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Database: PDB
Entry: 2QFO
LinkDB: 2QFO
Original site: 2QFO 
HEADER    CHAPERONE                               27-JUN-07   2QFO              
TITLE     HSP90 COMPLEXED WITH A143571 AND A516383                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 17-223;                                       
COMPND   5 SYNONYM: HSP 86, RENAL CARCINOMA ANTIGEN NY-REN-38;                  
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HSP90AA1, HSP90A, HSPC1, HSPCA;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI                                  
KEYWDS    PROTEIN-INHIBITOR COMPLEX, ATP-BINDING, CHAPERONE, NUCLEOTIDE-        
KEYWDS   2 BINDING, PHOSPHOPROTEIN, STRESS RESPONSE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.H.PARK                                                              
REVDAT   3   16-APR-14 2QFO    1       REMARK VERSN                             
REVDAT   2   24-FEB-09 2QFO    1       VERSN                                    
REVDAT   1   01-JUL-08 2QFO    0                                                
JRNL        AUTH   J.R.HUTH,C.PARK,A.M.PETROS,A.R.KUNZER,M.D.WENDT,X.WANG,      
JRNL        AUTH 2 C.L.LYNCH,J.C.MACK,K.M.SWIFT,R.A.JUDGE,J.CHEN,               
JRNL        AUTH 3 P.L.RICHARDSON,S.JIN,S.K.TAHIR,E.D.MATAYOSHI,S.A.DORWIN,     
JRNL        AUTH 4 U.S.LADROR,J.M.SEVERIN,K.A.WALTER,D.M.BARTLEY,S.W.FESIK,     
JRNL        AUTH 5 S.W.ELMORE,P.J.HAJDUK                                        
JRNL        TITL   DISCOVERY AND DESIGN OF NOVEL HSP90 INHIBITORS USING         
JRNL        TITL 2 MULTIPLE FRAGMENT-BASED DESIGN STRATEGIES.                   
JRNL        REF    CHEM.BIOL.DRUG DES.           V.  70     1 2007              
JRNL        REFN                   ISSN 1747-0277                               
JRNL        PMID   17630989                                                     
JRNL        DOI    10.1111/J.1747-0285.2007.00535.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.68 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2002                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 119369.740                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 58785                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5969                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 64715                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.68                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4447                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE                    : 0.2650                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.40                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 515                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3254                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 320                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.90000                                             
REMARK   3    B22 (A**2) : 2.75000                                              
REMARK   3    B33 (A**2) : -1.86000                                             
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) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.05                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 6.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.23                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.11                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.114                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.900                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.670                           
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) : 0.550 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 0.930 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.340 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.890 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 43.07                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.P                                  
REMARK   3  PARAMETER FILE  2  : ACCELRYS_CNX_TOPPAR:WATER_REP.PARAM            
REMARK   3  PARAMETER FILE  3  : ACCELRYS_CNX_TOPPAR:ION.PARAM                  
REMARK   3  PARAMETER FILE  4  : A14.PAR                                        
REMARK   3  PARAMETER FILE  5  : A51.PAR                                        
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : A14.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : A51.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2QFO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043539.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 110.0                              
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-BM                              
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                  : SI                                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61674                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.680                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1YER                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 35 MG/ML WITH A RESERVOIR     
REMARK 280  OF 22-30 % (W/V) PEG4000, 0.1 M TRIS-HCL PH 8.5, 0.2 M MGCL2,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       32.07850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.37750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.07850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.37750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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 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    THR A  94       42.15   -108.89                                   
REMARK 500    ALA A 111     -126.84     53.93                                   
REMARK 500    ALA A 166     -139.46     71.07                                   
REMARK 500    ARG A 182      139.26   -171.35                                   
REMARK 500    THR B  94       42.93   -107.48                                   
REMARK 500    ILE B 110       54.34    -98.03                                   
REMARK 500    ALA B 166     -139.32     69.40                                   
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 A13 A 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A51 A 999                 
DBREF  2QFO A   17   223  UNP    P07900   HS90A_HUMAN     17    223             
DBREF  2QFO B   17   223  UNP    P07900   HS90A_HUMAN     17    223             
SEQRES   1 A  207  VAL GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN LEU          
