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Database: PDB
Entry: 2F4J
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Original site: 2F4J 
HEADER    TRANSFERASE                             23-NOV-05   2F4J              
TITLE     STRUCTURE OF THE KINASE DOMAIN OF AN IMATINIB-RESISTANT ABL MUTANT IN 
TITLE    2 COMPLEX WITH THE AURORA KINASE INHIBITOR VX-680                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL1;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 227-513;                           
COMPND   5 SYNONYM: P150, C- ABL;                                               
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: ABL1, ABL, JTK7;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-STAR;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-TEV                                
KEYWDS    KINASE, KINASE INHIBITOR, ABL, TRANSFERASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.YOUNG,N.P.SHAH,L.H.CHAO,P.ZARRINKAR,P.SAWYERS,J.KURIYAN           
REVDAT   3   18-OCT-17 2F4J    1       REMARK                                   
REVDAT   2   24-FEB-09 2F4J    1       VERSN                                    
REVDAT   1   24-JAN-06 2F4J    0                                                
JRNL        AUTH   M.A.YOUNG,N.P.SHAH,L.H.CHAO,M.SEELIGER,Z.V.MILANOV,          
JRNL        AUTH 2 W.H.BIGGS,D.K.TREIBER,H.K.PATEL,P.P.ZARRINKAR,D.J.LOCKHART,  
JRNL        AUTH 3 C.L.SAWYERS,J.KURIYAN                                        
JRNL        TITL   STRUCTURE OF THE KINASE DOMAIN OF AN IMATINIB-RESISTANT ABL  
JRNL        TITL 2 MUTANT IN COMPLEX WITH THE AURORA KINASE INHIBITOR VX-680.   
JRNL        REF    CANCER RES.                   V.  66  1007 2006              
JRNL        REFN                   ISSN 0008-5472                               
JRNL        PMID   16424036                                                     
JRNL        DOI    10.1158/0008-5472.CAN-05-2788                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.91 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) : 1.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.29                          
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)   (%) : 85.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 23335                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1612                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.91                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 50.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1638                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 87                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.039                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2328                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 211                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.14000                                             
REMARK   3    B22 (A**2) : -8.84000                                             
REMARK   3    B33 (A**2) : -3.30000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.55000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
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) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.29                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.690                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : CNS BULK SOLVENT MODEL USED                          
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 47.71                                                
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  : VX680.PAR                                      
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: CROSS-VALIDATION METHOD:                  
REMARK   3   -> "THROUGHOUT"                                                    
REMARK   3   FREE R VALUE TEST SET SELECTION CRITERIA:                          
REMARK   3    -> "RANDOM"                                                       
REMARK   4                                                                      
REMARK   4 2F4J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000035443.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-OCT-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 3.5                                
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24731                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.12100                            
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) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 56.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52900                            
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: PDB ENTRY 1M52                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% W/V PEG1500, 0.1M CITRIC ACID, PH    
REMARK 280  3.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       29.70850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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    PRO A 309   C   -  N   -  CA  ANGL. DEV. =  10.6 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    LYS A 245     -132.31   -116.25                                   
REMARK 500    ASP A 276      -57.87     87.20                                   
REMARK 500    THR A 277      144.69     -6.01                                   
REMARK 500    PRO A 309     -108.39     10.53                                   
REMARK 500    ASP A 363       42.78   -154.44                                   
REMARK 500    ASP A 381       83.86     46.92                                   
REMARK 500    PRO A 402       90.98    -67.39                                   
REMARK 500    TYR A 440       63.27     38.98                                   
