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Database: PDB
Entry: 5J6L
LinkDB: 5J6L
Original site: 5J6L 
HEADER    CHAPERONE                               05-APR-16   5J6L              
TITLE     CRYSTAL STRUCTURE OF HSP90-ALPHA N-DOMAIN IN COMPLEX WITH N-BUTYL-5-  
TITLE    2 [4-(2-FLUORO-PHENYL)-5-OXO-4,5-DIHYDRO-1H-[1,2,4]TRIAZOL-3-YL]-2,4-  
TITLE    3 DIHYDROXY-N-METHYL-BENZAMIDE                                         
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                                                      
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: 562                                         
KEYWDS    COMPLEX STRUCTURE, CHAPERONE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.AMARAL,P.MATIAS                                                     
REVDAT   2   24-JAN-18 5J6L    1       JRNL                                     
REVDAT   1   06-DEC-17 5J6L    0                                                
JRNL        AUTH   M.AMARAL,D.B.KOKH,J.BOMKE,A.WEGENER,H.P.BUCHSTALLER,         
JRNL        AUTH 2 H.M.EGGENWEILER,P.MATIAS,C.SIRRENBERG,R.C.WADE,M.FRECH       
JRNL        TITL   PROTEIN CONFORMATIONAL FLEXIBILITY MODULATES KINETICS AND    
JRNL        TITL 2 THERMODYNAMICS OF DRUG BINDING.                              
JRNL        REF    NAT COMMUN                    V.   8  2276 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29273709                                                     
JRNL        DOI    10.1038/S41467-017-02258-W                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 30717                          
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)  : 0.208                          
REMARK   3   R VALUE            (WORKING SET)  : 0.207                          
REMARK   3   FREE R VALUE                      : 0.226                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1536                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : NULL                     
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.75                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : NULL                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.45                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2770                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.3890                   
REMARK   3   BIN FREE R VALUE                        : 0.4030                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.01                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 146                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1628                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 203                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.23                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.08520                                              
REMARK   3    B22 (A**2) : -2.91410                                             
REMARK   3    B33 (A**2) : 1.82890                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.270               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.109               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.101               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.103               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.097               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 1694   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 2290   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 601    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 46     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 244    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 1694   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 231    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2096   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.99                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.12                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.56                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5J6L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220016.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30736                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.360                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.7500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.930                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1YES                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FLUORIDE 0.1 M BIS TRIS     
REMARK 280  PROPANE PH 8.5 20 % W/V PEG 3350, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 277.15K                                                 
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       33.61050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.01150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       49.77300            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.61050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.01150            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.77300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.61050            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.01150            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       49.77300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.61050            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       45.01150            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.77300            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000      -67.22100            
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     ASP A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     LYS A   224                                                      
REMARK 465     GLU A   225                                                      
REMARK 465     ARG A   226                                                      
REMARK 465     ASP A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     GLU A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     ASP A   232                                                      
REMARK 465     ASP A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  16    CG   CD   OE1  OE2                                  
REMARK 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     -133.37     66.34                                   
REMARK 500    ARG A 182      142.58   -172.16                                   
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 603        DISTANCE =  8.99 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6GC A 301                 
DBREF  5J6L A    9   236  UNP    P07900   HS90A_HUMAN      9    236             
SEQADV 5J6L ALA A  107  UNP  P07900    LEU   107 CONFLICT                       
SEQRES   1 A  228  ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE ALA          
SEQRES   2 A  228  PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE ILE          
SEQRES   3 A  228  ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG GLU          
SEQRES   4 A  228  LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE ARG          
SEQRES   5 A  228  TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER GLY          
SEQRES   6 A  228  LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN ASP          
SEQRES   7 A  228  ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET THR          
SEQRES   8 A  228  LYS ALA ASP LEU ILE ASN ASN ALA GLY THR ILE ALA LYS          
SEQRES   9 A  228  SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA GLY          
SEQRES  10 A  228  ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY PHE          
SEQRES  11 A  228  TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL ILE          
SEQRES  12 A  228  THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU SER          
SEQRES  13 A  228  SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR GLY          
SEQRES  14 A  228  GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS LEU          
SEQRES  15 A  228  LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG ILE          
SEQRES  16 A  228  LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY TYR          
SEQRES  17 A  228  PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP LYS GLU          
SEQRES  18 A  228  VAL SER ASP ASP GLU ALA GLU                                  
HET    6GC  A 301      29                                                       
HETNAM     6GC N-BUTYL-5-[4-(2-FLUOROPHENYL)-5-OXO-4,5-DIHYDRO-1H-1,2,          
HETNAM   2 6GC  4-TRIAZOL-3-YL]-2,4-DIHYDROXY-N-METHYLBENZAMIDE                 
FORMUL   2  6GC    C20 H21 F N4 O4                                              
FORMUL   3  HOH   *203(H2 O)                                                    
HELIX    1 AA1 GLN A   23  THR A   36  1                                  14    
HELIX    2 AA2 GLU A   42  ASP A   66  1                                  25    
HELIX    3 AA3 PRO A   67  ASP A   71  5                                   5    
HELIX    4 AA4 THR A   99  GLY A  108  1                                  10    
HELIX    5 AA5 GLY A  108  GLY A  125  1                                  18    
HELIX    6 AA6 ASP A  127  GLY A  135  5                                   9    
HELIX    7 AA7 VAL A  136  LEU A  143  5                                   8    
HELIX    8 AA8 GLU A  192  LEU A  198  5                                   7    
HELIX    9 AA9 GLU A  199  SER A  211  1                                  13    
SHEET    1 AA1 8 GLU A  18  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  ILE A  91   O  VAL A 186           
SHEET    7 AA1 8 ILE A  78  ASN A  83 -1  N  ILE A  81   O  THR A  90           
SHEET    8 AA1 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
SITE     1 AC1 16 ASN A  51  ALA A  55  LYS A  58  ASP A  93                    
SITE     2 AC1 16 ILE A  96  GLY A  97  MET A  98  ASN A 106                    
SITE     3 AC1 16 PHE A 138  VAL A 150  TRP A 162  THR A 184                    
SITE     4 AC1 16 VAL A 186  HOH A 410  HOH A 462  HOH A 468                    
CRYST1   67.221   90.023   99.546  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      0.014876  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011108  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010046        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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