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Database: PDB
Entry: 1KAY
LinkDB: 1KAY
Original site: 1KAY 
HEADER    HYDROLASE                               15-APR-96   1KAY              
TITLE     70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71A MUTANT            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 70KD HEAT SHOCK COGNATE PROTEIN;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ATPASE DOMAIN;                                             
COMPND   5 SYNONYM: HSC70;                                                      
COMPND   6 EC: 3.6.1.3;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913                                                 
KEYWDS    ATP-BINDING, HEAT SHOCK, HYDROLASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.O'BRIEN,K.M.FLAHERTY,D.B.MCKAY                                    
REVDAT   3   24-FEB-09 1KAY    1       VERSN                                    
REVDAT   2   01-APR-03 1KAY    1       JRNL                                     
REVDAT   1   08-NOV-96 1KAY    0                                                
JRNL        AUTH   M.C.O'BRIEN,K.M.FLAHERTY,D.B.MCKAY                           
JRNL        TITL   LYSINE 71 OF THE CHAPERONE PROTEIN HSC70 IS                  
JRNL        TITL 2 ESSENTIAL FOR ATP HYDROLYSIS.                                
JRNL        REF    J.BIOL.CHEM.                  V. 271 15874 1996              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   8663302                                                      
JRNL        DOI    10.1074/JBC.271.27.15874                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.M.WILBANKS,D.B.MCKAY                                       
REMARK   1  TITL   HOW POTASSIUM AFFECTS THE ACTIVITY OF THE                    
REMARK   1  TITL 2 MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS               
REMARK   1  TITL 3 SPECIFICALLY IN THE ATPASE ACTIVE SITE                       
REMARK   1  REF    J.BIOL.CHEM.                  V. 270  2251 1995              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.M.FLAHERTY,S.M.WILBANKS,C.DELUCA-FLAHERTY,                 
REMARK   1  AUTH 2 D.B.MCKAY                                                    
REMARK   1  TITL   STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK             
REMARK   1  TITL 2 COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY. II.                 
REMARK   1  TITL 3 STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND           
REMARK   1  TITL 4 TO WILD TYPE AND MUTANT ATPASE FRAGMENT                      
REMARK   1  REF    J.BIOL.CHEM.                  V. 269 12899 1994              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 39751                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 2897                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 435                                     
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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.26                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.87                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.10                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KAY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40944                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.6                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.04300                            
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       71.95000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.10000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.30000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       23.10000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       71.95000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.30000            
REMARK 290   SMTRY3   4  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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LYS A     3                                                      
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     ARG A  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 137    CG   CD   CE   NZ                                   
REMARK 470     LYS A 188    CG   CD   CE   NZ                                   
REMARK 470     LYS A 248    CG   CD   CE   NZ                                   
REMARK 470     LYS A 250    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    LYS A 361       17.08   -141.12                                   