REMARK 500    ASP A 455       16.22     84.24                                   
REMARK 500    LEU A 510       -2.65    -59.60                                   
REMARK 500    LYS A 512      -25.16   -168.29                                   
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 VX6 A 514                 
DBREF  2F4J A  227   513  GB     62362414 NP_005148      227    513             
SEQADV 2F4J PRO A  396  GB   62362414  HIS   396 ENGINEERED                     
SEQADV 2F4J MET A  228  GB   62362414  VAL   228 CLONING ARTIFACT               
SEQRES   1 A  287  GLY MET SER PRO ASN TYR ASP LYS TRP GLU MET GLU ARG          
SEQRES   2 A  287  THR ASP ILE THR MET LYS HIS LYS LEU GLY GLY GLY GLN          
SEQRES   3 A  287  TYR GLY GLU VAL TYR GLU GLY VAL TRP LYS LYS TYR SER          
SEQRES   4 A  287  LEU THR VAL ALA VAL LYS THR LEU LYS GLU ASP THR MET          
SEQRES   5 A  287  GLU VAL GLU GLU PHE LEU LYS GLU ALA ALA VAL MET LYS          
SEQRES   6 A  287  GLU ILE LYS HIS PRO ASN LEU VAL GLN LEU LEU GLY VAL          
SEQRES   7 A  287  CYS THR ARG GLU PRO PRO PHE TYR ILE ILE THR GLU PHE          
SEQRES   8 A  287  MET THR TYR GLY ASN LEU LEU ASP TYR LEU ARG GLU CYS          
SEQRES   9 A  287  ASN ARG GLN GLU VAL ASN ALA VAL VAL LEU LEU TYR MET          
SEQRES  10 A  287  ALA THR GLN ILE SER SER ALA MET GLU TYR LEU GLU LYS          
SEQRES  11 A  287  LYS ASN PHE ILE HIS ARG ASP LEU ALA ALA ARG ASN CYS          
SEQRES  12 A  287  LEU VAL GLY GLU ASN HIS LEU VAL LYS VAL ALA ASP PHE          
SEQRES  13 A  287  GLY LEU SER ARG LEU MET THR GLY ASP THR TYR THR ALA          
SEQRES  14 A  287  PRO ALA GLY ALA LYS PHE PRO ILE LYS TRP THR ALA PRO          
SEQRES  15 A  287  GLU SER LEU ALA TYR ASN LYS PHE SER ILE LYS SER ASP          
SEQRES  16 A  287  VAL TRP ALA PHE GLY VAL LEU LEU TRP GLU ILE ALA THR          
SEQRES  17 A  287  TYR GLY MET SER PRO TYR PRO GLY ILE ASP LEU SER GLN          
SEQRES  18 A  287  VAL TYR GLU LEU LEU GLU LYS ASP TYR ARG MET GLU ARG          
SEQRES  19 A  287  PRO GLU GLY CYS PRO GLU LYS VAL TYR GLU LEU MET ARG          
SEQRES  20 A  287  ALA CYS TRP GLN TRP ASN PRO SER ASP ARG PRO SER PHE          
SEQRES  21 A  287  ALA GLU ILE HIS GLN ALA PHE GLU THR MET PHE GLN GLU          
SEQRES  22 A  287  SER SER ILE SER ASP GLU VAL GLU LYS GLU LEU GLY LYS          
SEQRES  23 A  287  GLN                                                          
HET    VX6  A 514      33                                                       
HETNAM     VX6 CYCLOPROPANECARBOXYLIC ACID {4-[4-(4-METHYL-PIPERAZIN-           
HETNAM   2 VX6  1-YL)-6-(5-METHYL-2H-PYRAZOL-3-YLAMINO)-PYRIMIDIN-2-            
HETNAM   3 VX6  YLSULFANYL]-PHENYL}-AMIDE                                       
FORMUL   2  VX6    C23 H28 N8 O S                                               
FORMUL   3  HOH   *211(H2 O)                                                    
HELIX    1   1 GLU A  238  THR A  240  5                                   3    
HELIX    2   2 GLY A  249  GLN A  252  5                                   4    
HELIX    3   3 LYS A  263  SER A  265  5                                   3    
HELIX    4   4 GLU A  279  LYS A  291  1                                  13    
HELIX    5   5 ASN A  322  CYS A  330  1                                   9    
HELIX    6   6 ASN A  336  ASN A  358  1                                  23    
HELIX    7   7 ALA A  365  ARG A  367  5                                   3    
HELIX    8   8 GLU A  373  HIS A  375  5                                   3    
HELIX    9   9 PRO A  402  THR A  406  5                                   5    
HELIX   10  10 ALA A  407  ASN A  414  1                                   8    
HELIX   11  11 SER A  417  THR A  434  1                                  18    
HELIX   12  12 ASP A  444  SER A  446  5                                   3    
HELIX   13  13 GLN A  447  LYS A  454  1                                   8    
HELIX   14  14 PRO A  465  TRP A  476  1                                  12    
HELIX   15  15 ASN A  479  ARG A  483  5                                   5    
HELIX   16  16 SER A  485  LEU A  510  1                                  26    
SHEET    1   A 5 ILE A 242  LYS A 247  0                                        
SHEET    2   A 5 VAL A 256  TRP A 261 -1  O  VAL A 260   N  THR A 243           
SHEET    3   A 5 LEU A 266  THR A 272 -1  O  VAL A 270   N  TYR A 257           
SHEET    4   A 5 TYR A 312  GLU A 316 -1  O  ILE A 313   N  LYS A 271           
SHEET    5   A 5 LEU A 301  CYS A 305 -1  N  LEU A 302   O  ILE A 314           
SHEET    1   B 2 PHE A 359  ILE A 360  0                                        
SHEET    2   B 2 ARG A 386  LEU A 387 -1  O  ARG A 386   N  ILE A 360           
SHEET    1   C 2 CYS A 369  VAL A 371  0                                        
SHEET    2   C 2 VAL A 377  VAL A 379 -1  O  LYS A 378   N  LEU A 370           
SHEET    1   D 2 TYR A 393  THR A 394  0                                        
SHEET    2   D 2 LYS A 415  PHE A 416 -1  O  PHE A 416   N  TYR A 393           
SITE     1 AC1 16 HOH A   9  HOH A  16  GLY A 249  TYR A 253                    
SITE     2 AC1 16 VAL A 256  ALA A 269  LYS A 271  GLU A 286                    
SITE     3 AC1 16 THR A 315  GLU A 316  PHE A 317  MET A 318                    
SITE     4 AC1 16 THR A 319  GLY A 321  LEU A 370  ASP A 381                    
CRYST1   44.768   59.417   66.896  90.00  98.42  90.00 P 1 21 1      2          
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      0.022337  0.000000  0.003306        0.00000                         
SCALE2      0.000000  0.016830  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015111        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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