GenomeNet

Database: PDB
Entry: 1NGC
LinkDB: 1NGC
Original site: 1NGC 
HEADER    HYDROLASE(ACTING ON ACID ANHYDRIDES)    17-MAY-94   1NGC              
TITLE     STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE              
TITLE    2 PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE                
TITLE    3 ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT            
TITLE    4 ATPASE FRAGMENT                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT-SHOCK COGNATE 70 KD PROTEIN;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.6.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 ORGAN: BRAIN                                                         
KEYWDS    HYDROLASE(ACTING ON ACID ANHYDRIDES)                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.FLAHERTY,S.M.WILBANKS,C.DELUCA-FLAHERTY,D.B.MCKAY                 
REVDAT   3   24-FEB-09 1NGC    1       VERSN                                    
REVDAT   2   01-APR-03 1NGC    1       JRNL                                     
REVDAT   1   31-AUG-94 1NGC    0                                                
JRNL        AUTH   K.M.FLAHERTY,S.M.WILBANKS,C.DELUCA-FLAHERTY,                 
JRNL        AUTH 2 D.B.MCKAY                                                    
JRNL        TITL   STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK             
JRNL        TITL 2 COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY. II.                 
JRNL        TITL 3 STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND           
JRNL        TITL 4 TO WILD TYPE AND MUTANT ATPASE FRAGMENT.                     
JRNL        REF    J.BIOL.CHEM.                  V. 269 12899 1994              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   8175707                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
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.    2.20 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) : 2.20                           
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             : 14049                          
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) : 0.188                           
REMARK   3   FREE R VALUE                     : NULL                            
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            : 2926                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 141                                     
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) : 1.40                            
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 1NGC 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) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
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   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
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       72.65000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.45000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.50000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       23.45000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       72.65000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.50000            
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 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  45     -169.80   -126.39                                   
REMARK 500    GLN A  58       12.92   -152.10                                   
REMARK 500    ILE A  74      134.82    -36.56                                   
REMARK 500    THR A 140      -55.98   -120.46                                   
REMARK 500    LYS A 250       49.99     37.18                                   
REMARK 500    GLU A 289     -120.61     59.65                                   
REMARK 500    PHE A 354       31.37    -92.82                                   
REMARK 500    ASN A 355       56.40     39.91                                   
REMARK 500    LYS A 361       33.09   -158.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 487  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 579   O                                                      
REMARK 620 2 PO4 A 488   O2  174.9                                              
REMARK 620 3 ADP A 486   O2B  92.0  82.8                                        
REMARK 620 4 HOH A 577   O    76.6 103.0  88.0                                  
REMARK 620 5 HOH A 578   O    87.6  97.5 172.3  99.3                            
REMARK 620 6 HOH A 626   O    95.6  83.9  83.9 168.6  88.6                      
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 PO4 A 488                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 486                 
DBREF  1NGC A    1   386  UNP    P19120   HSP7C_BOVIN      1    386             
SEQADV 1NGC SER A  206  UNP  P19120    ASP   206 CONFLICT                       
