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Database: PDB
Entry: 2QF6
LinkDB: 2QF6
Original site: 2QF6 
HEADER    CHAPERONE                               26-JUN-07   2QF6              
TITLE     HSP90 COMPLEXED WITH A56322                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HSP 86, RENAL CARCINOMA ANTIGEN NY- REN-38;                 
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: HSP90AA1, HSP90A, HSPC1, HSPCA;                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI                                  
KEYWDS    PROTEIN-INHIBITOR COMPLEX, CHAPERONE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.H.PARK                                                              
REVDAT   2   24-FEB-09 2QF6    1       VERSN                                    
REVDAT   1   01-JUL-08 2QF6    0                                                
JRNL        AUTH   J.R.HUTH,C.PARK,A.M.PETROS,A.R.KUNZER,M.D.WENDT,             
JRNL        AUTH 2 X.WANG,C.L.LYNCH,J.C.MACK,K.M.SWIFT,R.A.JUDGE,               
JRNL        AUTH 3 J.CHEN,P.L.RICHARDSON,S.JIN,S.K.TAHIR,                       
JRNL        AUTH 4 E.D.MATAYOSHI,S.A.DORWIN,U.S.LADROR,J.M.SEVERIN,             
JRNL        AUTH 5 K.A.WALTER,D.M.BARTLEY,S.W.FESIK,S.W.ELMORE,                 
JRNL        AUTH 6 P.J.HAJDUK                                                   
JRNL        TITL   DISCOVERY AND DESIGN OF NOVEL HSP90 INHIBITORS               
JRNL        TITL 2 USING 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   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 114746.710                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 21867                          
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) : 0.290                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2166                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
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) : 24085                
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.21                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1586                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3250                       
REMARK   3   BIN FREE R VALUE                    : 0.3810                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 179                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.028                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6512                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.91000                                              
REMARK   3    B22 (A**2) : 9.91000                                              
REMARK   3    B33 (A**2) : -19.83000                                            
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) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.38                            
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) : 0.49                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.48                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.73                            
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) : 1.720 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.930 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.480 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.900 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 14.73                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
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.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  : A56.PAR                                        
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : A56.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2QF6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043521.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 110.0                              
REMARK 200  PH                             : 6.5                                
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   : 23078                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.42900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
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: 1YER.PDB                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22 %(W/V) PEG 8000, 0.1 M NA             
REMARK 280  CACODYLATE, 0.2 M AMMONIUM SULFATE, PH 6.5, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
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   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       90.38950            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       59.41200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       59.41200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      135.58425            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       59.41200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       59.41200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       45.19475            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       59.41200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.41200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      135.58425            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       59.41200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.41200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       45.19475            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.38950            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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    ALA A  24      -68.48    -17.32                                   
REMARK 500    ASN A  40       32.72    -99.91                                   
REMARK 500    GLU A  42      -14.17    -47.95                                   
REMARK 500    ASP A  66       98.12    174.45                                   
REMARK 500    LYS A  69       -9.03    -55.24                                   
REMARK 500    THR A 109     -105.15   -109.87                                   
REMARK 500    ALA A 111      -48.43    147.27                                   
REMARK 500    SER A 113      -84.66    -81.76                                   
