W.BORNMANN,B.CLARKSON,G.SUPERTI-FURGA,J.KURIYAN              
JRNL        TITL   STRUCTURAL BASIS FOR THE AUTOINHIBITION OF C-ABL             
JRNL        TITL 2 TYROSINE KINASE                                              
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 112   859 2003              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   12654251                                                     
JRNL        DOI    10.1016/S0092-8674(03)00194-6                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   O.HANTSCHEL,B.NAGAR,S.GUETTLER,J.KRETZSCHMAR,                
REMARK   1  AUTH 2 K.DOREY,J.KURIYAN,G.SUPERTI-FURGA                            
REMARK   1  TITL   A MYRISTOYL/PHOSPHOTYROSINE SWITCH REGULATES C-ABL           
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V. 112   845 2003              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  DOI    10.1016/S0092-8674(03)00191-0                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.42 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.42                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 16203                          
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 SET) : 0.306                           
REMARK   3   FREE R VALUE                     : 0.315                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1106                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.61                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1965                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190                       
REMARK   3   BIN FREE R VALUE                    : 0.3330                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 121                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.030                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6582                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 73                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 84.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 123.30                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -19.23000                                            
REMARK   3    B22 (A**2) : 20.33000                                             
REMARK   3    B33 (A**2) : -1.11000                                             
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) : 0.50                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.44                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.53                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.05                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.450 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.970 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.530 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 9.080 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.28                                                 
REMARK   3   BSOL        : 59.72                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : P16.PAR                                        
REMARK   3  PARAMETER FILE  3  : MYR.PAR                                        
REMARK   3  PARAMETER FILE  4  : &_1_PARAMETER_INFILE_4                         
REMARK   3  PARAMETER FILE  5  : &_1_PARAMETER_INFILE_5                         
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : &_1_TOPOLOGY_INFILE_1                          
REMARK   3  TOPOLOGY FILE  2   : &_1_TOPOLOGY_INFILE_2                          
REMARK   3  TOPOLOGY FILE  3   : &_1_TOPOLOGY_INFILE_3                          
REMARK   3  TOPOLOGY FILE  4   : &_1_TOPOLOGY_INFILE_4                          
REMARK   3  TOPOLOGY FILE  5   : &_1_TOPOLOGY_INFILE_5                          
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE STRUCTURE WAS REFINED BY              
REMARK   3  SUPERIMPOSING THE REFINED HIGH RESOLUTION STRUCTURE OF C-ABL        
REMARK   3  (PDB ENTRY 1OPK) ON THE MOLECULAR REPLACEMENT SOLUTION AND          
REMARK   3  OPTIMIZING POSITIONS OF INDIVIDUAL DOMAINS BY RIGID-BODY            
REMARK   3  REFINEMENT. FOLLOWING THIS, ONLY OVERALL DOMAIN B-FACTORS WERE      
REMARK   3  APPLIED TO MOLECULE B, WHEREAS INDIVIDUAL B-FACTORS WERE            
REMARK   3  REFINED FOR MOLECULE A.                                             
REMARK   4                                                                      
REMARK   4 1OPL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018538.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17250                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 75.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRIES 1M52, 2ABL                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M AMMONIUM TARTRATE , PH 7.0,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.19200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.19200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       38.50850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      136.69200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       38.50850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      136.69200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       62.19200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       38.50850            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      136.69200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       62.19200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       38.50850            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      136.69200            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       77.01700            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       62.19200            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     PHE A    22                                                      
REMARK 465     ILE A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     LYS A    28                                                      
REMARK 465     ARG A    29                                                      
REMARK 465     ASP A    30                                                      
REMARK 465     SER A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     ARG A    33                                                      
REMARK 465     HIS A    34                                                      
REMARK 465     GLY A    35                                                      
REMARK 465     GLY A    36                                                      
REMARK 465     PRO A    37                                                      
REMARK 465     HIS A    38                                                      
REMARK 465     CYS A    39                                                      
REMARK 465     ASN A    40                                                      
REMARK 465     VAL A    41                                                      
REMARK 465     PHE A    42                                                      
REMARK 465     VAL A    43                                                      
REMARK 465     GLU A    44                                                      
REMARK 465     HIS A    45                                                      
REMARK 465     GLU A    46                                                      
REMARK 465     ALA A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     GLN A    49                                                      
REMARK 465     ARG A    50                                                      
REMARK 465     PRO A    51                                                      
REMARK 465     VAL A    52                                                      
REMARK 465     ALA A    53                                                      
REMARK 465     SER A    54                                                      
REMARK 465     ASP A    55                                                      
REMARK 465     PHE A    56                                                      
REMARK 465     GLU A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     GLN A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     LEU A    61                                                      
