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Database: PDB
Entry: 1BYQ
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Original site: 1BYQ 
HEADER    CHAPERONE                               19-OCT-98   1BYQ              
TITLE     HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (HEAT SHOCK PROTEIN 90);                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 9 - 236;                                          
COMPND   5 SYNONYM: HSP90;                                                      
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET3D                                     
KEYWDS    CHAPERONE PROTEIN, ATP BINDING                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.RUSSO,N.P.PAVLETICH                                               
REVDAT   4   24-FEB-09 1BYQ    1       VERSN                                    
REVDAT   3   01-APR-03 1BYQ    1       JRNL                                     
REVDAT   2   22-DEC-99 1BYQ    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   28-OCT-98 1BYQ    0                                                
JRNL        AUTH   W.M.OBERMANN,H.SONDERMANN,A.A.RUSSO,N.P.PAVLETICH,           
JRNL        AUTH 2 F.U.HARTL                                                    
JRNL        TITL   IN VIVO FUNCTION OF HSP90 IS DEPENDENT ON ATP                
JRNL        TITL 2 BINDING AND ATP HYDROLYSIS.                                  
JRNL        REF    J.CELL BIOL.                  V. 143   901 1998              
JRNL        REFN                   ISSN 0021-9525                               
JRNL        PMID   9817749                                                      
JRNL        DOI    10.1083/JCB.143.4.901                                        
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 31430                          
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 SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1600                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1678                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 384                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.600 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.500 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BYQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB008151.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 108.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33303                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1YES                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.50                                  
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       21.25000            
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 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     ASP A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     LYS A   224                                                      
REMARK 465     GLU A   225                                                      
REMARK 465     ARG A   226                                                      
REMARK 465     ASP A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     GLU A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     ASP A   232                                                      
REMARK 465     ASP A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 201   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 201   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    THR A  63     -111.23    -54.74                                   
REMARK 500    LEU A  64      -36.29    -23.51                                   
REMARK 500    LYS A  69       17.80   -170.11                                   
REMARK 500    SER A  72      175.36     38.62                                   
REMARK 500    LYS A  74      -68.06    178.93                                   
REMARK 500    ALA A 166     -143.65     70.86                                   
REMARK 500    GLN A 212       39.17    -83.40                                   
REMARK 500    PHE A 213       10.79   -160.71                                   
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 A2098        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH A2150        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH A2226        DISTANCE =  8.76 ANGSTROMS                       
REMARK 525    HOH A2238        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH A2246        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH A2251        DISTANCE =  6.81 ANGSTROMS                       
REMARK 525    HOH A2265        DISTANCE =  8.11 ANGSTROMS                       
REMARK 525    HOH A2269        DISTANCE = 10.80 ANGSTROMS                       
REMARK 525    HOH A2271        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH A2279        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A2298        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A2310        DISTANCE =  9.67 ANGSTROMS                       
REMARK 525    HOH A2311        DISTANCE =  7.51 ANGSTROMS                       
REMARK 525    HOH A2318        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH A2320        DISTANCE =  8.45 ANGSTROMS                       
REMARK 525    HOH A2321        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH A2325        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH A2328        DISTANCE =  8.61 ANGSTROMS                       
REMARK 525    HOH A2329        DISTANCE =  7.85 ANGSTROMS                       
REMARK 525    HOH A2330        DISTANCE =  9.97 ANGSTROMS                       
REMARK 525    HOH A2347        DISTANCE = 12.36 ANGSTROMS                       
REMARK 525    HOH A2351        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH A2358        DISTANCE = 10.57 ANGSTROMS                       
REMARK 525    HOH A2363        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH A2364        DISTANCE = 11.25 ANGSTROMS                       
REMARK 525    HOH A2372        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A2373        DISTANCE = 12.63 ANGSTROMS                       
REMARK 525    HOH A2375        DISTANCE =  6.03 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A2001   O1A                                                    
REMARK 620 2 HOH A2291   O    92.5                                              
REMARK 620 3 HOH A2290   O    97.2  86.8                                        
REMARK 620 4 ASN A  51   OD1  89.9  85.2 169.5                                  
REMARK 620 5 HOH A2289   O   175.4  91.0  86.0  87.4                            
REMARK 620 6 ADP A2001   O1B  86.2 178.5  93.9  94.2  90.3                      
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 MG A 1001                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 2001                
DBREF  1BYQ A    9   236  UNP    P07900   HS90A_HUMAN      8    235             
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 THR 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 LEU 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     MG  A1001       1                                                       
HET    ADP  A2001      27                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  ADP    C10 H15 N5 O10 P2                                            
FORMUL   4  HOH   *384(H2 O)                                                    
HELIX    1   1 ALA A   24  ASN A   35  1                                  12    
HELIX    2   2 LYS A   41  GLU A   62  5                                  22    
HELIX    3   3 LYS A  100  ASN A  106  1                                   7    
HELIX    4   4 THR A  115  ALA A  124  1                                  10    
HELIX    5   5 ILE A  128  PHE A  134  5                                   7    
HELIX    6   6 GLY A  137  LEU A  143  5                                   7    
HELIX    7   7 GLU A  192  LEU A  198  5                                   7    
HELIX    8   8 GLU A  200  HIS A  210  1                                  11    
SHEET    1   A 8 VAL A  17  ALA A  21  0                                        
SHEET    2   A 8 SER A 169  THR A 174 -1  N  VAL A 172   O  GLU A  18           
SHEET    3   A 8 GLN A 159  SER A 164 -1  N  GLU A 163   O  THR A 171           
SHEET    4   A 8 ALA A 145  LYS A 153 -1  N  THR A 152   O  TYR A 160           
SHEET    5   A 8 GLY A 183  LEU A 190 -1  N  HIS A 189   O  GLU A 146           
SHEET    6   A 8 THR A  88  ASP A  93 -1  N  ASP A  93   O  THR A 184           
SHEET    7   A 8 HIS A  77  ASN A  83 -1  N  ASN A  83   O  THR A  88           
SHEET    8   A 8 PRO A 217  PHE A 221  1  N  PRO A 217   O  ILE A  78           
LINK        MG    MG A1001                 O1A ADP A2001     1555   1555  2.08  
LINK        MG    MG A1001                 O   HOH A2291     1555   1555  2.15  
LINK        MG    MG A1001                 O   HOH A2290     1555   1555  2.10  
LINK        MG    MG A1001                 OD1 ASN A  51     1555   1555  2.06  
LINK        MG    MG A1001                 O   HOH A2289     1555   1555  2.16  
LINK        MG    MG A1001                 O1B ADP A2001     1555   1555  2.08  
SITE     1 AC1  5 ASN A  51  ADP A2001  HOH A2289  HOH A2290                    
SITE     2 AC1  5 HOH A2291                                                     
SITE     1 AC2 26 ASN A  51  ALA A  55  ASP A  93  MET A  98                    
SITE     2 AC2 26 ASN A 106  LEU A 107  VAL A 136  GLY A 137                    
SITE     3 AC2 26 PHE A 138  THR A 184   MG A1001  HOH A2003                    
SITE     4 AC2 26 HOH A2004  HOH A2012  HOH A2014  HOH A2108                    
SITE     5 AC2 26 HOH A2129  HOH A2140  HOH A2170  HOH A2187                    
SITE     6 AC2 26 HOH A2253  HOH A2260  HOH A2289  HOH A2290                    
SITE     7 AC2 26 HOH A2291  HOH A2366                                          
CRYST1   53.140   42.500   53.960  90.00 115.53  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      0.018818  0.000000  0.008988        0.00000                         
SCALE2      0.000000  0.023529  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020537        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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