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Database: PDB
Entry: 5VYY
LinkDB: 5VYY
Original site: 5VYY 
HEADER    CHAPERONE/INHIBITOR                     26-MAY-17   5VYY              
TITLE     STRUCTURE OF HUMAN HSP90-ALPHA BOUND TO RESORCINYLIC INHIBITOR BNIM   
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    CHAPERONE, CHAPERONE-INHIBITOR, CHAPERONE-INHIBITOR COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.S.QUE,D.T.GEWIRTH                                                   
REVDAT   2   25-APR-18 5VYY    1       JRNL                                     
REVDAT   1   18-APR-18 5VYY    0                                                
JRNL        AUTH   N.L.S.QUE,V.M.CROWLEY,A.S.DUERFELDT,J.ZHAO,C.N.KENT,         
JRNL        AUTH 2 B.S.J.BLAGG,D.T.GEWIRTH                                      
JRNL        TITL   STRUCTURE BASED DESIGN OF A GRP94-SELECTIVE INHIBITOR:       
JRNL        TITL 2 EXPLOITING A KEY RESIDUE IN GRP94 TO OPTIMIZE                
JRNL        TITL 3 PARALOG-SELECTIVE BINDING.                                   
JRNL        REF    J. MED. CHEM.                 V.  61  2793 2018              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29528635                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B01608                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 24866                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.5163 -  4.3168    0.98     1719   150  0.1614 0.1674        
REMARK   3     2  4.3168 -  3.4275    1.00     1691   148  0.1551 0.2031        
REMARK   3     3  3.4275 -  2.9945    1.00     1653   145  0.1938 0.2302        
REMARK   3     4  2.9945 -  2.7209    1.00     1655   145  0.2072 0.2513        
REMARK   3     5  2.7209 -  2.5259    1.00     1663   144  0.1959 0.2558        
REMARK   3     6  2.5259 -  2.3770    1.00     1631   144  0.1918 0.2123        
REMARK   3     7  2.3770 -  2.2580    1.00     1629   142  0.1865 0.2328        
REMARK   3     8  2.2580 -  2.1597    1.00     1645   144  0.1893 0.2329        
REMARK   3     9  2.1597 -  2.0766    1.00     1632   143  0.1921 0.2129        
REMARK   3    10  2.0766 -  2.0050    0.99     1625   142  0.1955 0.2328        
REMARK   3    11  2.0050 -  1.9423    1.00     1614   141  0.2069 0.2383        
REMARK   3    12  1.9423 -  1.8868    0.99     1625   142  0.2147 0.2718        
REMARK   3    13  1.8868 -  1.8371    0.99     1598   140  0.2251 0.2667        
REMARK   3    14  1.8371 -  1.7923    0.91     1486   130  0.2681 0.3432        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.640           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.68                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           1697                                  
REMARK   3   ANGLE     :  1.085           2287                                  
REMARK   3   CHIRALITY :  0.056            259                                  
REMARK   3   PLANARITY :  0.006            291                                  
REMARK   3   DIHEDRAL  : 12.807           1019                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VYY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228130.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-12                          
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               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24883                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.11                                           
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000 MME, SODIUM FORMATE, SODIUM     
REMARK 280  CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
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                                         
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       42.63100            
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       42.63100            
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       33.53750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.02750            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.53750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.02750            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       42.63100            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.53750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.02750            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       42.63100            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.53750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       46.02750            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -42.63100            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 NA    NA A 306  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     LYS A   224                                                      
REMARK 465     GLU A   225                                                      
REMARK 465     ARG A   226                                                      
REMARK 465     ASP A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     GLU A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     ASP A   232                                                      
REMARK 465     ASP A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 112    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  38      127.41    -37.10                                   
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 305  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A  27   O                                                      
REMARK 620 2 SER A  31   OG   70.4                                              
REMARK 620 3 HOH A 404   O   118.6  58.0                                        
REMARK 620 4 HOH A 477   O   110.8 161.8 109.1                                  
REMARK 620 5 HOH A 544   O   115.4  92.7  98.8 102.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 306  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 193   O                                                      
REMARK 620 2 HOH A 428   O   116.5                                              
REMARK 620 3 ASP A 193   O     0.0 116.5                                        
REMARK 620 4 HOH A 428   O   130.4  72.5 130.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9QY A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 306                  
DBREF  5VYY A    1   236  UNP    P07900   HS90A_HUMAN    123    358             
SEQADV 5VYY MET A  -19  UNP  P07900              INITIATING METHIONINE          