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 561        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH A 580        DISTANCE =  5.61 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 487  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 486   O2B                                                    
REMARK 620 2 HOH A 904   O    93.2                                              
REMARK 620 3 HOH A 905   O   174.0  91.3                                        
REMARK 620 4 HOH A 906   O    89.8  86.0  86.7                                  
REMARK 620 5 HOH A 907   O   102.2  83.8  82.1 164.7                            
REMARK 620 6 HOH A 910   O    90.0 176.3  85.3  92.2  97.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 490   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A  15   O                                                      
REMARK 620 2 ASP A  10   OD2 138.9                                              
REMARK 620 3 ASP A  10   OD1 113.2  42.6                                        
REMARK 620 4  MG A 487  MG   128.1  85.0  78.6                                  
REMARK 620 5 ATP A 486   O2B 102.0 116.2 107.5  32.5                            
REMARK 620 6 HOH A 906   O   164.3  56.5  76.1  38.9  62.5                      
REMARK 620 7 HOH A 910   O   116.4  75.9  50.2  33.9  57.6  58.7                
REMARK 620 8 HOH A 923   O    92.0  91.2 131.5 118.2 106.5  90.4 148.8          
REMARK 620 9 GLY A  12   N    53.3 103.1  63.3 100.0 100.0 128.4  70.8 140.3    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 491   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 204   O                                                      
REMARK 620 2 THR A 204   OG1  65.3                                              
REMARK 620 3 ASP A 206   OD2 100.1  71.7                                        
REMARK 620 4 ATP A 486   O3G  64.4  54.4 125.9                                  
REMARK 620 5 GLY A 201   N    51.3 106.6 143.7  66.8                            
REMARK 620 6 ASP A 199   O    68.3 121.3  83.3 127.4  66.4                      
REMARK 620 7 ASP A 199   OD1 112.2 174.4 113.9 120.0  68.8  60.4                
REMARK 620 8 HOH A 907   O   129.5  88.3 111.8  65.2 104.3 150.2  89.8          
REMARK 620 9 HOH A 904   O   115.1 128.9 144.0  78.8  65.9 102.3  46.8  50.2    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 492   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 206   OD1                                                    
REMARK 620 2 THR A 204   OG1 104.5                                              
REMARK 620 3 ASP A 206   OD2  43.5  73.8                                        
REMARK 620 4 HOH A 900   O   124.8  80.3  89.6                                  
REMARK 620 5 TYR A 149   OH   86.3 136.9 129.7 127.4                            
REMARK 620 6 HOH A 908   O   158.5  93.8 156.9  68.9  72.5                      
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 487                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 451                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 455                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 490                   
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 491                   
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 492                   
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 486                 
DBREF  1KAY A    1   381  UNP    P19120   HSP7C_BOVIN      1    381             
SEQADV 1KAY ALA A   71  UNP  P19120    LYS    71 ENGINEERED                     
SEQRES   1 A  381  MET SER LYS GLY PRO ALA VAL GLY ILE ASP LEU GLY THR          
SEQRES   2 A  381  THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY LYS VAL          
SEQRES   3 A  381  GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR THR PRO          
SEQRES   4 A  381  SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU ILE GLY          
SEQRES   5 A  381  ASP ALA ALA LYS ASN GLN VAL ALA MET ASN PRO THR ASN          
SEQRES   6 A  381  THR VAL PHE ASP ALA ALA ARG LEU ILE GLY ARG ARG PHE          
SEQRES   7 A  381  ASP ASP ALA VAL VAL GLN SER ASP MET LYS HIS TRP PRO          
SEQRES   8 A  381  PHE MET VAL VAL ASN ASP ALA GLY ARG PRO LYS VAL GLN          
SEQRES   9 A  381  VAL GLU TYR LYS GLY GLU THR LYS SER PHE TYR PRO GLU          
SEQRES  10 A  381  GLU VAL SER SER MET VAL LEU THR LYS MET LYS GLU ILE          
SEQRES  11 A  381  ALA GLU ALA TYR LEU GLY LYS THR VAL THR ASN ALA VAL          
SEQRES  12 A  381  VAL THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG GLN          