REMARK 465     SER A    62                                                      
REMARK 465     GLU A    63                                                      
REMARK 465     ALA A    64                                                      
REMARK 465     ALA A    65                                                      
REMARK 465     ARG A    66                                                      
REMARK 465     TRP A    67                                                      
REMARK 465     ASN A    68                                                      
REMARK 465     SER A    69                                                      
REMARK 465     LYS A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     ASN A    72                                                      
REMARK 465     LEU A    73                                                      
REMARK 465     LEU A    74                                                      
REMARK 465     ALA A    75                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     PRO A    77                                                      
REMARK 465     SER A    78                                                      
REMARK 465     GLU A    79                                                      
REMARK 465     ASN A    80                                                      
REMARK 465     GLU A   532                                                      
REMARK 465     ASN A   533                                                      
REMARK 465     LEU A   534                                                      
REMARK 465     TYR A   535                                                      
REMARK 465     PHE A   536                                                      
REMARK 465     GLN A   537                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     VAL B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     ASP B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     PRO B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     LEU B    17                                                      
REMARK 465     PRO B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     LEU B    20                                                      
REMARK 465     HIS B    21                                                      
REMARK 465     PHE B    22                                                      
REMARK 465     ILE B    23                                                      
REMARK 465     LYS B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     ALA B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     LYS B    28                                                      
REMARK 465     ARG B    29                                                      
REMARK 465     ASP B    30                                                      
REMARK 465     SER B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     ARG B    33                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     GLY B    35                                                      
REMARK 465     GLY B    36                                                      
REMARK 465     PRO B    37                                                      
REMARK 465     HIS B    38                                                      
REMARK 465     CYS B    39                                                      
REMARK 465     ASN B    40                                                      
REMARK 465     VAL B    41                                                      
REMARK 465     PHE B    42                                                      
REMARK 465     VAL B    43                                                      
REMARK 465     GLU B    44                                                      
REMARK 465     HIS B    45                                                      
REMARK 465     GLU B    46                                                      
REMARK 465     ALA B    47                                                      
REMARK 465     LEU B    48                                                      
REMARK 465     GLN B    49                                                      
REMARK 465     ARG B    50                                                      
REMARK 465     PRO B    51                                                      
REMARK 465     VAL B    52                                                      
REMARK 465     ALA B    53                                                      
REMARK 465     SER B    54                                                      
REMARK 465     ASP B    55                                                      
REMARK 465     PHE B    56                                                      
REMARK 465     GLU B    57                                                      
REMARK 465     PRO B    58                                                      
REMARK 465     GLN B    59                                                      
REMARK 465     GLY B    60                                                      
REMARK 465     LEU B    61                                                      
REMARK 465     SER B    62                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     ALA B    64                                                      
REMARK 465     ALA B    65                                                      
REMARK 465     ARG B    66                                                      
REMARK 465     TRP B    67                                                      
REMARK 465     ASN B    68                                                      
REMARK 465     SER B    69                                                      
REMARK 465     LYS B    70                                                      
REMARK 465     GLU B    71                                                      
REMARK 465     ASN B    72                                                      
REMARK 465     LEU B    73                                                      
REMARK 465     LEU B    74                                                      
REMARK 465     ALA B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     PRO B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     GLU B    79                                                      
REMARK 465     ASN B    80                                                      
REMARK 465     ASP B    81                                                      
REMARK 465     PRO B    82                                                      
REMARK 465     ASN B    83                                                      
REMARK 465     LEU B    84                                                      
REMARK 465     PHE B    85                                                      
REMARK 465     VAL B    86                                                      
REMARK 465     ALA B    87                                                      
REMARK 465     LEU B    88                                                      
REMARK 465     TYR B    89                                                      
REMARK 465     ASP B    90                                                      
REMARK 465     PHE B    91                                                      
REMARK 465     VAL B    92                                                      
REMARK 465     ALA B    93                                                      
REMARK 465     SER B    94                                                      
REMARK 465     GLY B    95                                                      
REMARK 465     ASP B    96                                                      
REMARK 465     ASN B    97                                                      
REMARK 465     THR B    98                                                      
REMARK 465     LEU B    99                                                      
REMARK 465     SER B   100                                                      
REMARK 465     ILE B   101                                                      
REMARK 465     THR B   102                                                      
REMARK 465     LYS B   103                                                      
REMARK 465     GLY B   104                                                      
REMARK 465     GLU B   105                                                      
