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Database: PDB
Entry: 6GQS
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HEADER    CHAPERONE                               08-JUN-18   6GQS              
TITLE     STRUCTURE OF HUMAN HEAT SHOCK PROTEIN 90-ALPHA N-TERMINAL DOMAIN      
TITLE    2 (HSP90-NTD) VARIANT K112R IN COMPLEX WITH AMPCP                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HEAT SHOCK 86 KDA,HSP86,LIPOPOLYSACCHARIDE-ASSOCIATED       
COMPND   5 PROTEIN 2,LPS-ASSOCIATED PROTEIN 2,RENAL CARCINOMA ANTIGEN NY-REN-38;
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HSP90AA1, HSP90A, HSPC1, HSPCA;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    CHAPERONE, HSP90, NTD, ALPHA, K112R, COMPLEX, NUCLEOTIDE, AMPCP       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.TASSONE,C.POZZI,S.MANGANI,M.BOTTA                                   
REVDAT   2   10-OCT-18 6GQS    1       COMPND JRNL                              
REVDAT   1   03-OCT-18 6GQS    0                                                
JRNL        AUTH   G.TASSONE,S.MANGANI,M.BOTTA,C.POZZI                          
JRNL        TITL   PROBING THE ROLE OF ARG97 IN HEAT SHOCK PROTEIN 90           
JRNL        TITL 2 N-TERMINAL DOMAIN FROM THE PARASITE LEISHMANIA BRAZILIENSIS  
JRNL        TITL 3 THROUGH SITE-DIRECTED MUTAGENESIS ON THE HUMAN COUNTERPART.  
JRNL        REF    BIOCHIM BIOPHYS ACTA          V.1866  1190 2018              
JRNL        REF  2 PROTEINS PROTEOM                                             
JRNL        REFN                   ISSN 1878-1454                               
JRNL        PMID   30248409                                                     
JRNL        DOI    10.1016/J.BBAPAP.2018.09.005                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.43 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0222                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 38537                          
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2091                            
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) : 1.43                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.47                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2856                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 154                          
REMARK   3   BIN FREE R VALUE                    : 0.2760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1826                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 357                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.01000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.067         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.067         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.045         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.122         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2043 ; 0.011 ; 0.012       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2795 ; 1.849 ; 1.663       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   276 ; 6.715 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   108 ;36.982 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   380 ;11.772 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;24.265 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   286 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1537 ; 0.011 ; 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):   994 ; 1.026 ; 1.201       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1255 ; 1.633 ; 1.798       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1049 ; 1.435 ; 1.328       
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):  3271 ; 5.161 ;18.098       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -5        A   227                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9417   1.1382  14.5131              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0273 T22:   0.0111                                     
REMARK   3      T33:   0.0151 T12:   0.0024                                     
REMARK   3      T13:  -0.0184 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0975 L22:   0.0197                                     
REMARK   3      L33:   0.4708 L12:  -0.0016                                     
REMARK   3      L13:   0.0411 L23:   0.0830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0161 S12:   0.0286 S13:   0.0046                       
REMARK   3      S21:   0.0105 S22:  -0.0066 S23:  -0.0102                       
REMARK   3      S31:   0.0094 S32:  -0.0222 S33:  -0.0095                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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: NULL                                      
REMARK   4                                                                      
REMARK   4 6GQS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010414.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-FEB-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97622                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40642                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
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: 2XK2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PRECIPITANT: 25 % WT/VOL PEG 2000,       
REMARK 280  200MM MGCL2, 100 MM SODIUM CACODYLATE, PH 6.5 SAMPLE: HSP90A-NTD    
REMARK 280  K112R 20 MG/ML, 10 MM AMPCP, 500 MM NACL, 20 MM TRIS, PH 7.5,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       21.08650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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 TOTAL BURIED SURFACE AREA: 950 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 13080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 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     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  14    CD   OE1  OE2                                       
REMARK 470     GLU A 178    CD   OE1  OE2                                       
REMARK 470     LYS A 209    CE   NZ                                             
REMARK 470     LYS A 224    CE   NZ                                             
REMARK 470     GLU A 225    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 227    CG   OD1  OD2                                       
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    ASN A  40       38.21     72.13                                   
REMARK 500    ASN A  40       51.50   -115.54                                   
REMARK 500    ALA A 166     -151.43     65.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  60         0.10    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 757        DISTANCE =  6.05 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  51   OD1                                                    
REMARK 620 2 A12 A 301   O3B  96.3                                              
REMARK 620 3 A12 A 301   O1A  91.5  89.4                                        
REMARK 620 4 HOH A 452   O   162.7  81.6 105.6                                  
REMARK 620 5 HOH A 452   O   163.0  99.9  83.4  29.0                            