REMARK 500    ALA A 126      149.30    -19.49                                   
REMARK 500    ASP A 157     -170.39    -69.42                                   
REMARK 500    ASP A 193       31.06    -85.29                                   
REMARK 500    ALA B  24      -68.41    -17.28                                   
REMARK 500    ASN B  40       33.36    -98.75                                   
REMARK 500    GLU B  42      -14.75    -48.88                                   
REMARK 500    ASP B  66       98.37    174.30                                   
REMARK 500    LYS B  69       -8.82    -55.74                                   
REMARK 500    THR B 109     -105.56   -110.65                                   
REMARK 500    ALA B 111      -48.33    146.59                                   
REMARK 500    SER B 113      -84.77    -82.11                                   
REMARK 500    ALA B 126      149.35    -20.13                                   
REMARK 500    ASP B 193       30.25    -84.49                                   
REMARK 500    ALA C  24      -67.69    -17.33                                   
REMARK 500    ASN C  40       32.33    -99.63                                   
REMARK 500    GLU C  42      -15.41    -49.05                                   
REMARK 500    ASP C  66       97.43    173.32                                   
REMARK 500    LYS C  69       -8.93    -54.61                                   
REMARK 500    THR C 109     -106.17   -112.81                                   
REMARK 500    ALA C 111      -48.78    146.22                                   
REMARK 500    SER C 113      -84.57    -82.63                                   
REMARK 500    ALA C 126      148.94    -20.11                                   
REMARK 500    ALA D  24      -66.96    -16.43                                   
REMARK 500    ASN D  40       31.47    -98.52                                   
REMARK 500    GLU D  42      -14.05    -49.69                                   
REMARK 500    ASP D  66       97.13    173.70                                   
REMARK 500    LYS D  69       -8.42    -55.40                                   
REMARK 500    THR D 109     -106.38   -111.24                                   
REMARK 500    ALA D 111      -49.79    147.70                                   
REMARK 500    SER D 113      -84.28    -82.81                                   
REMARK 500    ALA D 126      148.85    -21.57                                   
REMARK 500    ASP D 193       31.35    -83.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 266        DISTANCE =  6.11 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A56 A 256                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A56 B 256                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A56 C 256                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A56 D 256                 
DBREF  2QF6 A   17   223  UNP    P07900   HS90A_HUMAN     17    223             
DBREF  2QF6 B   17   223  UNP    P07900   HS90A_HUMAN     17    223             
DBREF  2QF6 C   17   223  UNP    P07900   HS90A_HUMAN     17    223             
DBREF  2QF6 D   17   223  UNP    P07900   HS90A_HUMAN     17    223             
SEQADV 2QF6 THR A   63  UNP  P07900    SER    63 CONFLICT                       
SEQADV 2QF6 THR B   63  UNP  P07900    SER    63 CONFLICT                       
SEQADV 2QF6 THR C   63  UNP  P07900    SER    63 CONFLICT                       
SEQADV 2QF6 THR D   63  UNP  P07900    SER    63 CONFLICT                       
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 THR 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 THR 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              
SEQRES   1 C  207  VAL GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN LEU          
SEQRES   2 C  207  MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS GLU          
SEQRES   3 C  207  ILE PHE LEU ARG GLU LEU ILE SER ASN SER SER ASP ALA          
SEQRES   4 C  207  LEU ASP LYS ILE ARG TYR GLU THR LEU THR ASP PRO SER          
SEQRES   5 C  207  LYS LEU ASP SER GLY LYS GLU LEU HIS ILE ASN LEU ILE          
SEQRES   6 C  207  PRO ASN LYS GLN ASP ARG THR LEU THR ILE VAL ASP THR          
SEQRES   7 C  207  GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN LEU          
SEQRES   8 C  207  GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET GLU          
SEQRES   9 C  207  ALA LEU GLN ALA GLY ALA ASP ILE SER MET ILE GLY GLN          
SEQRES  10 C  207  PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA GLU          
SEQRES  11 C  207  LYS VAL THR VAL ILE THR LYS HIS ASN ASP ASP GLU GLN          
SEQRES  12 C  207  TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR VAL          
SEQRES  13 C  207  ARG THR ASP THR GLY GLU PRO MET GLY ARG GLY THR LYS          
SEQRES  14 C  207  VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR LEU          
SEQRES  15 C  207  GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS LYS HIS SER          
SEQRES  16 C  207  GLN PHE ILE GLY TYR PRO ILE THR LEU PHE VAL GLU              
SEQRES   1 D  207  VAL GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN LEU          
SEQRES   2 D  207  MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS GLU          
SEQRES   3 D  207  ILE PHE LEU ARG GLU LEU ILE SER ASN SER SER ASP ALA          
SEQRES   4 D  207  LEU ASP LYS ILE ARG TYR GLU THR LEU THR ASP PRO SER          
SEQRES   5 D  207  LYS LEU ASP SER GLY LYS GLU LEU HIS ILE ASN LEU ILE          
SEQRES   6 D  207  PRO ASN LYS GLN ASP ARG THR LEU THR ILE VAL ASP THR          
SEQRES   7 D  207  GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN LEU          
SEQRES   8 D  207  GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET GLU          
SEQRES   9 D  207  ALA LEU GLN ALA GLY ALA ASP ILE SER MET ILE GLY GLN          
SEQRES  10 D  207  PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA GLU          
SEQRES  11 D  207  LYS VAL THR VAL ILE THR LYS HIS ASN ASP ASP GLU GLN          
SEQRES  12 D  207  TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR VAL          