SEQRES   2 A  207  MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS GLU          
SEQRES   3 A  207  ILE PHE LEU ARG GLU LEU ILE SER ASN SER SER ASP ALA          
SEQRES   4 A  207  LEU ASP LYS ILE ARG TYR GLU SER LEU THR ASP PRO SER          
SEQRES   5 A  207  LYS LEU ASP SER GLY LYS GLU LEU HIS ILE ASN LEU ILE          
SEQRES   6 A  207  PRO ASN LYS GLN ASP ARG THR LEU THR ILE VAL ASP THR          
SEQRES   7 A  207  GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN LEU          
SEQRES   8 A  207  GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET GLU          
SEQRES   9 A  207  ALA LEU GLN ALA GLY ALA ASP ILE SER MET ILE GLY GLN          
SEQRES  10 A  207  PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA GLU          
SEQRES  11 A  207  LYS VAL THR VAL ILE THR LYS HIS ASN ASP ASP GLU GLN          
SEQRES  12 A  207  TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR VAL          
SEQRES  13 A  207  ARG THR ASP THR GLY GLU PRO MET GLY ARG GLY THR LYS          
SEQRES  14 A  207  VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR LEU          
SEQRES  15 A  207  GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS LYS HIS SER          
SEQRES  16 A  207  GLN PHE ILE GLY TYR PRO ILE THR LEU PHE VAL GLU              
SEQRES   1 B  207  VAL GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN LEU          
SEQRES   2 B  207  MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS GLU          
SEQRES   3 B  207  ILE PHE LEU ARG GLU LEU ILE SER ASN SER SER ASP ALA          
SEQRES   4 B  207  LEU ASP LYS ILE ARG TYR GLU SER LEU THR ASP PRO SER          
SEQRES   5 B  207  LYS LEU ASP SER GLY LYS GLU LEU HIS ILE ASN LEU ILE          
SEQRES   6 B  207  PRO ASN LYS GLN ASP ARG THR LEU THR ILE VAL ASP THR          
SEQRES   7 B  207  GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN LEU          
SEQRES   8 B  207  GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET GLU          
SEQRES   9 B  207  ALA LEU GLN ALA GLY ALA ASP ILE SER MET ILE GLY GLN          
SEQRES  10 B  207  PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA GLU          
SEQRES  11 B  207  LYS VAL THR VAL ILE THR LYS HIS ASN ASP ASP GLU GLN          
SEQRES  12 B  207  TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR VAL          
SEQRES  13 B  207  ARG THR ASP THR GLY GLU PRO MET GLY ARG GLY THR LYS          
SEQRES  14 B  207  VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR LEU          
SEQRES  15 B  207  GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS LYS HIS SER          
SEQRES  16 B  207  GLN PHE ILE GLY TYR PRO ILE THR LEU PHE VAL GLU              
HET    A13  A 900      12                                                       
HET    A51  A 999      14                                                       
HETNAM     A13 4-METHYL-6-(TRIFLUOROMETHYL)PYRIMIDIN-2-AMINE                    
HETNAM     A51 (3E)-3-[(PHENYLAMINO)METHYLIDENE]DIHYDROFURAN-2(3H)-ONE          
FORMUL   3  A13    C6 H6 F3 N3                                                  
FORMUL   4  A51    C11 H11 N O2                                                 
FORMUL   5  HOH   *320(H2 O)                                                    
HELIX    1   1 GLN A   23  THR A   36  1                                  14    
HELIX    2   2 GLU A   42  ASP A   66  1                                  25    
HELIX    3   3 PRO A   67  ASP A   71  5                                   5    
HELIX    4   4 THR A   99  THR A  109  1                                  11    
HELIX    5   5 GLY A  114  ALA A  124  1                                  11    
HELIX    6   6 ASP A  127  GLY A  135  5                                   9    
HELIX    7   7 VAL A  136  LEU A  143  5                                   8    
HELIX    8   8 GLU A  192  LEU A  198  5                                   7    
HELIX    9   9 GLU A  199  SER A  211  1                                  13    
HELIX   10  10 GLN B   23  THR B   36  1                                  14    
HELIX   11  11 GLU B   42  ASP B   66  1                                  25    
HELIX   12  12 PRO B   67  ASP B   71  5                                   5    
HELIX   13  13 THR B   99  ASN B  105  1                                   7    
HELIX   14  14 ASN B  106  THR B  109  5                                   4    
HELIX   15  15 ILE B  110  ALA B  124  1                                  15    
HELIX   16  16 ASP B  127  GLY B  135  5                                   9    
HELIX   17  17 VAL B  136  LEU B  143  5                                   8    
HELIX   18  18 GLU B  192  LEU B  198  5                                   7    
HELIX   19  19 GLU B  199  SER B  211  1                                  13    
SHEET    1   A 8 GLU A  18  ALA A  21  0                                        
SHEET    2   A 8 SER A 169  THR A 174 -1  O  PHE A 170   N  PHE A  20           
SHEET    3   A 8 TYR A 160  SER A 164 -1  N  ALA A 161   O  ARG A 173           
SHEET    4   A 8 ALA A 145  LYS A 153 -1  N  VAL A 150   O  TRP A 162           
SHEET    5   A 8 GLY A 183  LEU A 190 -1  O  ILE A 187   N  THR A 149           
SHEET    6   A 8 THR A  88  ASP A  93 -1  N  ILE A  91   O  VAL A 186           
SHEET    7   A 8 ILE A  78  ASN A  83 -1  N  ASN A  79   O  VAL A  92           
SHEET    8   A 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
SHEET    1   B 8 GLU B  18  ALA B  21  0                                        
SHEET    2   B 8 SER B 169  THR B 174 -1  O  PHE B 170   N  PHE B  20           
SHEET    3   B 8 TYR B 160  SER B 164 -1  N  ALA B 161   O  ARG B 173           
SHEET    4   B 8 ALA B 145  LYS B 153 -1  N  VAL B 150   O  TRP B 162           
SHEET    5   B 8 GLY B 183  LEU B 190 -1  O  ILE B 187   N  THR B 149           
SHEET    6   B 8 THR B  88  ASP B  93 -1  N  ILE B  91   O  VAL B 186           
SHEET    7   B 8 ILE B  78  ASN B  83 -1  N  ILE B  81   O  THR B  90           
SHEET    8   B 8 ILE B 218  LEU B 220  1  O  THR B 219   N  LEU B  80           
SITE     1 AC1  8 ASN A  51  ALA A  55  ASP A  93  ILE A  96                    
SITE     2 AC1  8 GLY A  97  MET A  98  LEU A 107  THR A 184                    
SITE     1 AC2  5 ASN A  51  ASN A 106  GLY A 135  GLY A 137                    
SITE     2 AC2  5 PHE A 138                                                     
CRYST1   64.157   88.755   98.445  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015587  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011267  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010158        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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