REMARK 465     LYS B   106                                                      
REMARK 465     LEU B   107                                                      
REMARK 465     ARG B   108                                                      
REMARK 465     VAL B   109                                                      
REMARK 465     LEU B   110                                                      
REMARK 465     GLY B   111                                                      
REMARK 465     TYR B   112                                                      
REMARK 465     ASN B   113                                                      
REMARK 465     HIS B   114                                                      
REMARK 465     ASN B   115                                                      
REMARK 465     GLY B   116                                                      
REMARK 465     GLU B   117                                                      
REMARK 465     TRP B   118                                                      
REMARK 465     CYS B   119                                                      
REMARK 465     GLU B   120                                                      
REMARK 465     ALA B   121                                                      
REMARK 465     GLN B   122                                                      
REMARK 465     THR B   123                                                      
REMARK 465     LYS B   124                                                      
REMARK 465     ASN B   125                                                      
REMARK 465     GLY B   126                                                      
REMARK 465     GLN B   127                                                      
REMARK 465     GLY B   128                                                      
REMARK 465     TRP B   129                                                      
REMARK 465     VAL B   130                                                      
REMARK 465     PRO B   131                                                      
REMARK 465     SER B   132                                                      
REMARK 465     ASN B   133                                                      
REMARK 465     TYR B   134                                                      
REMARK 465     ILE B   135                                                      
REMARK 465     THR B   136                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     VAL B   138                                                      
REMARK 465     ASN B   139                                                      
REMARK 465     LYS B   238                                                      
REMARK 465     ARG B   239                                                      
REMARK 465     ASN B   240                                                      
REMARK 465     LYS B   241                                                      
REMARK 465     PRO B   242                                                      
REMARK 465     THR B   243                                                      
REMARK 465     VAL B   244                                                      
REMARK 465     TYR B   245                                                      
REMARK 465     GLY B   246                                                      
REMARK 465     VAL B   247                                                      
REMARK 465     SER B   248                                                      
REMARK 465     PRO B   249                                                      
REMARK 465     ASN B   250                                                      
REMARK 465     TYR B   251                                                      
REMARK 465     SER B   519                                                      
REMARK 465     SER B   520                                                      
REMARK 465     ILE B   521                                                      
REMARK 465     SER B   522                                                      
REMARK 465     ASP B   523                                                      
REMARK 465     GLU B   524                                                      
REMARK 465     VAL B   525                                                      
REMARK 465     GLU B   526                                                      
REMARK 465     LYS B   527                                                      
REMARK 465     GLU B   528                                                      
REMARK 465     LEU B   529                                                      
REMARK 465     GLY B   530                                                      
REMARK 465     LYS B   531                                                      
REMARK 465     GLU B   532                                                      
REMARK 465     ASN B   533                                                      
REMARK 465     LEU B   534                                                      
REMARK 465     TYR B   535                                                      
REMARK 465     PHE B   536                                                      
REMARK 465     GLN B   537                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A  95   N   -  CA  -  C   ANGL. DEV. = -15.3 DEGREES          
REMARK 500    TYR A 459   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    LEU B 464   CB  -  CA  -  C   ANGL. DEV. =  13.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  94      -38.38   -150.89                                   
REMARK 500    ASP A 226       54.43     39.63                                   
REMARK 500    ASP A 252       86.58     42.30                                   
REMARK 500    LYS A 264     -141.84   -119.82                                   
REMARK 500    LYS A 282      -27.96    -35.66                                   
REMARK 500    THR A 296     -105.40   -133.93                                   
REMARK 500    ARG A 381       -6.86     73.72                                   
REMARK 500    THR A 408      108.73    -54.69                                   
REMARK 500    TYR A 459       72.87     52.54                                   
REMARK 500    LEU A 464       22.87    -78.97                                   
REMARK 500    SER A 519      159.53    169.52                                   
REMARK 500    ASP B 226       54.28     39.72                                   
REMARK 500    THR B 259       21.23    -74.62                                   
REMARK 500    LYS B 264     -141.87   -119.82                                   
REMARK 500    LYS B 282      -29.11    -37.34                                   
REMARK 500    THR B 296     -162.26    175.15                                   
REMARK 500    GLU B 298      161.41    -44.90                                   
REMARK 500    ARG B 381       -6.95     73.81                                   
REMARK 500    THR B 408      108.70    -54.56                                   
REMARK 500    ASP B 463      131.91    -34.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MYR A  538                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 538                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P16 A 539                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P16 B 538                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OPJ   RELATED DB: PDB                                   
REMARK 900 C-ABL KINASE DOMAIN IN COMPLEX WITH A MYRISTOYLATED PEPTIDE          
REMARK 900 RELATED ID: 1OPK   RELATED DB: PDB                                   
REMARK 900 C-ABL SH3-SH2-KINASE DOMAINS IN COMPLEX WITH MYRISTIC ACID           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE BOUND MYRISTOYL GROUP IS FROM THE NATURALLY                      
REMARK 999 OCCURRING N-TERMINAL MYRISTOYL MODIFICATION THAT                     
REMARK 999 IS CONNECTED TO THE SH3 DOMAIN OF THE PROTEIN CHAIN A                
REMARK 999 BY 79 RESIDUES THAT COULD NOT BE MODELED. AN O                       
REMARK 999 ATOM HAS BEEN INTENTIONALLY OMITTED FROM MYR SINCE                   
REMARK 999 THE O ATOM IS NOT CHEMICALLY PRESENT IN A MYRISTOYL                  
REMARK 999 GROUP THAT IS ATTACHED TO THE PROTEIN.                               