SEQRES  13 D  207  ARG THR ASP THR GLY GLU PRO MET GLY ARG GLY THR LYS          
SEQRES  14 D  207  VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR LEU          
SEQRES  15 D  207  GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS LYS HIS SER          
SEQRES  16 D  207  GLN PHE ILE GLY TYR PRO ILE THR LEU PHE VAL GLU              
HET    A56  A 256      19                                                       
HET    A56  B 256      19                                                       
HET    A56  C 256      19                                                       
HET    A56  D 256      19                                                       
HETNAM     A56 6-(3-BROMO-2-NAPHTHYL)-1,3,5-TRIAZINE-2,4-DIAMINE                
FORMUL   5  A56    4(C13 H10 BR N5)                                             
FORMUL   9  HOH   *130(H2 O)                                                    
HELIX    1   1 GLN A   23  ASN A   35  1                                  13    
HELIX    2   2 GLU A   42  THR A   65  1                                  24    
HELIX    3   3 ASP A   66  ASP A   71  5                                   6    
HELIX    4   4 THR A   99  LEU A  107  1                                   9    
HELIX    5   5 ALA A  111  ALA A  124  1                                  14    
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  ASN B   35  1                                  13    
HELIX   11  11 GLU B   42  THR B   65  1                                  24    
HELIX   12  12 ASP B   66  ASP B   71  5                                   6    
HELIX   13  13 THR B   99  LEU B  107  1                                   9    
HELIX   14  14 LYS B  112  ALA B  124  1                                  13    
HELIX   15  15 ASP B  127  GLY B  135  5                                   9    
HELIX   16  16 VAL B  136  LEU B  143  5                                   8    
HELIX   17  17 GLU B  192  LEU B  198  5                                   7    
HELIX   18  18 GLU B  199  SER B  211  1                                  13    
HELIX   19  19 GLN C   23  ASN C   35  1                                  13    
HELIX   20  20 GLU C   42  THR C   65  1                                  24    
HELIX   21  21 ASP C   66  ASP C   71  5                                   6    
HELIX   22  22 THR C   99  LEU C  107  1                                   9    
HELIX   23  23 LYS C  112  ALA C  124  1                                  13    
HELIX   24  24 ASP C  127  GLY C  135  5                                   9    
HELIX   25  25 VAL C  136  LEU C  143  5                                   8    
HELIX   26  26 GLU C  192  LEU C  198  5                                   7    
HELIX   27  27 GLU C  199  SER C  211  1                                  13    
HELIX   28  28 GLN D   23  ASN D   35  1                                  13    
HELIX   29  29 GLU D   42  THR D   65  1                                  24    
HELIX   30  30 ASP D   66  ASP D   71  5                                   6    
HELIX   31  31 THR D   99  LEU D  107  1                                   9    
HELIX   32  32 LYS D  112  ALA D  124  1                                  13    
HELIX   33  33 ASP D  127  GLY D  135  5                                   9    
HELIX   34  34 VAL D  136  LEU D  143  5                                   8    
HELIX   35  35 GLU D  192  LEU D  198  5                                   7    
HELIX   36  36 GLU D  199  SER D  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 GLN A 159  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 GLN B 159  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  ASN B  79   O  VAL B  92           
SHEET    8   B 8 ILE B 218  LEU B 220  1  O  THR B 219   N  LEU B  80           
SHEET    1   C 8 GLU C  18  ALA C  21  0                                        
SHEET    2   C 8 SER C 169  THR C 174 -1  O  PHE C 170   N  PHE C  20           
SHEET    3   C 8 GLN C 159  SER C 164 -1  N  ALA C 161   O  ARG C 173           
SHEET    4   C 8 ALA C 145  LYS C 153 -1  N  VAL C 150   O  TRP C 162           
SHEET    5   C 8 GLY C 183  LEU C 190 -1  O  ILE C 187   N  THR C 149           
SHEET    6   C 8 THR C  88  ASP C  93 -1  N  ILE C  91   O  VAL C 186           
SHEET    7   C 8 ILE C  78  ASN C  83 -1  N  ASN C  79   O  VAL C  92           
SHEET    8   C 8 ILE C 218  LEU C 220  1  O  THR C 219   N  LEU C  80           
SHEET    1   D 8 GLU D  18  ALA D  21  0                                        
SHEET    2   D 8 SER D 169  THR D 174 -1  O  PHE D 170   N  PHE D  20           
SHEET    3   D 8 GLN D 159  SER D 164 -1  N  ALA D 161   O  ARG D 173           
SHEET    4   D 8 ALA D 145  LYS D 153 -1  N  VAL D 150   O  TRP D 162           
SHEET    5   D 8 GLY D 183  LEU D 190 -1  O  ILE D 187   N  THR D 149           
SHEET    6   D 8 THR D  88  ASP D  93 -1  N  ILE D  91   O  VAL D 186           
SHEET    7   D 8 ILE D  78  ASN D  83 -1  N  ASN D  79   O  VAL D  92           
SHEET    8   D 8 ILE D 218  LEU D 220  1  O  THR D 219   N  LEU D  80           
SITE     1 AC1  9 ALA A  55  ASP A  93  MET A  98  ASN A 106                    
SITE     2 AC1  9 LEU A 107  GLY A 135  PHE A 138  TYR A 139                    
SITE     3 AC1  9 THR A 184                                                     
SITE     1 AC2  7 SER B  52  ALA B  55  ASP B  93  ASN B 106                    
SITE     2 AC2  7 GLY B 135  PHE B 138  THR B 184                               
SITE     1 AC3  7 ALA C  55  ASP C  93  GLY C  97  MET C  98                    
SITE     2 AC3  7 ASN C 106  PHE C 138  THR C 184                               
SITE     1 AC4  9 ALA D  55  ASP D  93  MET D  98  ASN D 106                    
SITE     2 AC4  9 LEU D 107  GLY D 135  PHE D 138  TYR D 139                    
SITE     3 AC4  9 THR D 184                                                     
CRYST1  118.824  118.824  180.779  90.00  90.00  90.00 P 43 21 2    32          
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      0.008416  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008416  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005532        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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