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 SER 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    ADP  A 486      27                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  ADP    C10 H15 N5 O10 P2                                            
FORMUL   5  HOH   *141(H2 O)                                                    
HELIX    1   1 GLY A   52  ASN A   57  1                                   6    
HELIX    2   2 ASN A   62  THR A   64  5                                   3    
HELIX    3   3 ASP A   69  LEU A   73  5                                   5    
HELIX    4   4 ASP A   80  LYS A   88  1                                   9    
HELIX    5   5 TYR A  115  GLY A  136  1                                  22    
HELIX    6   6 ASN A  151  ILE A  164  1                                  14    
HELIX    7   7 GLU A  175  TYR A  183  1                                   9    
HELIX    8   8 GLY A  229  LYS A  250  1                                  22    
HELIX    9   9 ASN A  256  SER A  275  1                                  20    
HELIX   10  10 ARG A  299  ASN A  306  1                                   8    
HELIX   11  11 ASN A  306  THR A  313  1                                   8    
HELIX   12  12 THR A  313  LYS A  325  1                                  13    
HELIX   13  13 ASP A  327  ILE A  331  5                                   5    
HELIX   14  14 GLY A  338  ARG A  342  5                                   5    
HELIX   15  15 ILE A  343  PHE A  354  1                                  12    
HELIX   16  16 GLU A  367  LEU A  380  1                                  14    
SHEET    1   A 5 LYS A  25  ILE A  28  0                                        
SHEET    2   A 5 TYR A  15  GLN A  22 -1  O  VAL A  20   N  GLU A  27           
SHEET    3   A 5 VAL A   7  ASP A  10 -1  N  GLY A   8   O  GLY A  19           
SHEET    4   A 5 ASN A 141  VAL A 146  1  O  ASN A 141   N  VAL A   7           
SHEET    5   A 5 ASN A 168  ASN A 174  1  O  ASN A 168   N  ALA A 142           
SHEET    1   B 3 LYS A  25  ILE A  28  0                                        
SHEET    2   B 3 TYR A  15  GLN A  22 -1  O  VAL A  20   N  GLU A  27           
SHEET    3   B 3 THR A  38  PRO A  39 -1  N  THR A  38   O  SER A  16           
SHEET    1   C 3 ARG A  49  ILE A  51  0                                        
SHEET    2   C 3 VAL A  42  PHE A  44 -1  O  ALA A  43   N  LEU A  50           
SHEET    3   C 3 THR A  66  VAL A  67 -1  N  VAL A  67   O  VAL A  42           
SHEET    1   D 3 MET A  93  ASP A  97  0                                        
SHEET    2   D 3 ARG A 100  TYR A 107 -1  O  ARG A 100   N  ASP A  97           
SHEET    3   D 3 GLU A 110  PHE A 114 -1  O  GLU A 110   N  TYR A 107           
SHEET    1   E 4 VAL A 219  ASP A 225  0                                        
SHEET    2   E 4 PHE A 205  ILE A 212 -1  N  PHE A 205   O  ASP A 225           
SHEET    3   E 4 ARG A 193  LEU A 200 -1  O  ARG A 193   N  ILE A 212           
SHEET    4   E 4 ASP A 333  VAL A 337  1  O  ASP A 333   N  LEU A 196           
SHEET    1   F 2 GLN A 279  TYR A 288  0                                        
SHEET    2   F 2 ILE A 291  THR A 298 -1  N  ILE A 291   O  TYR A 288           
LINK        MG    MG A 487                 O   HOH A 579     1555   1555  2.06  
LINK        MG    MG A 487                 O2  PO4 A 488     1555   1555  2.08  
LINK        MG    MG A 487                 O2B ADP A 486     1555   1555  2.06  
LINK        MG    MG A 487                 O   HOH A 577     1555   1555  2.13  
LINK        MG    MG A 487                 O   HOH A 578     1555   1555  1.94  
LINK        MG    MG A 487                 O   HOH A 626     1555   1555  2.07  
SITE     1 AC1  6 ADP A 486  PO4 A 488  HOH A 577  HOH A 578                    
SITE     2 AC1  6 HOH A 579  HOH A 626                                          
SITE     1 AC2  9 GLY A  12  THR A  13  LYS A  71  GLU A 175                    
SITE     2 AC2  9 THR A 204  ADP A 486   MG A 487  HOH A 578                    
SITE     3 AC2  9 HOH A 626                                                     
SITE     1 AC3 27 THR A  13  THR A  14  TYR A  15  GLY A 201                    
SITE     2 AC3 27 GLY A 202  GLY A 230  GLU A 268  LYS A 271                    
SITE     3 AC3 27 ARG A 272  SER A 275  GLY A 338  GLY A 339                    
SITE     4 AC3 27 SER A 340  ARG A 342  ILE A 343  ASP A 366                    
SITE     5 AC3 27  MG A 487  PO4 A 488  HOH A 537  HOH A 549                    
SITE     6 AC3 27 HOH A 551  HOH A 568  HOH A 577  HOH A 579                    
SITE     7 AC3 27 HOH A 580  HOH A 581  HOH A 626                               
CRYST1  145.300   65.000   46.900  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      0.006882  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015385  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021322        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system