GenomeNet

Database: PDB
Entry: 3O0I
LinkDB: 3O0I
Original site: 3O0I 
HEADER    CHAPERONE/INHIBITOR                     19-JUL-10   3O0I              
TITLE     STRUCTURE OF THE HUMAN HSP90-ALPHA N-DOMAIN BOUND TO THE HSP90        
TITLE    2 INHIBITOR PU-H54                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HSP90AA1 PROTEIN;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN RESIDUES 1-236;                          
COMPND   5 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;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21DE3                                    
KEYWDS    HSP90 HEAT-SHOCK PROTEINS, CHAPERONE-INHIBITOR COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.M.SEIDLER,D.T.GEWIRTH                                               
REVDAT   3   20-NOV-13 3O0I    1       JRNL                                     
REVDAT   2   11-SEP-13 3O0I    1       JRNL                                     
REVDAT   1   05-OCT-11 3O0I    0                                                
JRNL        AUTH   P.D.PATEL,P.YAN,P.M.SEIDLER,H.J.PATEL,W.SUN,C.YANG,N.S.QUE,  
JRNL        AUTH 2 T.TALDONE,P.FINOTTI,R.A.STEPHANI,D.T.GEWIRTH,G.CHIOSIS       
JRNL        TITL   PARALOG-SELECTIVE HSP90 INHIBITORS DEFINE TUMOR-SPECIFIC     
JRNL        TITL 2 REGULATION OF HER2.                                          
JRNL        REF    NAT.CHEM.BIOL.                V.   9   677 2013              
JRNL        REFN                   ISSN 1552-4450                               
JRNL        PMID   23995768                                                     
JRNL        DOI    10.1038/NCHEMBIO.1335                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.47 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 46912                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2492                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.47                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.51                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2612                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 159                          
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1611                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 267                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.069         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.071         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.042         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.063         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1664 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2249 ; 1.104 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   207 ; 5.410 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    70 ;32.372 ;24.857       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   294 ;10.274 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;16.620 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   258 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1225 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1028 ; 0.468 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1655 ; 0.904 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   636 ; 1.304 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   594 ; 2.216 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3O0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060510.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : .9793                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49404                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.470                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.03900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 58.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5-FOLD MOLAR EXCESS PU-H54 LIGAND, 12-   
REMARK 280  16% PEG-2KMME, 225-300 MM MGCL2, SODIUM CACODYLATE, PH 6.5, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
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       33.35550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.44050            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       49.30150            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.35550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.44050            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.30150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.35550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.44050            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       49.30150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.35550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       45.44050            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.30150            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
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     LYS A   224                                                      
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  16    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     GLU A 120    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 123    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 178    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 192    CG   CD   OE1  OE2                                  
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    TYR A  38      111.16   -162.53                                   
REMARK 500    ALA A 166     -146.92     61.76                                   
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 P54 A 237                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3C11   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE N-DOMAIN OF GRP94 BOUND TO THE HSP90                
REMARK 900 INHIBITOR PU-H54                                                     
DBREF  3O0I A    1   236  UNP    Q2VPJ6   Q2VPJ6_HUMAN     1    236             
SEQADV 3O0I MET A  -19  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I GLY A  -18  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I SER A  -17  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I SER A  -16  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I HIS A  -15  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I HIS A  -14  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I HIS A  -13  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I HIS A  -12  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I HIS A  -11  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I HIS A  -10  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I SER A   -9  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I SER A   -8  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I GLY A   -7  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I LEU A   -6  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I VAL A   -5  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I PRO A   -4  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I ARG A   -3  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I GLY A   -2  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I SER A   -1  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQADV 3O0I HIS A    0  UNP  Q2VPJ6              EXPRESSION TAG                 
SEQRES   1 A  256  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  256  LEU VAL PRO ARG GLY SER HIS MET PRO GLU GLU THR GLN          
SEQRES   3 A  256  THR GLN ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR          
SEQRES   4 A  256  PHE ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU          
SEQRES   5 A  256  ILE ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU          
SEQRES   6 A  256  ARG GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS          
SEQRES   7 A  256  ILE ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP          
SEQRES   8 A  256  SER GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS          
SEQRES   9 A  256  GLN ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY          
SEQRES  10 A  256  MET THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE          
SEQRES  11 A  256  ALA LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN          
SEQRES  12 A  256  ALA GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL          
SEQRES  13 A  256  GLY PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR          
SEQRES  14 A  256  VAL ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP          
SEQRES  15 A  256  GLU SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP          
SEQRES  16 A  256  THR GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU          
SEQRES  17 A  256  HIS LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG          
SEQRES  18 A  256  ARG ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE          
SEQRES  19 A  256  GLY TYR PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP          
SEQRES  20 A  256  LYS GLU VAL SER ASP ASP GLU ALA GLU                          
HET    P54  A 237      29                                                       
HETNAM     P54 8-[(2,4-DIMETHYLPHENYL)SULFANYL]-3-PENT-4-YN-1-YL-3H-            
HETNAM   2 P54  PURIN-6-AMINE                                                   
FORMUL   2  P54    C18 H19 N5 S                                                 
FORMUL   3  HOH   *267(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  ASN A  105  1                                   7    
HELIX    5   5 ASN A  105  ALA A  124  1                                  20    
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    
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  LEU A  89   O  LEU A 188           
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           
SITE     1 AC1 10 ASN A  51  ALA A  55  ASP A  93  MET A  98                    
SITE     2 AC1 10 PHE A 138  TRP A 162  THR A 184  HOH A 272                    
SITE     3 AC1 10 HOH A 284  HOH A 312                                          
CRYST1   66.711   90.881   98.603  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      0.014990  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011003  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010142        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system