SEQRES  13 A  381  ALA THR LYS ASP ALA GLY THR ILE ALA GLY LEU ASN VAL          
SEQRES  14 A  381  LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA ILE ALA          
SEQRES  15 A  381  TYR GLY LEU ASP LYS LYS VAL GLY ALA GLU ARG ASN VAL          
SEQRES  16 A  381  LEU ILE PHE ASP LEU GLY GLY GLY THR PHE ASP VAL SER          
SEQRES  17 A  381  ILE LEU THR ILE GLU ASP GLY ILE PHE GLU VAL LYS SER          
SEQRES  18 A  381  THR ALA GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP          
SEQRES  19 A  381  ASN ARG MET VAL ASN HIS PHE ILE ALA GLU PHE LYS ARG          
SEQRES  20 A  381  LYS HIS LYS LYS ASP ILE SER GLU ASN LYS ARG ALA VAL          
SEQRES  21 A  381  ARG ARG LEU ARG THR ALA CYS GLU ARG ALA LYS ARG THR          
SEQRES  22 A  381  LEU SER SER SER THR GLN ALA SER ILE GLU ILE ASP SER          
SEQRES  23 A  381  LEU TYR GLU GLY ILE ASP PHE TYR THR SER ILE THR ARG          
SEQRES  24 A  381  ALA ARG PHE GLU GLU LEU ASN ALA ASP LEU PHE ARG GLY          
SEQRES  25 A  381  THR LEU ASP PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS          
SEQRES  26 A  381  LEU ASP LYS SER GLN ILE HIS ASP ILE VAL LEU VAL GLY          
SEQRES  27 A  381  GLY SER THR ARG ILE PRO LYS ILE GLN LYS LEU LEU GLN          
SEQRES  28 A  381  ASP PHE PHE ASN GLY LYS GLU LEU ASN LYS SER ILE ASN          
SEQRES  29 A  381  PRO ASP GLU ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA          
SEQRES  30 A  381  ALA ILE LEU SER                                              
HET     MG  A 487       1                                                       
HET     CL  A 451       1                                                       
HET     CL  A 455       1                                                       
HET      K  A 490       1                                                       
HET      K  A 491       1                                                       
HET      K  A 492       1                                                       
HET    ATP  A 486      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM       K POTASSIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   2   MG    MG 2+                                                        
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5    K    3(K 1+)                                                      
FORMUL   8  ATP    C10 H16 N5 O13 P3                                            
FORMUL   9  HOH   *435(H2 O)                                                    
HELIX    1   1 GLY A   52  GLN A   58  5                                   7    
HELIX    2   2 PRO A   63  ASN A   65  5                                   3    
HELIX    3   3 ALA A   70  LEU A   73  1                                   4    
HELIX    4   4 ALA A   81  LYS A   88  1                                   8    
HELIX    5   5 PRO A  116  LEU A  135  1                                  20    
HELIX    6   6 ASP A  152  ILE A  164  1                                  13    
HELIX    7   7 GLU A  175  TYR A  183  1                                   9    
HELIX    8   8 GLY A  230  HIS A  249  1                                  20    
HELIX    9   9 LYS A  257  SER A  275  1                                  19    
HELIX   10  10 ARG A  299  ALA A  324  1                                  26    
HELIX   11  11 LYS A  328  GLN A  330  5                                   3    
HELIX   12  12 GLY A  339  ARG A  342  5                                   4    
HELIX   13  13 PRO A  344  PHE A  353  1                                  10    
HELIX   14  14 ALA A  368  ILE A  379  1                                  12    
SHEET    1   A 5 ASN A 168  ASN A 174  0                                        
SHEET    2   A 5 ASN A 141  VAL A 146  1  N  ALA A 142   O  ASN A 168           
SHEET    3   A 5 VAL A   7  LEU A  11  1  N  VAL A   7   O  VAL A 143           
SHEET    4   A 5 SER A  16  GLN A  22 -1  N  GLY A  19   O  GLY A   8           
SHEET    5   A 5 LYS A  25  ILE A  28 -1  N  GLU A  27   O  VAL A  20           
SHEET    1   B 2 VAL A  42  PHE A  44  0                                        
SHEET    2   B 2 ARG A  49  ILE A  51 -1  N  LEU A  50   O  ALA A  43           
SHEET    1   C 3 MET A  93  ASP A  97  0                                        
SHEET    2   C 3 ARG A 100  TYR A 107 -1  N  GLN A 104   O  MET A  93           
SHEET    3   C 3 GLU A 110  TYR A 115 -1  N  PHE A 114   O  VAL A 103           
SHEET    1   D 4 ASP A 333  VAL A 337  0                                        
SHEET    2   D 4 ARG A 193  LEU A 200  1  N  LEU A 196   O  ASP A 333           
