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Database: PDB
Entry: 2QUR
LinkDB: 2QUR
Original site: 2QUR 
HEADER    SIGNALING PROTEIN, TRANSFERASE          06-AUG-07   2QUR              
TITLE     CRYSTAL STRUCTURE OF F327A/K285P MUTANT OF CAMP-DEPENDENT             
TITLE    2 PROTEIN KINASE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC             
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PKA C-ALPHA;                                                
COMPND   6 EC: 2.7.11.11;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: 20-MER FRAGMENT FROM CAMP-DEPENDENT PROTEIN                
COMPND  11 KINASE INHIBITOR ALPHA;                                              
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: RESIDUES 6-25;                                             
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_TAXID: 10090;                                               
SOURCE   4 GENE: PRKACA, PKACA;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PRSET;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES                                                       
KEYWDS    CRYSTAL STRUCTURE, CAMP-DEPENDENT PROTEIN KINASE,                     
KEYWDS   2 F327A/K285P MUTANT, ISOFORM SPECIFIC REGULATION, AGC-                
KEYWDS   3 SPECIFIC INSERT, SIGNALING PROTEIN, TRANSFERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.TAYLOR,J.YANG,J.WU                                                
REVDAT   3   16-JUN-09 2QUR    1       JRNL                                     
REVDAT   2   24-FEB-09 2QUR    1       VERSN                                    
REVDAT   1   29-JUL-08 2QUR    0                                                
JRNL        AUTH   J.YANG,E.J.KENNEDY,J.WU,M.S.DEAL,J.PENNYPACKER,              
JRNL        AUTH 2 G.GHOSH,S.S.TAYLOR                                           
JRNL        TITL   CONTRIBUTION OF NON-CATALYTIC CORE RESIDUES TO               
JRNL        TITL 2 ACTIVITY AND REGULATION IN PROTEIN KINASE A.                 
JRNL        REF    J.BIOL.CHEM.                  V. 284  6241 2009              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19122195                                                     
JRNL        DOI    10.1074/JBC.M805862200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
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)   (%) : 87.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 10089                          
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) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 520                             
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.59                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3910                       
REMARK   3   BIN FREE R VALUE                    : 0.4840                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 38                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.078                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2842                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 24                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 32.71000                                             
REMARK   3    B22 (A**2) : -16.83000                                            
REMARK   3    B33 (A**2) : -15.88000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.55                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.50                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.69                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 2QUR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044080.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 200.0                              
REMARK 200  PH                             : 7.5                                
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12647                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.44000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1ATP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-12% MPD, 100 MM TRIS-HCL, PLUS 10      
REMARK 280  MM DTT, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K     
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       28.78000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.31500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.25000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.31500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.78000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.25000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     GLY A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     SER A    10                                                      
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     GLU A  11    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  12    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  13    CG   CD   OE1  OE2                                  
REMARK 470     VAL A  15    CG1  CG2                                            
REMARK 470     LYS A  16    CG   CD   CE   NZ                                   
REMARK 470     GLU A  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  28    CG   CD   CE   NZ                                   
REMARK 470     GLN A  42    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  47    CG   CD   CE   NZ                                   
REMARK 470     LYS A  61    CG   CD   CE   NZ                                   
REMARK 470     LYS A  72    CG   CD   CE   NZ                                   
REMARK 470     LYS A  81    CG   CD   CE   NZ                                   
REMARK 470     LYS A  83    CG   CD   CE   NZ                                   
REMARK 470     HIS A 142    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 184    CG   OD1  OD2                                       
REMARK 470     LYS A 189    CG   CD   CE   NZ                                   
REMARK 470     LYS A 249    CG   CD   CE   NZ                                   
REMARK 470     ARG A 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 286    CG   OD1  ND2                                       
REMARK 470     LYS A 295    CG   CD   CE   NZ                                   
REMARK 470     LYS A 309    CG   CD   CE   NZ                                   
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     PHE A 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 470     ASP A 323    CG   OD1  OD2                                       
REMARK 470     THR A 324    OG1  CG2                                            
REMARK 470     SER A 325    OG                                                  
REMARK 470     ASN A 326    CG   OD1  ND2                                       
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     HIS B 379    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR A   195     O3P  TPO A   197              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  36       77.37     35.30                                   
REMARK 500    ALA A  38      170.93    175.23                                   
REMARK 500    PHE A  54      -17.18   -148.01                                   
REMARK 500    ARG A  56      128.32    146.22                                   