DBREF  1OPL A    1   531  UNP    P00519   ABL1_HUMAN       1    531             
DBREF  1OPL B    1   531  UNP    P00519   ABL1_HUMAN       1    531             
SEQADV 1OPL ARG A   29  UNP  P00519    LYS    29 ENGINEERED                     
SEQADV 1OPL ASP A   30  UNP  P00519    GLU    30 ENGINEERED                     
SEQADV 1OPL ASN A  382  UNP  P00519    ASP   382 ENGINEERED                     
SEQADV 1OPL GLU A  532  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL ASN A  533  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL LEU A  534  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL TYR A  535  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL PHE A  536  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL GLN A  537  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL ARG B   29  UNP  P00519    LYS    29 ENGINEERED                     
SEQADV 1OPL ASP B   30  UNP  P00519    GLU    30 ENGINEERED                     
SEQADV 1OPL ASN B  382  UNP  P00519    ASP   382 ENGINEERED                     
SEQADV 1OPL GLU B  532  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL ASN B  533  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL LEU B  534  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL TYR B  535  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL PHE B  536  UNP  P00519              CLONING ARTIFACT               
SEQADV 1OPL GLN B  537  UNP  P00519              CLONING ARTIFACT               
SEQRES   1 A  537  MET GLY GLN GLN PRO GLY LYS VAL LEU GLY ASP GLN ARG          
SEQRES   2 A  537  ARG PRO SER LEU PRO ALA LEU HIS PHE ILE LYS GLY ALA          
SEQRES   3 A  537  GLY LYS ARG ASP SER SER ARG HIS GLY GLY PRO HIS CYS          
SEQRES   4 A  537  ASN VAL PHE VAL GLU HIS GLU ALA LEU GLN ARG PRO VAL          
SEQRES   5 A  537  ALA SER ASP PHE GLU PRO GLN GLY LEU SER GLU ALA ALA          
SEQRES   6 A  537  ARG TRP ASN SER LYS GLU ASN LEU LEU ALA GLY PRO SER          
SEQRES   7 A  537  GLU ASN ASP PRO ASN LEU PHE VAL ALA LEU TYR ASP PHE          
SEQRES   8 A  537  VAL ALA SER GLY ASP ASN THR LEU SER ILE THR LYS GLY          
SEQRES   9 A  537  GLU LYS LEU ARG VAL LEU GLY TYR ASN HIS ASN GLY GLU          
SEQRES  10 A  537  TRP CYS GLU ALA GLN THR LYS ASN GLY GLN GLY TRP VAL          
SEQRES  11 A  537  PRO SER ASN TYR ILE THR PRO VAL ASN SER LEU GLU LYS          
SEQRES  12 A  537  HIS SER TRP TYR HIS GLY PRO VAL SER ARG ASN ALA ALA          
SEQRES  13 A  537  GLU TYR LEU LEU SER SER GLY ILE ASN GLY SER PHE LEU          
SEQRES  14 A  537  VAL ARG GLU SER GLU SER SER PRO GLY GLN ARG SER ILE          
SEQRES  15 A  537  SER LEU ARG TYR GLU GLY ARG VAL TYR HIS TYR ARG ILE          
SEQRES  16 A  537  ASN THR ALA SER ASP GLY LYS LEU TYR VAL SER SER GLU          
SEQRES  17 A  537  SER ARG PHE ASN THR LEU ALA GLU LEU VAL HIS HIS HIS          
SEQRES  18 A  537  SER THR VAL ALA ASP GLY LEU ILE THR THR LEU HIS TYR          
SEQRES  19 A  537  PRO ALA PRO LYS ARG ASN LYS PRO THR VAL TYR GLY VAL          
SEQRES  20 A  537  SER PRO ASN TYR ASP LYS TRP GLU MET GLU ARG THR ASP          
SEQRES  21 A  537  ILE THR MET LYS HIS LYS LEU GLY GLY GLY GLN TYR GLY          
SEQRES  22 A  537  GLU VAL TYR GLU GLY VAL TRP LYS LYS TYR SER LEU THR          
SEQRES  23 A  537  VAL ALA VAL LYS THR LEU LYS GLU ASP THR MET GLU VAL          
