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    HEADER    CHAPERONE                               02-MAR-04   1UYE              
    TITLE     HUMAN HSP90-ALPHA WITH 8-(2-CHLORO-3,4,5-TRIMETHOXY-BENZYL)           
    TITLE    2 -9-PENT-4-YLNYL-9H-PURIN-6-YLAMINE                                   
    COMPND    MOL_ID: 1;                                                            
    COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
    COMPND   3 CHAIN: A;                                                            
    COMPND   4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-235;                         
    COMPND   5 SYNONYM: HSP 86;                                                     
    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 ORGAN: SKIN;                                                         
    SOURCE   6 TISSUE: MELANOMA;                                                    
    SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
    SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
    SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
    SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET19;                                    
    SOURCE  11 OTHER_DETAILS: CLONED FROM IMAGE\:4026275                            
    KEYWDS    HSP90, ATPASE, PU9, CHAPERONE, ATP-BINDING, HEAT SHOCK                
    EXPDTA    X-RAY DIFFRACTION                                                     
    AUTHOR    L.WRIGHT,X.BARRIL,B.DYMOCK,L.SHERIDAN,A.SURGENOR,M.BESWICK,           
    AUTHOR   2 M.DRYSDALE,A.COLLIER,A.MASSEY,N.DAVIES,A.FINK,C.FROMONT,             
    AUTHOR   3 W.AHERNE,K.BOXALL,S.SHARP,P.WORKMAN,R.E.HUBBARD                      
    REVDAT   2   24-FEB-09 1UYE    1       VERSN                                    
    REVDAT   1   01-JUL-04 1UYE    0                                                
    JRNL        AUTH   L.WRIGHT,X.BARRIL,B.DYMOCK,L.SHERIDAN,A.SURGENOR,            
    JRNL        AUTH 2 M.BESWICK,M.DRYSDALE,A.COLLIER,A.MASSEY,N.DAVIES,            
    JRNL        AUTH 3 A.FINK,C.FROMONT,W.AHERNE,K.BOXALL,S.SHARP,                  
    JRNL        AUTH 4 P.WORKMAN,R.E.HUBBARD                                        
    JRNL        TITL   STRUCTURE-ACTIVITY RELATIONSHIPS IN PURINE-BASED             
    JRNL        TITL 2 INHIBITOR BINDING TO HSP90 ISOFORMS                          
    JRNL        REF    CHEM.BIOL.                    V.  11   775 2004              
    JRNL        REFN                   ISSN 1074-5521                               
    JRNL        PMID   15217611                                                     
    JRNL        DOI    10.1016/J.CHEMBIOL.2004.03.033                               
    REMARK   2                                                                      
    REMARK   2 RESOLUTION.    2.0  ANGSTROMS.                                       
    REMARK   3                                                                      
    REMARK   3 REFINEMENT.                                                          
    REMARK   3   PROGRAM     : REFMAC                                               
    REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
    REMARK   3                                                                      
    REMARK   3  DATA USED IN REFINEMENT.                                            
    REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
    REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.42                          
    REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
    REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
    REMARK   3   NUMBER OF REFLECTIONS             : 19286                          
    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) : NULL                            
    REMARK   3   R VALUE            (WORKING SET) : 0.18334                         
    REMARK   3   FREE R VALUE                     : 0.21814                         
    REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
    REMARK   3   FREE R VALUE TEST SET COUNT      : 1036                            
    REMARK   3                                                                      
    REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
    REMARK   3   PROTEIN ATOMS            : 1647                                    
    REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
    REMARK   3   HETEROGEN ATOMS          : 29                                      
    REMARK   3   SOLVENT ATOMS            : 277                                     
    REMARK   3                                                                      
    REMARK   3  B VALUES.                                                           
    REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
    REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.336                         
    REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
    REMARK   3    B11 (A**2) : -0.87                                                
    REMARK   3    B22 (A**2) : 0.61                                                 
    REMARK   3    B33 (A**2) : 0.26                                                 
    REMARK   3    B12 (A**2) : 0.00                                                 
    REMARK   3    B13 (A**2) : 0.00                                                 
    REMARK   3    B23 (A**2) : 0.00                                                 
    REMARK   3                                                                      
    REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
    REMARK   3   ESU BASED ON R VALUE                            (A): 0.154         
    REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
    REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.088         
    REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.098         
    REMARK   3                                                                      
    REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
    REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
    REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
    REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
    REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
    REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
    REMARK   3                                                                      
    REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
    REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
    REMARK   3                                                                      
    REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
    REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
    REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
    REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
    REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
    REMARK   3                                                                      
    REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
    REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
    REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
    REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
    REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
    REMARK   4                                                                      