REMARK 500    GLU A  64       -9.03    -57.57                                   
REMARK 500    SER A  65       -8.80   -140.15                                   
REMARK 500    PHE A 110     -178.27    175.61                                   
REMARK 500    ASP A 166       54.89   -140.60                                   
REMARK 500    LYS A 168      149.79    179.82                                   
REMARK 500    ASN A 171        1.90    -69.09                                   
REMARK 500    ASP A 184       73.35     53.68                                   
REMARK 500    PRO A 202      -62.49    -24.40                                   
REMARK 500    LYS A 217       -8.62    -59.28                                   
REMARK 500    ALA A 240     -160.41   -167.94                                   
REMARK 500    LEU A 284      158.43    -46.76                                   
REMARK 500    ILE A 291      -61.68    -99.35                                   
REMARK 500    ASP A 323       54.53    -58.13                                   
REMARK 500    SER A 325      144.50    165.22                                   
REMARK 500    ASN A 326     -142.46     85.42                                   
REMARK 500    ALA A 327     -152.43     75.72                                   
REMARK 500    GLU A 332       83.59    -63.02                                   
REMARK 500    SER B 369     -175.84    -63.05                                   
REMARK 500    ARG B 371       45.82    -88.48                                   
REMARK 500    HIS B 379       63.41    152.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE WILD TYPE PROTEIN COMPLEXED WITH            
REMARK 900 THE PEPTIDE INHIBITOR PKI(5-24) AND MNATP                            
REMARK 900 RELATED ID: 1J3H   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF APOENZYME OF PKA                                
DBREF  2QUR A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  2QUR B  361   380  UNP    P63248   IPKA_MOUSE       6     25             
SEQADV 2QUR TPO A  197  UNP  P05132    THR   198 MODIFIED RESIDUE               
SEQADV 2QUR PRO A  285  UNP  P05132    LYS   286 ENGINEERED                     
SEQADV 2QUR ALA A  327  UNP  P05132    PHE   328 ENGINEERED                     
SEQADV 2QUR SEP A  338  UNP  P05132    SER   339 MODIFIED RESIDUE               
SEQRES   1 A  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 A  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 A  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 A  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 A  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 A  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 A  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 A  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 A  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 A  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 A  350  HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA          
SEQRES  12 A  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 A  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 A  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 A  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 A  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 A  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 A  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 A  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 A  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 A  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 A  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU PRO ASN          
SEQRES  23 A  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 A  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 A  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 A  350  ASN ALA ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 A  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 B   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 B   20  ARG ARG ASN ALA ILE HIS ASP                                  
MODRES 2QUR TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 2QUR SEP A  338  SER  PHOSPHOSERINE                                      
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    ADP  B   1      27                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  ADP    C10 H15 N5 O10 P2                                            
FORMUL   4  HOH   *24(H2 O)                                                     
HELIX    1   1 GLN A   12  THR A   32  1                                  21    
HELIX    2   2 GLN A   39  ASP A   41  5                                   3    
HELIX    3   3 LYS A   76  LEU A   82  1                                   7    
HELIX    4   4 GLN A   84  GLN A   96  1                                  13    
HELIX    5   5 GLU A  127  GLY A  136  1                                  10    
HELIX    6   6 SER A  139  LEU A  160  1                                  22    
HELIX    7   7 LYS A  168  GLU A  170  5                                   3    
HELIX    8   8 THR A  201  LEU A  205  5                                   5    
HELIX    9   9 ALA A  206  LEU A  211  1                                   6    
HELIX   10  10 LYS A  217  GLY A  234  1                                  18    
HELIX   11  11 GLN A  242  GLY A  253  1                                  12    
HELIX   12  12 SER A  262  LEU A  273  1                                  12    
HELIX   13  13 VAL A  288  ASN A  293  1                                   6    
HELIX   14  14 HIS A  294  ALA A  298  5                                   5    
HELIX   15  15 ASP A  301  GLN A  307  1                                   7    
HELIX   16  16 CYS A  343  THR A  348  1                                   6    
HELIX   17  17 THR B  361  SER B  369  1                                   9    
SHEET    1   A 5 PHE A  43  GLY A  50  0                                        
SHEET    2   A 5 VAL A  57  HIS A  62 -1  O  LEU A  59   N  ILE A  46           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  TYR A  69   N  VAL A  60           
SHEET    4   A 5 ASN A 115  GLU A 121 -1  O  MET A 118   N  LYS A  72           
SHEET    5   A 5 LEU A 106  LYS A 111 -1  N  PHE A 110   O  TYR A 117           
SHEET    1   B 2 LEU A 162  ILE A 163  0                                        
SHEET    2   B 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1   C 2 LEU A 172  ILE A 174  0                                        
SHEET    2   C 2 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.33  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.33  
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.33  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
SITE     1 AC1  8 LEU A  49  ALA A  70  GLU A 121  TYR A 122                    
SITE     2 AC1  8 GLU A 127  ASN A 171  ASP A 184  ARG B 374                    
CRYST1   57.560   78.500  100.630  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      0.017373  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012739  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009937        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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