SEQRES  24 A  537  GLU GLU PHE LEU LYS GLU ALA ALA VAL MET LYS GLU ILE          
SEQRES  25 A  537  LYS HIS PRO ASN LEU VAL GLN LEU LEU GLY VAL CYS THR          
SEQRES  26 A  537  ARG GLU PRO PRO PHE TYR ILE ILE THR GLU PHE MET THR          
SEQRES  27 A  537  TYR GLY ASN LEU LEU ASP TYR LEU ARG GLU CYS ASN ARG          
SEQRES  28 A  537  GLN GLU VAL ASN ALA VAL VAL LEU LEU TYR MET ALA THR          
SEQRES  29 A  537  GLN ILE SER SER ALA MET GLU TYR LEU GLU LYS LYS ASN          
SEQRES  30 A  537  PHE ILE HIS ARG ASN LEU ALA ALA ARG ASN CYS LEU VAL          
SEQRES  31 A  537  GLY GLU ASN HIS LEU VAL LYS VAL ALA ASP PHE GLY LEU          
SEQRES  32 A  537  SER ARG LEU MET THR GLY ASP THR TYR THR ALA HIS ALA          
SEQRES  33 A  537  GLY ALA LYS PHE PRO ILE LYS TRP THR ALA PRO GLU SER          
SEQRES  34 A  537  LEU ALA TYR ASN LYS PHE SER ILE LYS SER ASP VAL TRP          
SEQRES  35 A  537  ALA PHE GLY VAL LEU LEU TRP GLU ILE ALA THR TYR GLY          
SEQRES  36 A  537  MET SER PRO TYR PRO GLY ILE ASP LEU SER GLN VAL TYR          
SEQRES  37 A  537  GLU LEU LEU GLU LYS ASP TYR ARG MET GLU ARG PRO GLU          
SEQRES  38 A  537  GLY CYS PRO GLU LYS VAL TYR GLU LEU MET ARG ALA CYS          
SEQRES  39 A  537  TRP GLN TRP ASN PRO SER ASP ARG PRO SER PHE ALA GLU          
SEQRES  40 A  537  ILE HIS GLN ALA PHE GLU THR MET PHE GLN GLU SER SER          
SEQRES  41 A  537  ILE SER ASP GLU VAL GLU LYS GLU LEU GLY LYS GLU ASN          
SEQRES  42 A  537  LEU TYR PHE GLN                                              
SEQRES   1 B  537  MET GLY GLN GLN PRO GLY LYS VAL LEU GLY ASP GLN ARG          
SEQRES   2 B  537  ARG PRO SER LEU PRO ALA LEU HIS PHE ILE LYS GLY ALA          
SEQRES   3 B  537  GLY LYS ARG ASP SER SER ARG HIS GLY GLY PRO HIS CYS          
SEQRES   4 B  537  ASN VAL PHE VAL GLU HIS GLU ALA LEU GLN ARG PRO VAL          
SEQRES   5 B  537  ALA SER ASP PHE GLU PRO GLN GLY LEU SER GLU ALA ALA          
SEQRES   6 B  537  ARG TRP ASN SER LYS GLU ASN LEU LEU ALA GLY PRO SER          
SEQRES   7 B  537  GLU ASN ASP PRO ASN LEU PHE VAL ALA LEU TYR ASP PHE          
SEQRES   8 B  537  VAL ALA SER GLY ASP ASN THR LEU SER ILE THR LYS GLY          
SEQRES   9 B  537  GLU LYS LEU ARG VAL LEU GLY TYR ASN HIS ASN GLY GLU          
SEQRES  10 B  537  TRP CYS GLU ALA GLN THR LYS ASN GLY GLN GLY TRP VAL          
SEQRES  11 B  537  PRO SER ASN TYR ILE THR PRO VAL ASN SER LEU GLU LYS          
SEQRES  12 B  537  HIS SER TRP TYR HIS GLY PRO VAL SER ARG ASN ALA ALA          
SEQRES  13 B  537  GLU TYR LEU LEU SER SER GLY ILE ASN GLY SER PHE LEU          
SEQRES  14 B  537  VAL ARG GLU SER GLU SER SER PRO GLY GLN ARG SER ILE          
SEQRES  15 B  537  SER LEU ARG TYR GLU GLY ARG VAL TYR HIS TYR ARG ILE          
SEQRES  16 B  537  ASN THR ALA SER ASP GLY LYS LEU TYR VAL SER SER GLU          
SEQRES  17 B  537  SER ARG PHE ASN THR LEU ALA GLU LEU VAL HIS HIS HIS          
SEQRES  18 B  537  SER THR VAL ALA ASP GLY LEU ILE THR THR LEU HIS TYR          
SEQRES  19 B  537  PRO ALA PRO LYS ARG ASN LYS PRO THR VAL TYR GLY VAL          
SEQRES  20 B  537  SER PRO ASN TYR ASP LYS TRP GLU MET GLU ARG THR ASP          
SEQRES  21 B  537  ILE THR MET LYS HIS LYS LEU GLY GLY GLY GLN TYR GLY          
SEQRES  22 B  537  GLU VAL TYR GLU GLY VAL TRP LYS LYS TYR SER LEU THR          
SEQRES  23 B  537  VAL ALA VAL LYS THR LEU LYS GLU ASP THR MET GLU VAL          
