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Database: PDB
Entry: 3QAL
LinkDB: 3QAL
Original site: 3QAL 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       11-JAN-11   3QAL              
TITLE     CRYSTAL STRUCTURE OF ARG280ALA MUTANT OF CATALYTIC SUBUNIT OF CAMP-   
TITLE    2 DEPENDENT PROTEIN KINASE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: E;                                                            
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROTEIN KINASE INHIBITOR;                                  
COMPND  10 CHAIN: I;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 6-23;                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES                                                       
KEYWDS    PROTEIN KINASE, GLU208/ARG280 PAIR, PKA, TRANSFERASE-TRANSFERASE      
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.YANG,J.WU,J.STEICHEN,S.S.TAYLOR                                     
REVDAT   2   19-JUN-13 3QAL    1       JRNL                                     
REVDAT   1   07-DEC-11 3QAL    0                                                
JRNL        AUTH   J.YANG,J.WU,J.M.STEICHEN,A.P.KORNEV,M.S.DEAL,S.LI,           
JRNL        AUTH 2 B.SANKARAN,V.L.WOODS,S.S.TAYLOR                              
JRNL        TITL   A CONSERVED GLU-ARG SALT BRIDGE CONNECTS COEVOLVED MOTIFS    
JRNL        TITL 2 THAT DEFINE THE EUKARYOTIC PROTEIN KINASE FOLD.              
JRNL        REF    J.MOL.BIOL.                   V. 415   666 2012              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   22138346                                                     
JRNL        DOI    10.1016/J.JMB.2011.11.035                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 1.70                           
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)   (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 48566                          
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) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2428                            
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            : 2839                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 373                                     
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) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
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 3QAL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063402.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48566                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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: PDB ENTRY 1ATP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13-15% MPD, 100 MM BICINE, 10 MM DTT,    
REMARK 280  PH 8.0, 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       28.87900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.85750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.04100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.85750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.87900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.04100            
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 300 REMARK: ONE MOLECULE PER ASYMMETRICAL UNIT                           
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: 3060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I                                  
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     ALA E     5                                                      
REMARK 465     ALA E     6                                                      
REMARK 465     LYS E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     GLN E    12                                                      
REMARK 465     GLU E    13                                                      
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     LYS E  16    CG   CD   CE   NZ                                   
REMARK 470     GLU E  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  21    CG   CD   CE   NZ                                   
REMARK 470     GLU E  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  81    CG   CD   CE   NZ                                   
REMARK 470     LYS E 105    CG   CD   CE   NZ                                   
REMARK 470     GLN E 176    CG   CD   OE1  NE2                                  
REMARK 470     LYS E 217    CG   CD   CE   NZ                                   
REMARK 470     LYS E 254    CG   CD   CE   NZ                                   
REMARK 470     ARG E 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL E 275    CG1  CG2                                            
REMARK 470     ASP E 276    CG   OD1  OD2                                       
REMARK 470     LEU E 277    CG   CD1  CD2                                       
REMARK 470     THR E 278    OG1  CG2                                            
REMARK 470     LYS E 279    CG   CD   CE   NZ                                   
REMARK 470     ASN E 283    CG   OD1  ND2                                       
REMARK 470     LEU E 284    CG   CD1  CD2                                       
REMARK 470     LYS E 285    CG   CD   CE   NZ                                   
REMARK 470     ASN E 286    CG   OD1  ND2                                       
REMARK 470     LYS E 295    CG   CD   CE   NZ                                   
REMARK 470     LYS E 317    CG   CD   CE   NZ                                   
REMARK 470     PHE E 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS E 319    CG   CD   CE   NZ                                   
REMARK 470     GLU E 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 334    CG   CD   OE1  OE2                                  
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    ASP E 166       44.13   -152.86                                   
REMARK 500    ASP E 184       80.89     59.31                                   
REMARK 500    ASN E 216     -158.56   -131.04                                   
REMARK 500    LEU E 273       32.38    -95.97                                   
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 E 353  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP E 351   O3G                                                    
REMARK 620 2 HOH E 608   O   107.6                                              
REMARK 620 3 ATP E 351   O1B  88.7  89.6                                        
REMARK 620 4 HOH E 818   O    93.2  93.6 175.5                                  
REMARK 620 5 ASP E 184   OD1 154.2  98.1  89.6  87.0                            