SEQADV 5VYY GLY A  -18  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY SER A  -17  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY SER A  -16  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY HIS A  -15  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY HIS A  -14  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY HIS A  -13  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY HIS A  -12  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY HIS A  -11  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY HIS A  -10  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY SER A   -9  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY SER A   -8  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY GLY A   -7  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY LEU A   -6  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY VAL A   -5  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY PRO A   -4  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY ARG A   -3  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY GLY A   -2  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY SER A   -1  UNP  P07900              EXPRESSION TAG                 
SEQADV 5VYY HIS A    0  UNP  P07900              EXPRESSION TAG                 
SEQRES   1 A  256  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  256  LEU VAL PRO ARG GLY SER HIS MET PRO GLU GLU THR GLN          
SEQRES   3 A  256  THR GLN ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR          
SEQRES   4 A  256  PHE ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU          
SEQRES   5 A  256  ILE ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU          
SEQRES   6 A  256  ARG GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS          
SEQRES   7 A  256  ILE ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP          
SEQRES   8 A  256  SER GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS          
SEQRES   9 A  256  GLN ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY          
SEQRES  10 A  256  MET THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE          
SEQRES  11 A  256  ALA LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN          
SEQRES  12 A  256  ALA GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL          
SEQRES  13 A  256  GLY PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR          
SEQRES  14 A  256  VAL ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP          
SEQRES  15 A  256  GLU SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP          
SEQRES  16 A  256  THR GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU          
SEQRES  17 A  256  HIS LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG          
SEQRES  18 A  256  ARG ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE          
SEQRES  19 A  256  GLY TYR PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP          
SEQRES  20 A  256  LYS GLU VAL SER ASP ASP GLU ALA GLU                          
HET    9QY  A 301      46                                                       
HET    FMT  A 302       5                                                       
HET    FMT  A 303       5                                                       
HET    EDO  A 304      10                                                       
HET     MG  A 305       1                                                       
HET     NA  A 306       1                                                       
HETNAM     9QY METHYL 2-[2-(1-BENZYL-1H-IMIDAZOL-2-YL)ETHYL]-3-CHLORO-          
HETNAM   2 9QY  4,6-DIHYDROXYBENZOATE                                           
HETNAM     FMT FORMIC ACID                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETSYN     9QY RESORCINYLIC INHIBITOR BNIM                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  9QY    C20 H19 CL N2 O4                                             
FORMUL   3  FMT    2(C H2 O2)                                                   
FORMUL   5  EDO    C2 H6 O2                                                     
FORMUL   6   MG    MG 2+                                                        
FORMUL   7   NA    NA 1+                                                        
FORMUL   8  HOH   *165(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  ASN A  106  1                                   8    
HELIX    5 AA5 GLY A  108  ALA A  124  1                                  17    
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 GLN A  194  LEU A  198  5                                   5    
HELIX    9 AA9 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  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           
LINK         O   ALA A  27                MG    MG A 305     1555   1555  2.83  
LINK         OG  SER A  31                MG    MG A 305     1555   1555  2.91  
LINK         O   ASP A 193                NA    NA A 306     1555   1555  2.53  
LINK        MG    MG A 305                 O   HOH A 404     1555   1555  2.70  
LINK        MG    MG A 305                 O   HOH A 477     1555   1555  2.61  
LINK        NA    NA A 306                 O   HOH A 428     1555   1555  2.58  
LINK         O   ASP A 193                NA    NA A 306     1555   3554  2.53  
LINK        MG    MG A 305                 O   HOH A 544     1555   8545  2.71  
LINK        NA    NA A 306                 O   HOH A 428     1555   3554  2.58  
SITE     1 AC1 11 ASN A  51  ALA A  55  ASP A  93  MET A  98                    
SITE     2 AC1 11 ASN A 106  PHE A 138  THR A 184  VAL A 186                    
SITE     3 AC1 11 HOH A 427  HOH A 431  HOH A 451                               
SITE     1 AC2  8 ASN A  51  GLY A 135  VAL A 136  GLY A 137                    
SITE     2 AC2  8 PHE A 138  HOH A 439  HOH A 503  HOH A 523                    
SITE     1 AC3  3 ASN A  35  THR A  36  HOH A 511                               
SITE     1 AC4  3 GLN A  85  GLU A 223  HOH A 528                               
SITE     1 AC5  6 ALA A  27  SER A  31  ALA A 166  HOH A 404                    
SITE     2 AC5  6 HOH A 477  HOH A 544                                          
SITE     1 AC6  3 ASP A 193  GLN A 194  HOH A 428                               
CRYST1   67.075   92.055   85.262  90.00  90.00  90.00 C 2 2 21      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      0.014909  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010863  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011729        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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