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Database: PDB
Entry: 6GPH
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HEADER    CHAPERONE                               05-JUN-18   6GPH              
TITLE     STRUCTURE OF HUMAN HEAT SHOCK PROTEIN 90-ALPHA N-TERMINAL DOMAIN      
TITLE    2 (HSP90-NTD) VARIANT K112A 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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    CHAPERONE, HSP90, NTD, ALPHA, K112A, COMPLEX, AMPCP, NUCLEOTIDE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.TASSONE,C.POZZI,S.MANGANI,M.BOTTA                                   
REVDAT   2   10-OCT-18 6GPH    1       COMPND JRNL                              
REVDAT   1   03-OCT-18 6GPH    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.    1.56 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 : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 30562                          
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1544                            
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) : 1.56                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.60                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2234                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 131                          
REMARK   3   BIN FREE R VALUE                    : 0.2480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1813                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 310                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.083         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.084         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.055         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.806         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
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):  1937 ; 0.016 ; 0.012       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2637 ; 2.160 ; 1.662       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   250 ; 6.704 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    95 ;36.731 ;23.789       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   345 ;11.015 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;23.606 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   271 ; 0.140 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1445 ; 0.014 ; 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):   967 ; 1.184 ; 1.183       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1219 ; 1.809 ; 1.771       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   970 ; 1.715 ; 1.321       
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):  2894 ; 4.601 ;17.379       
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    -6        A   226                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0750   0.9871  14.8160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0180 T22:   0.0072                                     
REMARK   3      T33:   0.0347 T12:   0.0018                                     
REMARK   3      T13:  -0.0235 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0807 L22:   0.0075                                     
REMARK   3      L33:   0.3917 L12:   0.0047                                     
REMARK   3      L13:   0.0109 L23:   0.0433                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0053 S12:   0.0233 S13:   0.0090                       
REMARK   3      S21:   0.0086 S22:  -0.0004 S23:  -0.0093                       
REMARK   3      S31:   0.0160 S32:  -0.0110 S33:  -0.0048                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 6GPH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010355.                                   
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) : 0.976220                           
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   : 32122                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.220                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37700                            
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   (%): 43.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PRECIPITANT: 25 % WT/VOL PEG 2000,2      
REMARK 280  200MM MGCL2, 100 MM SODIUM CACODYLATE, PH 6.5 SAMPLE: HSP90A-NTD    
REMARK 280  K112A 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       21.20000            
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: 910 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 13340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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     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     LEU A  -6    CG   CD1  CD2                                       
REMARK 470     LYS A  69    CG   CD   CE   NZ                                   
REMARK 470     LYS A 100    NZ                                                  
REMARK 470     LYS A 116    NZ                                                  
REMARK 470     GLU A 178    CD   OE1  OE2                                       
REMARK 470     GLU A 192    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 209    NZ                                                  
REMARK 470     LYS A 224    CD   CE   NZ                                        
REMARK 470     GLU A 225    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    ASP A  66       84.53   -156.30                                   
REMARK 500    ALA A 166     -153.15     68.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  51   OD1                                                    
REMARK 620 2 A12 A 301   O2B  96.1                                              
REMARK 620 3 A12 A 301   O1A  92.7  91.6                                        
