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Database: PDB
Entry: 1BA0
LinkDB: 1BA0
Original site: 1BA0 
HEADER    HYDROLASE                               21-APR-98   1BA0              
TITLE     HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL 1NGE           
TITLE    2 3                                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT-SHOCK COGNATE 70KD PROTEIN;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: 44KD ATPASE N-TERMINAL FRAGMENT;                           
COMPND   5 EC: 3.6.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 CELL_LINE: BL21 (DE3);                                               
SOURCE   6 ORGAN: BRAIN;                                                        
SOURCE   7 CELLULAR_LOCATION: CYTOSOL;                                          
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  10 EXPRESSION_SYSTEM_CELL_LINE: BL21 (DE3);                             
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PET21;                                     
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: BL21                                      
KEYWDS    HYDROLASE, ACTING ON ACID ANHYDRIDES, ATP-BINDING, HEAT               
KEYWDS   2 SHOCK                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.WILBANKS,D.B.MCKAY                                                
REVDAT   3   24-FEB-09 1BA0    1       VERSN                                    
REVDAT   2   01-APR-03 1BA0    1       JRNL                                     
REVDAT   1   15-JUL-98 1BA0    0                                                
JRNL        AUTH   S.M.WILBANKS,D.B.MCKAY                                       
JRNL        TITL   STRUCTURAL REPLACEMENT OF ACTIVE SITE MONOVALENT             
JRNL        TITL 2 CATIONS BY THE EPSILON-AMINO GROUP OF LYSINE IN              
JRNL        TITL 3 THE ATPASE FRAGMENT OF BOVINE HSC70.                         
JRNL        REF    BIOCHEMISTRY                  V.  37  7456 1998              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9585559                                                      
JRNL        DOI    10.1021/BI973046M                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
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   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.M.FLAHERTY,C.DELUCA-FLAHERTY,D.B.MCKAY                     
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF THE ATPASE FRAGMENT           
REMARK   1  TITL 2 OF A 70K HEAT-SHOCK COGNATE PROTEIN                          
REMARK   1  REF    NATURE                        V. 346   623 1990              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 34106                          
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) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3357                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.600                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.94                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1867                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 212                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.600                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2908                                    
REMARK   3   NUCLEIC ACID ATOMS       : 27                                      
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 423                                     
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) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 40.00                           
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) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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 1BA0 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        : OCT-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34106                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 1.00000                            
REMARK 200  R SYM                      (I) : 0.05600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.00000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.13300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 12.000                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1HPM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-8000 1.0M NACL 50MM CHES,        
REMARK 280  PH 9 1MM MGATP, PH 9.0                                              
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       71.65000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       23.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       71.65000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.90000            
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 465     GLY A   382                                                      
REMARK 465     ASP A   383                                                      
REMARK 465     LYS A   384                                                      
REMARK 465     SER A   385                                                      
REMARK 465     GLU A   386                                                      
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     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       19.71   -142.47                                   
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 625        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH A 673        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 705        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 938        DISTANCE =  6.88 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 ADP A 486   O2B                                                    
REMARK 620 2 PO4 A 488   O2   91.0                                              
REMARK 620 3 HOH A 560   O    91.2  83.0                                        
REMARK 620 4 HOH A 561   O   173.4  89.5  95.4                                  
REMARK 620 5 HOH A 562   O    89.0  90.2 173.3  84.5                            
REMARK 620 6 HOH A 563   O    86.9 169.7  87.0  93.7  99.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 490  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 486   O2B                                                    
REMARK 620 2 ASP A  10   OD2 129.2                                              
REMARK 620 3 HOH A 558   O   126.1  93.8                                        
REMARK 620 4 TYR A  15   O    99.6 112.8  88.5                                  
REMARK 620 5 HOH A 563   O    67.5  77.6  98.7 167.1                            
REMARK 620 N                    1     2     3     4                             