    REMARK   4 1UYE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
    REMARK 100                                                                      
    REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  05-MAR-04.                 
    REMARK 100 THE PDBE ID CODE IS EBI-14619.                                       
    REMARK 200                                                                      
    REMARK 200 EXPERIMENTAL DETAILS                                                 
    REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
    REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-03                          
    REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
    REMARK 200  PH                             : 6.50                               
    REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
    REMARK 200                                                                      
    REMARK 200  SYNCHROTRON              (Y/N) : N                                  
    REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
    REMARK 200  BEAMLINE                       : NULL                               
    REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RH-3R                       
    REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
    REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
    REMARK 200  MONOCHROMATOR                  : NULL                               
    REMARK 200  OPTICS                         : OSMIC BLUE MIRRORS                 
    REMARK 200                                                                      
    REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
    REMARK 200  DETECTOR MANUFACTURER          : RAXIS IV                           
    REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
    REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
    REMARK 200                                                                      
    REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46520                              
    REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
    REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
    REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
    REMARK 200                                                                      
    REMARK 200 OVERALL.                                                             
    REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
    REMARK 200  DATA REDUNDANCY                : 2.400                              
    REMARK 200  R MERGE                    (I) : 0.09200                            
    REMARK 200  R SYM                      (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.8000                             
    REMARK 200                                                                      
    REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
    REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
    REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.1                               
    REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
    REMARK 200  R MERGE FOR SHELL          (I) : 0.35200                            
    REMARK 200  R SYM FOR SHELL            (I) : NULL                               
    REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
    REMARK 200                                                                      
    REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
    REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
    REMARK 200 SOFTWARE USED: MOLREP                                                
    REMARK 200 STARTING MODEL: PDB ENTRY 1YER                                       
    REMARK 200                                                                      
    REMARK 200 REMARK: NULL                                                         
    REMARK 280                                                                      
    REMARK 280 CRYSTAL                                                              
    REMARK 280 SOLVENT CONTENT, VS  (%): 54                                         
    REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
    REMARK 280                                                                      
    REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG MME 2000,                        
    REMARK 280  0.1M NA CACODYLATE, PH6.5, 0.2M MGCL2.                              
    REMARK 290                                                                      
    REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
    REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z                                                 
    REMARK 290       4555   X,-Y,-Z                                                 
    REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
    REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
    REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
    REMARK 290       8555   X+1/2,-Y+1/2,-Z+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        0.00000            
    REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
    REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
    REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
    REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
    REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.35000            
    REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.37750            
    REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       49.08550            
    REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.35000            
    REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.37750            
    REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.08550            
    REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.35000            
    REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.37750            
    REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       49.08550            
    REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.35000            
    REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       45.37750            
    REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.08550            
    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 GENERATING THE BIOMOLECULE                                           
    REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
    REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
    REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
    REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
    REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
    REMARK 350                                                                      
    REMARK 350 BIOMOLECULE:  1                                                      
    REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
    REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
    REMARK 350 SOFTWARE USED: PQS                                                   
    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 400                                                                      
    REMARK 400 COMPOUND                                                             
    REMARK 400  MOLECULAR CHAPERONE HAS ATPASE ACTIVITY                             