SEQRES  24 B  537  GLU GLU PHE LEU LYS GLU ALA ALA VAL MET LYS GLU ILE          
SEQRES  25 B  537  LYS HIS PRO ASN LEU VAL GLN LEU LEU GLY VAL CYS THR          
SEQRES  26 B  537  ARG GLU PRO PRO PHE TYR ILE ILE THR GLU PHE MET THR          
SEQRES  27 B  537  TYR GLY ASN LEU LEU ASP TYR LEU ARG GLU CYS ASN ARG          
SEQRES  28 B  537  GLN GLU VAL ASN ALA VAL VAL LEU LEU TYR MET ALA THR          
SEQRES  29 B  537  GLN ILE SER SER ALA MET GLU TYR LEU GLU LYS LYS ASN          
SEQRES  30 B  537  PHE ILE HIS ARG ASN LEU ALA ALA ARG ASN CYS LEU VAL          
SEQRES  31 B  537  GLY GLU ASN HIS LEU VAL LYS VAL ALA ASP PHE GLY LEU          
SEQRES  32 B  537  SER ARG LEU MET THR GLY ASP THR TYR THR ALA HIS ALA          
SEQRES  33 B  537  GLY ALA LYS PHE PRO ILE LYS TRP THR ALA PRO GLU SER          
SEQRES  34 B  537  LEU ALA TYR ASN LYS PHE SER ILE LYS SER ASP VAL TRP          
SEQRES  35 B  537  ALA PHE GLY VAL LEU LEU TRP GLU ILE ALA THR TYR GLY          
SEQRES  36 B  537  MET SER PRO TYR PRO GLY ILE ASP LEU SER GLN VAL TYR          
SEQRES  37 B  537  GLU LEU LEU GLU LYS ASP TYR ARG MET GLU ARG PRO GLU          
SEQRES  38 B  537  GLY CYS PRO GLU LYS VAL TYR GLU LEU MET ARG ALA CYS          
SEQRES  39 B  537  TRP GLN TRP ASN PRO SER ASP ARG PRO SER PHE ALA GLU          
SEQRES  40 B  537  ILE HIS GLN ALA PHE GLU THR MET PHE GLN GLU SER SER          
SEQRES  41 B  537  ILE SER ASP GLU VAL GLU LYS GLU LEU GLY LYS GLU ASN          
SEQRES  42 B  537  LEU TYR PHE GLN                                              
HET    MYR  A 538      15                                                       
HET    P16  A 539      29                                                       
HET    P16  B 538      29                                                       
HETNAM     MYR MYRISTIC ACID                                                    
HETNAM     P16 6-(2,6-DICHLOROPHENYL)-2-{[3-(HYDROXYMETHYL)                     
HETNAM   2 P16  PHENYL]AMINO}-8-METHYLPYRIDO[2,3-D]PYRIMIDIN-7(8H)-ONE          
HETSYN     P16 PD166326                                                         
FORMUL   3  MYR    C14 H28 O2                                                   
FORMUL   4  P16    2(C21 H16 CL2 N4 O2)                                         
HELIX    1   1 SER A  140  HIS A  144  5                                   5    
HELIX    2   2 SER A  152  LEU A  160  1                                   9    
HELIX    3   3 SER A  161  GLY A  163  5                                   3    
HELIX    4   4 THR A  213  SER A  222  1                                  10    
HELIX    5   5 GLU A  257  THR A  259  5                                   3    
HELIX    6   6 GLY A  268  GLN A  271  5                                   4    
HELIX    7   7 LYS A  282  SER A  284  5                                   3    
HELIX    8   8 GLU A  298  ILE A  312  1                                  15    
HELIX    9   9 ASN A  341  CYS A  349  1                                   9    
HELIX   10  10 ASN A  355  LYS A  376  1                                  22    
HELIX   11  11 ALA A  384  ARG A  386  5                                   3    
HELIX   12  12 GLU A  392  HIS A  394  5                                   3    
HELIX   13  13 PRO A  421  THR A  425  5                                   5    