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 PO4 A 488                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 490                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 451                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 455                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 486                 
DBREF  1BA0 A    1   386  UNP    P19120   HSP7C_BOVIN      1    386             
SEQADV 1BA0 LYS A  206  UNP  P19120    ASP   206 ENGINEERED                     
SEQRES   1 A  386  MET SER LYS GLY PRO ALA VAL GLY ILE ASP LEU GLY THR          
SEQRES   2 A  386  THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY LYS VAL          
SEQRES   3 A  386  GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR THR PRO          
SEQRES   4 A  386  SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU ILE GLY          
SEQRES   5 A  386  ASP ALA ALA LYS ASN GLN VAL ALA MET ASN PRO THR ASN          
SEQRES   6 A  386  THR VAL PHE ASP ALA LYS ARG LEU ILE GLY ARG ARG PHE          
SEQRES   7 A  386  ASP ASP ALA VAL VAL GLN SER ASP MET LYS HIS TRP PRO          
SEQRES   8 A  386  PHE MET VAL VAL ASN ASP ALA GLY ARG PRO LYS VAL GLN          
SEQRES   9 A  386  VAL GLU TYR LYS GLY GLU THR LYS SER PHE TYR PRO GLU          
SEQRES  10 A  386  GLU VAL SER SER MET VAL LEU THR LYS MET LYS GLU ILE          
SEQRES  11 A  386  ALA GLU ALA TYR LEU GLY LYS THR VAL THR ASN ALA VAL          
SEQRES  12 A  386  VAL THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG GLN          
SEQRES  13 A  386  ALA THR LYS ASP ALA GLY THR ILE ALA GLY LEU ASN VAL          
SEQRES  14 A  386  LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA ILE ALA          
SEQRES  15 A  386  TYR GLY LEU ASP LYS LYS VAL GLY ALA GLU ARG ASN VAL          
SEQRES  16 A  386  LEU ILE PHE ASP LEU GLY GLY GLY THR PHE LYS VAL SER          
SEQRES  17 A  386  ILE LEU THR ILE GLU ASP GLY ILE PHE GLU VAL LYS SER          
SEQRES  18 A  386  THR ALA GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP          
SEQRES  19 A  386  ASN ARG MET VAL ASN HIS PHE ILE ALA GLU PHE LYS ARG          
SEQRES  20 A  386  LYS HIS LYS LYS ASP ILE SER GLU ASN LYS ARG ALA VAL          
SEQRES  21 A  386  ARG ARG LEU ARG THR ALA CYS GLU ARG ALA LYS ARG THR          
SEQRES  22 A  386  LEU SER SER SER THR GLN ALA SER ILE GLU ILE ASP SER          
SEQRES  23 A  386  LEU TYR GLU GLY ILE ASP PHE TYR THR SER ILE THR ARG          
SEQRES  24 A  386  ALA ARG PHE GLU GLU LEU ASN ALA ASP LEU PHE ARG GLY          
SEQRES  25 A  386  THR LEU ASP PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS          
SEQRES  26 A  386  LEU ASP LYS SER GLN ILE HIS ASP ILE VAL LEU VAL GLY          
SEQRES  27 A  386  GLY SER THR ARG ILE PRO LYS ILE GLN LYS LEU LEU GLN          
SEQRES  28 A  386  ASP PHE PHE ASN GLY LYS GLU LEU ASN LYS SER ILE ASN          
SEQRES  29 A  386  PRO ASP GLU ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA          
SEQRES  30 A  386  ALA ILE LEU SER GLY ASP LYS SER GLU                          
HET     MG  A 487       1                                                       
HET    PO4  A 488       5                                                       
HET     NA  A 490       1                                                       
HET     CL  A 451       1                                                       
HET     CL  A 455       1                                                       
HET    ADP  A 486      27                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4   NA    NA 1+                                                        
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   7  ADP    C10 H15 N5 O10 P2                                            
FORMUL   8  HOH   *423(H2 O)                                                    
HELIX    1   1 ASP A   53  GLN A   58  1                                   6    
HELIX    2   2 PRO A   63  ASN A   65  5                                   3    
HELIX    3   3 ALA A   70  ARG A   72  5                                   3    
HELIX    4   4 ALA A   81  HIS A   89  1                                   9    
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  ASP A  10  1  N  VAL A   7   O  VAL A 143           
SHEET    4   A 5 CYS A  17  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 ADP A 486                MG    MG A 487     1555   1555  2.05  
LINK         O2B ADP A 486                NA    NA A 490     1555   1555  2.37  
LINK        MG    MG A 487                 O2  PO4 A 488     1555   1555  2.15  
LINK        MG    MG A 487                 O   HOH A 560     1555   1555  2.17  
LINK        MG    MG A 487                 O   HOH A 561     1555   1555  2.05  
LINK        MG    MG A 487                 O   HOH A 562     1555   1555  2.05  
LINK        MG    MG A 487                 O   HOH A 563     1555   1555  2.15  
LINK        NA    NA A 490                 OD2 ASP A  10     1555   1555  2.45  
LINK        NA    NA A 490                 O   HOH A 558     1555   1555  2.31  
LINK        NA    NA A 490                 O   TYR A  15     1555   1555  2.44  
LINK        NA    NA A 490                 O   HOH A 563     1555   1555  2.80  
CISPEP   1 GLY A    4    PRO A    5          0         0.15                     
SITE     1 AC1  7 ADP A 486  PO4 A 488   NA A 490  HOH A 560                    
SITE     2 AC1  7 HOH A 561  HOH A 562  HOH A 563                               
SITE     1 AC2 14 GLY A  12  THR A  13  LYS A  71  PRO A 147                    
SITE     2 AC2 14 GLU A 175  THR A 204  LYS A 206  ADP A 486                    
SITE     3 AC2 14  MG A 487  HOH A 545  HOH A 560  HOH A 561                    
SITE     4 AC2 14 HOH A 562  HOH A1057                                          
SITE     1 AC3  6 ASP A  10  TYR A  15  ADP A 486   MG A 487                    
SITE     2 AC3  6 HOH A 558  HOH A 563                                          
SITE     1 AC4  5 TYR A 183  LYS A 345  LYS A 348  HOH A 537                    
SITE     2 AC4  5 HOH A 892                                                     
SITE     1 AC5  4 ASN A  31  ASP A  32  GLN A  33  LYS A 126                    
SITE     1 AC6 28 THR A  13  THR A  14  TYR A  15  GLY A 201                    
SITE     2 AC6 28 GLY A 202  GLY A 230  GLU A 268  LYS A 271                    
SITE     3 AC6 28 ARG A 272  SER A 275  GLY A 338  GLY A 339                    
SITE     4 AC6 28 SER A 340  ARG A 342  ASP A 366   MG A 487                    
SITE     5 AC6 28 PO4 A 488   NA A 490  HOH A 545  HOH A 558                    
SITE     6 AC6 28 HOH A 560  HOH A 562  HOH A 563  HOH A 564                    
SITE     7 AC6 28 HOH A 587  HOH A 799  HOH A 965  HOH A1053                    
CRYST1  143.300   63.800   46.500  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      0.006978  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015674  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021505        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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