    REMARK 465                                                                      
    REMARK 465 MISSING RESIDUES                                                     
    REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
    REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
    REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
    REMARK 465                                                                      
    REMARK 465   M RES C SSSEQI                                                     
    REMARK 465     MET A     1                                                      
    REMARK 465     PRO A     2                                                      
    REMARK 465     GLU A     3                                                      
    REMARK 465     GLU A     4                                                      
    REMARK 465     THR A     5                                                      
    REMARK 465     GLN A     6                                                      
    REMARK 465     THR A     7                                                      
    REMARK 465     GLN A     8                                                      
    REMARK 465     ASP A     9                                                      
    REMARK 465     GLN A    10                                                      
    REMARK 465     PRO A    11                                                      
    REMARK 465     MET A    12                                                      
    REMARK 465     GLU A    13                                                      
    REMARK 465     GLU A    14                                                      
    REMARK 465     GLU A    15                                                      
    REMARK 465     GLU A   225                                                      
    REMARK 465     ARG A   226                                                      
    REMARK 465     ASP A   227                                                      
    REMARK 465     LYS A   228                                                      
    REMARK 465     GLU A   229                                                      
    REMARK 465     VAL A   230                                                      
    REMARK 465     SER A   231                                                      
    REMARK 465     ASP A   232                                                      
    REMARK 465     ASP A   233                                                      
    REMARK 465     GLU A   234                                                      
    REMARK 465     ALA A   235                                                      
    REMARK 465     GLU A   236                                                      
    REMARK 500                                                                      
    REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
    REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
    REMARK 500                                                                      
    REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
    REMARK 500                                                                      
    REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
    REMARK 500   CB   THR A   109  -  O    HOH A  2153              1.61            
    REMARK 500   O    HOH A  2009  -  O    HOH A  2011              1.70            
    REMARK 500   O    HOH A  2030  -  O    HOH A  2076              1.98            
    REMARK 500                                                                      
    REMARK 500 REMARK: NULL                                                         
    REMARK 500                                                                      
    REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
    REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
    REMARK 500                                                                      
    REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
    REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
    REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
    REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
    REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
    REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
    REMARK 500                                                                      
    REMARK 500 DISTANCE CUTOFF:                                                     
    REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
    REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
    REMARK 500                                                                      
    REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
    REMARK 500                                                                      
    REMARK 500   O    HOH A  2003     O    HOH A  2271     8555      2.16           
    REMARK 500   O    HOH A  2030     O    HOH A  2030     2555      2.16           
    REMARK 500   O    HOH A  2078     O    HOH A  2086     2555      2.16           
    REMARK 500   O    HOH A  2110     O    HOH A  2209     8455      2.16           
    REMARK 500                                                                      
    REMARK 500 REMARK: NULL                                                         
    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    ASP A  93   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 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 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    ASP A  66       81.08   -152.11                                   
    REMARK 500    ASN A 105      -61.88   -121.10                                   
    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 800                                                                      
    REMARK 800 SITE                                                                 
    REMARK 800 SITE_IDENTIFIER: AC1                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PU9 A1224                 
    REMARK 900                                                                      
    REMARK 900 RELATED ENTRIES                                                      
    REMARK 900 RELATED ID: 1BYQ   RELATED DB: PDB                                   
    REMARK 900  HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG                             
    REMARK 900 RELATED ID: 1OSF   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90 IN COMPLEX WITH 17-DESMETHOXY-                          
    REMARK 900  17-N,N-DIMETHYLAMINOETHYLAMINO-GELDANAMYCIN                         
    REMARK 900 RELATED ID: 1YER   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN,                            
    REMARK 900  "CLOSED" CONFORMATION                                               
    REMARK 900 RELATED ID: 1YES   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN"                     
    REMARK 900  CONFORMATION                                                        
    REMARK 900 RELATED ID: 1YET   RELATED DB: PDB                                   
    REMARK 900  GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-                       
    REMARK 900  BINDING DOMAIN                                                      
    REMARK 900 RELATED ID: 1UY6   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  9-BUTYL-8-(3,4,5-TRIMETHOXY-BENZYL)-9H-PURIN-6-YLAMINE              