HELIX   14  14 ALA A  426  ASN A  433  1                                   8    
HELIX   15  15 SER A  436  THR A  453  1                                  18    
HELIX   16  16 GLN A  466  LYS A  473  1                                   8    
HELIX   17  17 PRO A  484  TRP A  495  1                                  12    
HELIX   18  18 ASN A  498  ARG A  502  5                                   5    
HELIX   19  19 SER A  504  THR A  514  1                                  11    
HELIX   20  20 SER A  520  LYS A  531  1                                  12    
HELIX   21  21 SER B  140  HIS B  144  5                                   5    
HELIX   22  22 SER B  152  SER B  161  1                                  10    
HELIX   23  23 THR B  213  SER B  222  1                                  10    
HELIX   24  24 GLU B  257  THR B  259  5                                   3    
HELIX   25  25 GLY B  268  GLN B  271  5                                   4    
HELIX   26  26 LYS B  282  SER B  284  5                                   3    
HELIX   27  27 GLU B  298  ILE B  312  1                                  15    
HELIX   28  28 LEU B  342  CYS B  349  1                                   8    
HELIX   29  29 ASN B  355  LYS B  376  1                                  22    
HELIX   30  30 ALA B  384  ARG B  386  5                                   3    
HELIX   31  31 GLU B  392  HIS B  394  5                                   3    
HELIX   32  32 PRO B  421  THR B  425  5                                   5    
HELIX   33  33 ALA B  426  ASN B  433  1                                   8    
HELIX   34  34 SER B  436  THR B  453  1                                  18    
HELIX   35  35 GLN B  466  LYS B  473  1                                   8    
HELIX   36  36 PRO B  484  TRP B  495  1                                  12    
HELIX   37  37 ASN B  498  ARG B  502  5                                   5    
HELIX   38  38 SER B  504  GLU B  518  1                                  15    
SHEET    1   A 5 GLN A 127  PRO A 131  0                                        
SHEET    2   A 5 TRP A 118  GLN A 122 -1  N  CYS A 119   O  VAL A 130           
SHEET    3   A 5 LYS A 106  TYR A 112 -1  O  ARG A 108   N  GLN A 122           
SHEET    4   A 5 LEU A  84  ALA A  87 -1  N  PHE A  85   O  LEU A 107           
SHEET    5   A 5 ILE A 135  PRO A 137 -1  O  THR A 136   N  VAL A  86           
SHEET    1   B 6 ARG A 189  ARG A 194  0                                        
SHEET    2   B 6 ARG A 180  TYR A 186 -1  O  ILE A 182   N  TYR A 193           
SHEET    3   B 6 SER A 167  GLU A 172 -1  O  SER A 167   N  ARG A 185           
SHEET    4   B 6 TYR A 147  PRO A 150  1  N  HIS A 148   O  VAL A 170           
SHEET    5   B 6 SER A 167  GLU A 172  1  O  VAL A 170   N  HIS A 148           
SHEET    6   B 6 TYR A 234  PRO A 235  1  O  TYR A 234   N  PHE A 168           
SHEET    1   C 2 ASN A 196  THR A 197  0                                        
SHEET    2   C 2 LEU A 203  TYR A 204 -1  O  TYR A 204   N  ASN A 196           
SHEET    1   D 5 ILE A 261  LYS A 266  0                                        
SHEET    2   D 5 VAL A 275  TRP A 280 -1  O  GLU A 277   N  LYS A 264           
SHEET    3   D 5 LEU A 285  THR A 291 -1  O  LEU A 285   N  TRP A 280           
SHEET    4   D 5 TYR A 331  GLU A 335 -1  O  ILE A 332   N  LYS A 290           