SHEET    3   D 4 PHE A 205  GLU A 213 -1  N  ILE A 212   O  ARG A 193           
SHEET    4   D 4 ILE A 216  ASP A 225 -1  N  ASP A 225   O  PHE A 205           
SHEET    1   E 2 GLN A 279  ILE A 284  0                                        
SHEET    2   E 2 PHE A 293  THR A 298 -1  N  ILE A 297   O  ALA A 280           
LINK         O2B ATP A 486                MG    MG A 487     1555   1555  1.97  
LINK        MG    MG A 487                 O   HOH A 904     1555   1555  2.16  
LINK        MG    MG A 487                 O   HOH A 905     1555   1555  2.14  
LINK        MG    MG A 487                 O   HOH A 906     1555   1555  2.27  
LINK        MG    MG A 487                 O   HOH A 907     1555   1555  1.96  
LINK        MG    MG A 487                 O   HOH A 910     1555   1555  2.00  
LINK         K     K A 490                 O   TYR A  15     1555   1555  2.59  
LINK         K     K A 490                 OD2 ASP A  10     1555   1555  2.59  
LINK         K     K A 490                 OD1 ASP A  10     1555   1555  3.21  
LINK         K     K A 490                MG    MG A 487     1555   1555  3.57  
LINK         K     K A 490                 O2B ATP A 486     1555   1555  2.57  
LINK         K     K A 490                 O   HOH A 906     1555   1555  3.13  
LINK         K     K A 490                 O   HOH A 910     1555   1555  3.15  
LINK         K     K A 490                 O   HOH A 923     1555   1555  2.70  
LINK         K     K A 490                 N   GLY A  12     1555   1555  3.70  
LINK         K     K A 491                 O   THR A 204     1555   1555  2.97  
LINK         K     K A 491                 OG1 THR A 204     1555   1555  2.85  
LINK         K     K A 491                 OD2 ASP A 206     1555   1555  2.79  
LINK         K     K A 491                 O3G ATP A 486     1555   1555  3.05  
LINK         K     K A 491                 N   GLY A 201     1555   1555  3.71  
LINK         K     K A 491                 O   ASP A 199     1555   1555  3.49  
LINK         K     K A 491                 OD1 ASP A 199     1555   1555  3.08  
LINK         K     K A 491                 O   HOH A 907     1555   1555  2.81  
LINK         K     K A 491                 O   HOH A 904     1555   1555  3.51  
LINK         K     K A 492                 OD1 ASP A 206     1555   1555  3.10  
LINK         K     K A 492                 OG1 THR A 204     1555   1555  2.73  
LINK         K     K A 492                 OD2 ASP A 206     1555   1555  2.77  
LINK         K     K A 492                 O   HOH A 900     1555   1555  2.82  
LINK         K     K A 492                 OH  TYR A 149     1555   1555  2.61  
LINK         K     K A 492                 O   HOH A 908     1555   1555  3.41  
CISPEP   1 GLY A    4    PRO A    5          0         0.23                     
SITE     1 AC1  7 ATP A 486    K A 490  HOH A 904  HOH A 905                    
SITE     2 AC1  7 HOH A 906  HOH A 907  HOH A 910                               
SITE     1 AC2  4 TYR A 183  LYS A 345  LYS A 348  HOH A 521                    
SITE     1 AC3  4 ASN A  31  ASP A  32  GLN A  33  LYS A 126                    
SITE     1 AC4  6 ASP A  10  GLY A  12  TYR A  15  ATP A 486                    
SITE     2 AC4  6  MG A 487  HOH A 923                                          
SITE     1 AC5  5 ASP A 199  THR A 204  ASP A 206  ATP A 486                    
SITE     2 AC5  5 HOH A 907                                                     
SITE     1 AC6  4 TYR A 149  THR A 204  ASP A 206  HOH A 900                    
SITE     1 AC7 31 GLY A  12  THR A  13  THR A  14  TYR A  15                    
SITE     2 AC7 31 GLY A 201  GLY A 202  GLY A 203  THR A 204                    
SITE     3 AC7 31 GLY A 230  GLU A 268  LYS A 271  ARG A 272                    
SITE     4 AC7 31 SER A 275  GLY A 338  GLY A 339  SER A 340                    
SITE     5 AC7 31 ARG A 342  ILE A 343  ASP A 366   MG A 487                    
SITE     6 AC7 31   K A 490    K A 491  HOH A 525  HOH A 531                    
SITE     7 AC7 31 HOH A 545  HOH A 650  HOH A 904  HOH A 906                    
SITE     8 AC7 31 HOH A 907  HOH A 910  HOH A 923                               
CRYST1  143.900   64.600   46.200  90.00  90.00  90.00 P 21 21 21    4          
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      0.006949  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015480  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021645        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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