REMARK 620 4 HOH A 585   O   171.0  91.3  92.2                                  
REMARK 620 5 HOH A 447   O    87.0 174.0  93.4  85.1                            
REMARK 620 6 HOH A 472   O    84.8  85.5 175.9  90.7  89.7                      
REMARK 620 N                    1     2     3     4     5                       
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 HOH A 410   O                                                      
REMARK 620 2 HOH A 704   O    83.3                                              
REMARK 620 3 HOH A 434   O    88.4  91.8                                        
REMARK 620 4 HOH A 497   O    91.7 170.8  80.3                                  
REMARK 620 5 HOH A 492   O   172.8  96.7  98.9  89.2                            
REMARK 620 6 HOH A 522   O    84.7  93.0 171.0  94.2  88.1                      
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: 6GP8   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN HEAT SHOCK PROTEIN 90-ALPHA N-TERMINAL DOMAIN     
REMARK 900 (HSP90-NTD) VARIANT K112A IN COMPLEX AMPCPP                          
REMARK 900 RELATED ID: 6GPF   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN HEAT SHOCK PROTEIN 90-ALPHA N-TERMINAL DOMAIN     
REMARK 900 (HSP90-NTD) VARIANT K112A IN COMPLEX WITH AMPPNP                     
DBREF  6GPH A    1   236  UNP    P07900   HS90A_HUMAN      1    236             
SEQADV 6GPH MET A  -19  UNP  P07900              INITIATING METHIONINE          
SEQADV 6GPH GLY A  -18  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH SER A  -17  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH SER A  -16  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH HIS A  -15  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH HIS A  -14  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH HIS A  -13  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH HIS A  -12  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH HIS A  -11  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH HIS A  -10  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH SER A   -9  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH SER A   -8  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH GLY A   -7  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH LEU A   -6  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH VAL A   -5  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH PRO A   -4  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH ARG A   -3  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH GLY A   -2  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH SER A   -1  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH HIS A    0  UNP  P07900              EXPRESSION TAG                 
SEQADV 6GPH ALA 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 ALA 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   *310(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 ASN A   40  GLU A   42  5                                   3    
HELIX    4 AA4 ILE A   43  SER A   63  1                                  21    
HELIX    5 AA5 LEU A   64  THR A   65  5                                   2    
HELIX    6 AA6 ASP A   66  SER A   72  5                                   7    
HELIX    7 AA7 THR A   99  LEU A  107  1                                   9    
HELIX    8 AA8 GLY A  114  ALA A  124  1                                  11    
HELIX    9 AA9 ASP A  127  GLY A  135  5                                   9    
HELIX   10 AB1 VAL A  136  LEU A  143  5                                   8    
HELIX   11 AB2 GLU A  192  LEU A  198  5                                   7    
HELIX   12 AB3 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 302     1555   1555  2.06  
LINK         O2B A12 A 301                MG    MG A 302     1555   1555  2.00  
LINK         O1A A12 A 301                MG    MG A 302     1555   1555  1.91  
LINK        MG    MG A 302                 O   HOH A 585     1555   1555  2.19  
LINK        MG    MG A 302                 O   HOH A 447     1555   1555  2.09  
LINK        MG    MG A 302                 O   HOH A 472     1555   1555  2.20  
LINK        MG    MG A 303                 O   HOH A 410     1555   1555  2.16  
LINK        MG    MG A 303                 O   HOH A 704     1555   1555  2.10  
LINK        MG    MG A 303                 O   HOH A 434     1555   1555  2.11  
LINK        MG    MG A 303                 O   HOH A 497     1555   1555  2.11  
LINK        MG    MG A 303                 O   HOH A 492     1555   2656  1.89  
LINK        MG    MG A 303                 O   HOH A 522     1555   2555  2.15  
SITE     1 AC1 27 SER A  -1  MET A   1  ASN A  51  ALA A  55                    
SITE     2 AC1 27 ASP A  93  MET A  98  ASN A 106  LEU A 107                    
SITE     3 AC1 27 GLY A 135  VAL A 136  GLY A 137  PHE A 138                    
SITE     4 AC1 27 THR A 184   MG A 302  HOH A 407  HOH A 432                    
SITE     5 AC1 27 HOH A 447  HOH A 461  HOH A 470  HOH A 472                    
SITE     6 AC1 27 HOH A 476  HOH A 510  HOH A 529  HOH A 538                    
SITE     7 AC1 27 HOH A 585  HOH A 598  HOH A 600                               
SITE     1 AC2  5 ASN A  51  A12 A 301  HOH A 447  HOH A 472                    
SITE     2 AC2  5 HOH A 585                                                     
SITE     1 AC3  4 HOH A 410  HOH A 434  HOH A 497  HOH A 704                    
CRYST1   54.348   42.400   55.020  90.00 116.54  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      0.018400  0.000000  0.009192        0.00000                         
SCALE2      0.000000  0.023585  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020317        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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