REMARK 620 6 HOH A 467   O    87.2 175.0  94.2  94.0  77.1                      
REMARK 620 7 HOH A 480   O    80.7  85.9 170.4  82.1 105.7  91.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 462   O                                                      
REMARK 620 2 HOH A 579   O    88.6                                              
REMARK 620 3 HOH A 468   O    78.8 111.5                                        
REMARK 620 4 HOH A 457   O   169.9  86.3  95.0                                  
REMARK 620 5 HOH A 705   O    90.0  67.2 168.7  96.1                            
REMARK 620 6 HOH A 485   O   100.7 159.7  88.1  86.9  94.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue A12 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 303                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6GP4   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN HEAT SHOCK PROTEIN 90-ALPHA N-TERMINAL DOMAIN     
REMARK 900 (HSP90-NTD) VARIANT K112A                                            
REMARK 900 RELATED ID: 6GPW   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN HEAT SHOCK PROTEIN 90-ALPHA N-TERMINAL DOMAIN     
REMARK 900 (HSP90-NTD)                                                          
DBREF  6GQS A    1   236  UNP    P07900   HS90A_HUMAN      1    236             
SEQADV 6GQS MET A  -19  UNP  P07900              INITIATING METHIONINE          
SEQADV 6GQS GLY A  -18  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS SER A  -17  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS SER A  -16  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS HIS A  -15  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS HIS A  -14  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS HIS A  -13  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS HIS A  -12  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS HIS A  -11  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS HIS A  -10  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS SER A   -9  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS SER A   -8  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS GLY A   -7  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS LEU A   -6  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS VAL A   -5  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS PRO A   -4  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS ARG A   -3  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS GLY A   -2  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS SER A   -1  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS HIS A    0  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GQS ARG A  112  UNP  P07900    LYS   112 ENGINEERED MUTATION            
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 ARG 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    A12  A 301      27                                                       
HET     MG  A 302       1                                                       
HET     MG  A 303       1                                                       
HETNAM     A12 PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     A12 ALPHA,BETA-METHYLENEADENOSINE-5'-DIPHOSPHATE                     
FORMUL   2  A12    C11 H17 N5 O9 P2                                             
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  HOH   *357(H2 O)                                                    
HELIX    1 AA1 MET A    1  GLN A    6  1                                   6    
HELIX    2 AA2 GLN A   23  ASN A   35  1                                  13    
HELIX    3 AA3 GLU A   42  SER A   63  1                                  22    
HELIX    4 AA4 LEU A   64  THR A   65  5                                   2    
HELIX    5 AA5 ASP A   66  SER A   72  5                                   7    
HELIX    6 AA6 THR A   99  LEU A  107  1                                   9    
HELIX    7 AA7 GLY A  114  ALA A  124  1                                  11    
HELIX    8 AA8 ASP A  127  GLY A  135  5                                   9    
HELIX    9 AA9 VAL A  136  LEU A  143  5                                   8    
HELIX   10 AB1 GLU A  192  LEU A  198  5                                   7    
HELIX   11 AB2 GLU A  199  SER A  211  1                                  13    
SHEET    1 AA1 8 VAL A  17  ALA A  21  0                                        
SHEET    2 AA1 8 SER A 169  THR A 174 -1  O  PHE A 170   N  PHE A  20           
SHEET    3 AA1 8 TYR A 160  SER A 164 -1  N  ALA A 161   O  ARG A 173           
SHEET    4 AA1 8 ALA A 145  LYS A 153 -1  N  VAL A 150   O  TRP A 162           
SHEET    5 AA1 8 GLY A 183  LEU A 190 -1  O  ILE A 187   N  THR A 149           
SHEET    6 AA1 8 THR A  88  ASP A  93 -1  N  LEU A  89   O  LEU A 188           
SHEET    7 AA1 8 ILE A  78  ASN A  83 -1  N  ASN A  83   O  THR A  88           
SHEET    8 AA1 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
LINK         OD1 ASN A  51                MG    MG A 303     1555   1555  2.06  
LINK         O3B A12 A 301                MG    MG A 303     1555   1555  2.02  
LINK         O1A A12 A 301                MG    MG A 303     1555   1555  2.01  
LINK        MG    MG A 302                 O   HOH A 462     1555   1555  2.13  
LINK        MG    MG A 302                 O   HOH A 579     1555   1555  2.74  
LINK        MG    MG A 302                 O   HOH A 468     1555   1555  2.03  
LINK        MG    MG A 303                 O  AHOH A 452     1555   1555  2.00  
LINK        MG    MG A 303                 O  BHOH A 452     1555   1555  2.34  
LINK        MG    MG A 303                 O   HOH A 467     1555   1555  2.06  
LINK        MG    MG A 303                 O   HOH A 480     1555   1555  2.35  
LINK        MG    MG A 302                 O   HOH A 457     1555   2556  2.17  
LINK        MG    MG A 302                 O   HOH A 705     1555   2556  2.22  
LINK        MG    MG A 302                 O   HOH A 485     1555   2556  2.00  
SITE     1 AC1 26 ASN A  51  ALA A  55  ASP A  93  MET A  98                    
SITE     2 AC1 26 ASN A 106  LEU A 107  ARG A 112  GLY A 135                    
SITE     3 AC1 26 VAL A 136  GLY A 137  PHE A 138  THR A 184                    
SITE     4 AC1 26  MG A 303  HOH A 406  HOH A 424  HOH A 450                    
SITE     5 AC1 26 HOH A 452  HOH A 456  HOH A 461  HOH A 467                    
SITE     6 AC1 26 HOH A 480  HOH A 481  HOH A 527  HOH A 536                    
SITE     7 AC1 26 HOH A 572  HOH A 634                                          
SITE     1 AC2  3 HOH A 462  HOH A 468  HOH A 579                               
SITE     1 AC3  5 ASN A  51  A12 A 301  HOH A 452  HOH A 467                    
SITE     2 AC3  5 HOH A 480                                                     
CRYST1   53.791   42.173   54.572  90.00 116.61  90.00 P 1 21 1      2          
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      0.018590  0.000000  0.009314        0.00000                         
SCALE2      0.000000  0.023712  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020496        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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