SHEET    5   D 5 LEU A 320  CYS A 324 -1  N  LEU A 321   O  ILE A 333           
SHEET    1   E 2 PHE A 378  ILE A 379  0                                        
SHEET    2   E 2 SER A 404  ARG A 405 -1  N  SER A 404   O  ILE A 379           
SHEET    1   F 2 CYS A 388  VAL A 390  0                                        
SHEET    2   F 2 VAL A 396  VAL A 398 -1  O  LYS A 397   N  LEU A 389           
SHEET    1   G 2 TYR A 412  THR A 413  0                                        
SHEET    2   G 2 LYS A 434  PHE A 435 -1  N  PHE A 435   O  TYR A 412           
SHEET    1   H 6 ARG B 189  ARG B 194  0                                        
SHEET    2   H 6 ARG B 180  TYR B 186 -1  O  ILE B 182   N  TYR B 193           
SHEET    3   H 6 SER B 167  GLU B 172 -1  O  SER B 167   N  ARG B 185           
SHEET    4   H 6 TYR B 147  PRO B 150  1  N  HIS B 148   O  VAL B 170           
SHEET    5   H 6 SER B 167  GLU B 172  1  O  VAL B 170   N  HIS B 148           
SHEET    6   H 6 TYR B 234  PRO B 235  1  O  TYR B 234   N  PHE B 168           
SHEET    1   I 2 ASN B 196  THR B 197  0                                        
SHEET    2   I 2 LEU B 203  TYR B 204 -1  O  TYR B 204   N  ASN B 196           
SHEET    1   J 5 ILE B 261  LYS B 266  0                                        
SHEET    2   J 5 VAL B 275  TRP B 280 -1  O  GLU B 277   N  LYS B 264           
SHEET    3   J 5 LEU B 285  THR B 291 -1  O  LEU B 285   N  TRP B 280           
SHEET    4   J 5 TYR B 331  GLU B 335 -1  O  ILE B 332   N  LYS B 290           
SHEET    5   J 5 LEU B 320  CYS B 324 -1  N  LEU B 321   O  ILE B 333           
SHEET    1   K 3 GLY B 340  ASN B 341  0                                        
SHEET    2   K 3 CYS B 388  VAL B 390 -1  N  VAL B 390   O  GLY B 340           
SHEET    3   K 3 VAL B 396  VAL B 398 -1  O  LYS B 397   N  LEU B 389           
SHEET    1   L 2 PHE B 378  ILE B 379  0                                        
SHEET    2   L 2 SER B 404  ARG B 405 -1  N  SER B 404   O  ILE B 379           
SHEET    1   M 2 TYR B 412  THR B 413  0                                        
SHEET    2   M 2 LYS B 434  PHE B 435 -1  N  PHE B 435   O  TYR B 412           
CISPEP   1 PRO A  328    PRO A  329          0        -0.49                     
CISPEP   2 PRO B  328    PRO B  329          0        -0.46                     
SITE     1 AC1  4 LEU A 360  GLU A 481  ILE A 521  LEU A 529                    
SITE     1 AC2 15 TYR A 272  VAL A 275  ALA A 288  LYS A 290                    
SITE     2 AC2 15 GLU A 305  MET A 309  ILE A 332  THR A 334                    
SITE     3 AC2 15 GLU A 335  MET A 337  GLY A 340  LEU A 389                    
SITE     4 AC2 15 ALA A 399  ASP A 400  PHE A 401                               
SITE     1 AC3 10 TYR B 272  GLU B 305  MET B 309  THR B 334                    
SITE     2 AC3 10 GLU B 335  MET B 337  GLY B 340  LEU B 389                    
SITE     3 AC3 10 ALA B 399  PHE B 401                                          
CRYST1   77.017  273.384  124.384  90.00  90.00  90.00 C 2 2 21     16          
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      0.012984  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003658  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008040        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system