    REMARK 900 RELATED ID: 1UY7   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  9-BUTYL-8-(4-METHOXY-BENZYL)-9H-PURIN-6-YLAMINE                     
    REMARK 900 RELATED ID: 1UY8   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  9-BUTYL-8-(3-TRIMETHOXY-BENZYL)-9H-PURIN-6YLAMINE                   
    REMARK 900 RELATED ID: 1UY9   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  8-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUTYL-                             
    REMARK 900  9H-PURIN-6-YLAMINE                                                  
    REMARK 900 RELATED ID: 1UYC   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  9-BUTYL-8-(2,5-DIMETHOXY-BENZYL)-9H-PURIN-6-YLAMINE                 
    REMARK 900 RELATED ID: 1UYD   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  9-BUTYL-8- (2-CHLORO-3,4,5-TRIMETHOXY-BENZYL)                       
    REMARK 900  -9H-PURIN-6-YLAMINE                                                 
    REMARK 900 RELATED ID: 1UYF   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  8-(2-CHLORO-3,4,5-TRIMETHOXY-BENZYL)                                
    REMARK 900  -2-FLUORO-9-PENT-4-YLNYL-9H-PURIN-6-YLAMINE                         
    REMARK 900 RELATED ID: 1UYG   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  8-(2,5-DIMETHOXY-BENZYL)-2-FLUORO-9H-PURIN-6-YLAMINE                
    REMARK 900 RELATED ID: 1UYH   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  9-BUTYL-8-(2,5-DIMETHOXY-BENZYL)-2-                                 
    REMARK 900  FLUORO-9H-PURIN-6-YLAMINE                                           
    REMARK 900 RELATED ID: 1UYI   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  8-(2,5-DIMETHOXY-BENZYL)-2-FLUORO-9-                                
    REMARK 900  PENT-9H-PURIN-6-YLAMINE                                             
    REMARK 900 RELATED ID: 1UYK   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-ALPHA WITH                                              
    REMARK 900  8-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUTYL                              
    REMARK 900  -2-FLUORO-9H-PURIN-6-YLAMINE                                        
    REMARK 900 RELATED ID: 1UYL   RELATED DB: PDB                                   
    REMARK 900  STRUCTURE-ACTIVITY RELATIONSHIPS IN PURINE-BASED                    
    REMARK 900  INHIBITOR BINDING TO HSP90 ISOFORMS                                 
    REMARK 900 RELATED ID: 1UYM   RELATED DB: PDB                                   
    REMARK 900  HUMAN HSP90-BETA WITH PU3                                           
    REMARK 900  (9-BUTYL-8(3,4,5-TRIMETHOXY-BENZYL)-9H-PURIN-6-YLAMINE)             
    DBREF  1UYE A    1     1  PDB    1UYE     1UYE             1      1             
    DBREF  1UYE A    2   236  UNP    P07900   HS9A_HUMAN       1    235             
    SEQADV 1UYE SER A   63  UNP  P07900    THR    62 CONFLICT                       
    SEQRES   1 A  236  MET PRO GLU GLU THR GLN THR GLN ASP GLN PRO MET GLU          
    SEQRES   2 A  236  GLU GLU GLU VAL GLU THR PHE ALA PHE GLN ALA GLU ILE          
    SEQRES   3 A  236  ALA GLN LEU MET SER LEU ILE ILE ASN THR PHE TYR SER          
    SEQRES   4 A  236  ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE SER ASN SER          
    SEQRES   5 A  236  SER ASP ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR          
    SEQRES   6 A  236  ASP PRO SER LYS LEU ASP SER GLY LYS GLU LEU HIS ILE          
    SEQRES   7 A  236  ASN LEU ILE PRO ASN LYS GLN ASP ARG THR LEU THR ILE          
    SEQRES   8 A  236  VAL ASP THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE          
    SEQRES   9 A  236  ASN ASN LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA          
    SEQRES  10 A  236  PHE MET GLU ALA LEU GLN ALA GLY ALA ASP ILE SER MET          
    SEQRES  11 A  236  ILE GLY GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU          
    SEQRES  12 A  236  VAL ALA GLU LYS VAL THR VAL ILE THR LYS HIS ASN ASP          
    SEQRES  13 A  236  ASP GLU GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER          
    SEQRES  14 A  236  PHE THR VAL ARG THR ASP THR GLY GLU PRO MET GLY ARG          
    SEQRES  15 A  236  GLY THR LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR          
    SEQRES  16 A  236  GLU TYR LEU GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS          
    SEQRES  17 A  236  LYS HIS SER GLN PHE ILE GLY TYR PRO ILE THR LEU PHE          
    SEQRES  18 A  236  VAL GLU LYS GLU ARG ASP LYS GLU VAL SER ASP ASP GLU          
    SEQRES  19 A  236  ALA GLU                                                      
    HET    PU9  A1224      29                                                       
    HETNAM     PU9 8-(2-CHLORO-3,4,5-TRIMETHOXY-BENZYL)-9-PENT-                     
    HETNAM   2 PU9  4-YLNYL-9H-PURIN-6-YLAMINE                                      
    FORMUL   2  PU9    C20 H22 CL N5 O3                                             
    FORMUL   3  HOH   *277(H2 O1)                                                   
    HELIX    1   1 GLN A   23  THR A   36  1                                  14    
    HELIX    2   2 ASN A   40  GLU A   42  5                                   3    
    HELIX    3   3 ILE A   43  ASP A   66  1                                  24    
    HELIX    4   4 PRO A   67  ASP A   71  5                                   5    
    HELIX    5   5 THR A   99  ASN A  105  1                                   7    
    HELIX    6   6 ASN A  105  GLN A  123  1                                  19    
    HELIX    7   7 ASP A  127  GLY A  135  5                                   9    
    HELIX    8   8 VAL A  136  LEU A  143  5                                   8    
    HELIX    9   9 GLU A  192  LEU A  198  5                                   7    
    HELIX   10  10 GLU A  199  SER A  211  1                                  13    
    SHEET    1  AA 8 GLU A  18  ALA A  21  0                                        
    SHEET    2  AA 8 SER A 169  THR A 174 -1  O  PHE A 170   N  PHE A  20           
    SHEET    3  AA 8 GLN A 159  SER A 164 -1  O  ALA A 161   N  ARG A 173           
    SHEET    4  AA 8 ALA A 145  LYS A 153 -1  O  VAL A 148   N  SER A 164           
    SHEET    5  AA 8 GLY A 183  LEU A 190 -1  O  GLY A 183   N  LYS A 153           
    SHEET    6  AA 8 THR A  88  ASP A  93 -1  O  LEU A  89   N  LEU A 188           
    SHEET    7  AA 8 ILE A  78  ASN A  83 -1  O  ASN A  79   N  VAL A  92           
    SHEET    8  AA 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
    CISPEP   1 GLU A  223    LYS A  224          0        21.58                     
    SITE     1 AC1 14 ASN A  51  ALA A  55  ASP A  93  MET A  98                    
    SITE     2 AC1 14 LEU A 107  ALA A 111  GLY A 135  PHE A 138                    
    SITE     3 AC1 14 TYR A 139  TRP A 162  THR A 184  HOH A2275                    
    SITE     4 AC1 14 HOH A2276  HOH A2277                                          
    CRYST1   66.700   90.755   98.171  90.00  90.00  90.00 I 2 2 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      0.014992  0.000000  0.000000        0.00000                         
    SCALE2      0.000000  0.011019  0.000000        0.00000                         
    SCALE3      0.000000  0.000000  0.010186        0.00000                         

