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Database: PDB
Entry: 4CWN
LinkDB: 4CWN
Original site: 4CWN 
HEADER    CHAPERONE                               03-APR-14   4CWN              
TITLE     HUMAN HSP90 ALPHA N-TERMINAL DOMAIN IN COMPLEX WITH AN                
TITLE    2 AMINOTRIAZOLOQUINAZOLINE INHIBITOR                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 9-236;                         
COMPND   5 SYNONYM: HEAT SHOCK 86 KDA, HSP 86, HSP86, RENAL CARCINOMA ANTIGEN   
COMPND   6 NY-REN-38;                                                           
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET15                                      
KEYWDS    CHAPERONE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.CASALE,N.AMBOLDI,G.BRASCA,D.CARONNI,N.COLOMBO,C.DALVIT,E.R.FELDER,  
AUTHOR   2 G.FOGLIATTO,A.ISACCHI,S.MANTEGANI,P.POLUCCI,L.RICEPUTI,F.SOLA,       
AUTHOR   3 C.VISCO,F.ZUCCOTTO,F.CASUSCELLI                                      
REVDAT   3   28-JUN-17 4CWN    1       REMARK                                   
REVDAT   2   06-AUG-14 4CWN    1       JRNL                                     
REVDAT   1   09-JUL-14 4CWN    0                                                
JRNL        AUTH   E.CASALE,N.AMBOLDI,M.G.BRASCA,D.CARONNI,N.COLOMBO,C.DALVIT,  
JRNL        AUTH 2 E.R.FELDER,G.FOGLIATTO,A.GALVANI,A.ISACCHI,P.POLUCCI,        
JRNL        AUTH 3 L.RICEPUTI,F.SOLA,C.VISCO,F.ZUCCOTTO,F.CASUSCELLI            
JRNL        TITL   FRAGMENT-BASED HIT DISCOVERY AND STRUCTURE-BASED             
JRNL        TITL 2 OPTIMIZATION OF AMINOTRIAZOLOQUINAZOLINES AS NOVEL HSP90     
JRNL        TITL 3 INHIBITORS.                                                  
JRNL        REF    BIOORG.MED.CHEM.              V.  22  4135 2014              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   24980703                                                     
JRNL        DOI    10.1016/J.BMC.2014.05.056                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 26676                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1416                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1780                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.3770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1626                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 193                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.45000                                             
REMARK   3    B22 (A**2) : 0.43000                                              
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): 0.113         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.110         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.043         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1680 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2268 ; 1.262 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   206 ; 5.497 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    74 ;33.015 ;25.135       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   306 ;12.251 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;19.287 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   257 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1239 ; 0.004 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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   : 1.40                                          
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 4CWN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290060235.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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 MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28100                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       33.58950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.35600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       49.61600            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.58950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.35600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.61600            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.58950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.35600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       49.61600            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.58950            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       45.35600            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.61600            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.8 KCAL/MOL                         
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     GLY A     7                                                      
REMARK 465     PRO 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    16                                                      
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 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 166     -143.05     64.02                                   
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 6LV A 1224                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CWF   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90 ALPHA N-TERMINAL DOMAIN IN COMPLEX WITH AN               
REMARK 900 AMINOTRIAZOLOQUINAZOLINE INHIBITOR                                   
REMARK 900 RELATED ID: 4CWO   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90 ALPHA N-TERMINAL DOMAIN IN COMPLEX WITH AN               
REMARK 900 AMINOTRIAZOLOQUINAZOLINE INHIBITOR                                   
REMARK 900 RELATED ID: 4CWP   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90 ALPHA N-TERMINAL DOMAIN IN COMPLEX WITH AN               
REMARK 900 AMINOTRIAZOLOQUINAZOLINE INHIBITOR                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST TWO RESIDUES  GP  ARE EXPRESSION  TAG                      
DBREF  4CWN A    9   236  UNP    P07900   HS90A_HUMAN      9    236             
SEQADV 4CWN GLY A    7  UNP  P07900              EXPRESSION TAG                 
SEQADV 4CWN PRO A    8  UNP  P07900              EXPRESSION TAG                 
SEQRES   1 A  230  GLY PRO ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR          
SEQRES   2 A  230  PHE ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU          
SEQRES   3 A  230  ILE ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU          
SEQRES   4 A  230  ARG GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS          
SEQRES   5 A  230  ILE ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP          
SEQRES   6 A  230  SER GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS          
SEQRES   7 A  230  GLN ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY          
SEQRES   8 A  230  MET THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE          
SEQRES   9 A  230  ALA LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN          
SEQRES  10 A  230  ALA GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL          
SEQRES  11 A  230  GLY PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR          
SEQRES  12 A  230  VAL ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP          
SEQRES  13 A  230  GLU SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP          
SEQRES  14 A  230  THR GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU          
SEQRES  15 A  230  HIS LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG          
SEQRES  16 A  230  ARG ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE          
SEQRES  17 A  230  GLY TYR PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP          
SEQRES  18 A  230  LYS GLU VAL SER ASP ASP GLU ALA GLU                          
HET    6LV  A1224      25                                                       
HETNAM     6LV 5-(3,5-DIMETHOXYBENZYL)[1,2,4]TRIAZOLO[1,5-                      
HETNAM   2 6LV  C]QUINAZOLIN-2-AMINE                                            
FORMUL   2  6LV    C18 H17 N5 O2                                                
FORMUL   3  HOH   *193(H2 O)                                                    
HELIX    1   1 GLN A   23  THR A   36  1                                  14    
HELIX    2   2 GLU A   42  LEU A   64  1                                  23    
HELIX    3   3 ASP A   66  ASP A   71  5                                   6    
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  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           
SITE     1 AC1 14 ASN A  51  ALA A  55  ASP A  93  ILE A  96                    
SITE     2 AC1 14 GLY A  97  MET A  98  LEU A 107  PHE A 138                    
SITE     3 AC1 14 TYR A 139  VAL A 150  TRP A 162  HOH A2058                    
SITE     4 AC1 14 HOH A2105  HOH A2193                                          
CRYST1   67.179   90.712   99.232  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      0.014886  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011024  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010077        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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