    3D molecular view of vibration

    Displacement vectors
    Display
    Animation
    Display

    Still image of displacement vectors and GIF animation


    Mode 1

    Time-average properties and properties of the 10 lowest-frequency modes

    Fluctuation of atoms:
    Time average and for the 3 lowest-frequency modes.
    Fluctuation of dihedral angles:
    Time average and for the 3 lowest-frequency modes.
    Fluctuation of atomsFluctuation of dihedral angles

    Correlations between fluctuations of atoms

    Mode 1
    Correlations between fluctuations of atoms - Mode 1
    Time Average
    Time Average
    Distance map
    Distance map

    Calculation note

    PDB file name : pdb1uye.ent

    Chains and HETATMs selected: 
      ATOM        A

    The following atoms are removed from PDB data on concern that they may have 
    abnormally large fluctuations, because they interact with few atoms.
      ATOM   1506  CG  LYS A 208     -12.643   8.667   4.949  1.00 44.75           C  
      ATOM   1507  CD  LYS A 208     -13.320   9.210   3.683  1.00 52.01           C  
      ATOM   1508  CE  LYS A 208     -14.274   8.159   3.052  1.00 57.03           C  
      ATOM   1509  NZ  LYS A 208     -15.703   8.402   3.480  1.00 60.14           N  

    = Normal mode analysis calculation =

    No. of modes used in the calculation : All modes.

    Parameters of potential energies:
      1-4 and 1-5 non-bonded interactions: E(d) = A*exp(-d(PDB)**2/B**2)(d-d(PDB))**2.
      Loop-closing potential:              E(d) = A*(d-d(PDB))**2.
        for a disulfide bond and one of the bonds in the DNA and RNA sugar ring.
      where d and d(PDB) are distances between atoms in calculation and in PDB data, 
      respectively.

      Interaction type   A       B      Cutoff distance (A)
        1-4             1.00    5.00      100.00
        1-5             1.00    5.00      100.00
        Loop-closing  100.00

    Temperature adjustment by magnitude of fluctuation:
      Set to mean displacements of atoms       0.500 A

    Animation
      No. of frames: 11
      Mean displacements (A):    0.50

    Displacement vector
      Mean length of vectors (A):    3.00