REMARK 620 6 ASP E 184   OD2  94.6 157.2  85.6  90.2  59.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 352  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP E 351   O2A                                                    
REMARK 620 2 ASN E 171   OD1 102.0                                              
REMARK 620 3 HOH E 620   O    87.6  90.7                                        
REMARK 620 4 ASP E 184   OD2  88.9  95.2 173.7                                  
REMARK 620 5 ATP E 351   O2G 140.7 117.3  93.8  85.6                            
REMARK 620 6 ATP E 351   O3B  78.1 179.2  88.5  85.6  62.7                      
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 ATP E 351                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E 352                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E 353                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF   PROTEIN KINASE       
REMARK 800  INHIBITOR, ALPHA, ISOFORM CRA_A                                     
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC SUBUNIT OF CAMP-DEPENDENT             
REMARK 900 PROTEIN KINASE                                                       
REMARK 900 RELATED ID: 3QAM   RELATED DB: PDB                                   
DBREF  3QAL E    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  3QAL I    5    22  UNP    Q3UTL0   Q3UTL0_MOUSE     6     23             
SEQADV 3QAL ALA E  280  UNP  P05132    ARG   281 ENGINEERED MUTATION            
SEQRES   1 E  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 E  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 E  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 E  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 E  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 E  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 E  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 E  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 E  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 E  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 E  350  HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA          
SEQRES  12 E  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 E  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 E  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 E  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 E  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 E  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 E  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 E  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 E  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 E  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 E  350  GLN VAL ASP LEU THR LYS ALA PHE GLY ASN LEU LYS ASN          
SEQRES  23 E  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 E  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 E  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 E  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 E  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 I   18  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 I   18  ARG ARG ASN ALA ILE                                          
MODRES 3QAL TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 3QAL SEP E  338  SER  PHOSPHOSERINE                                      
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET    ATP  E 351      31                                                       
HET     MG  E 352       1                                                       
HET     MG  E 353       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  ATP    C10 H16 N5 O13 P3                                            
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  HOH   *373(H2 O)                                                    
HELIX    1   1 SER E   14  THR E   32  1                                  19    
HELIX    2   2 GLN E   39  ASP E   41  5                                   3    
HELIX    3   3 LYS E   76  LEU E   82  1                                   7    
HELIX    4   4 GLN E   84  GLN E   96  1                                  13    
HELIX    5   5 GLU E  127  GLY E  136  1                                  10    
HELIX    6   6 SER E  139  LEU E  160  1                                  22    
HELIX    7   7 LYS E  168  GLU E  170  5                                   3    
HELIX    8   8 THR E  201  LEU E  205  5                                   5    
HELIX    9   9 ALA E  206  LEU E  211  1                                   6    
HELIX   10  10 LYS E  217  GLY E  234  1                                  18    
HELIX   11  11 GLN E  242  GLY E  253  1                                  12    
HELIX   12  12 SER E  262  LEU E  273  1                                  12    
HELIX   13  13 VAL E  288  ASN E  293  1                                   6    
HELIX   14  14 HIS E  294  ALA E  298  5                                   5    
HELIX   15  15 ASP E  301  GLN E  307  1                                   7    
HELIX   16  16 THR I    5  ALA I   12  1                                   8    
SHEET    1   A 5 PHE E  43  THR E  51  0                                        
SHEET    2   A 5 ARG E  56  HIS E  62 -1  O  LEU E  59   N  LYS E  47           
SHEET    3   A 5 HIS E  68  ASP E  75 -1  O  ILE E  73   N  ARG E  56           
SHEET    4   A 5 ASN E 115  GLU E 121 -1  O  MET E 120   N  ALA E  70           
SHEET    5   A 5 LEU E 106  LYS E 111 -1  N  PHE E 110   O  TYR E 117           
SHEET    1   B 2 LEU E 162  ILE E 163  0                                        
SHEET    2   B 2 LYS E 189  ARG E 190 -1  O  LYS E 189   N  ILE E 163           
SHEET    1   C 2 LEU E 172  ILE E 174  0                                        
SHEET    2   C 2 ILE E 180  VAL E 182 -1  O  GLN E 181   N  LEU E 173           
LINK         C   TRP E 196                 N   TPO E 197     1555   1555  1.33  
LINK         C   TPO E 197                 N   LEU E 198     1555   1555  1.33  
LINK         C   VAL E 337                 N   SEP E 338     1555   1555  1.33  
LINK         C   SEP E 338                 N   ILE E 339     1555   1555  1.33  
LINK         O3G ATP E 351                MG    MG E 353     1555   1555  1.98  
LINK         O2A ATP E 351                MG    MG E 352     1555   1555  1.99  
LINK        MG    MG E 353                 O   HOH E 608     1555   1555  2.03  
LINK         OD1 ASN E 171                MG    MG E 352     1555   1555  2.04  
LINK        MG    MG E 352                 O   HOH E 620     1555   1555  2.06  
LINK         O1B ATP E 351                MG    MG E 353     1555   1555  2.07  
LINK        MG    MG E 353                 O   HOH E 818     1555   1555  2.07  
LINK         OD2 ASP E 184                MG    MG E 352     1555   1555  2.08  
LINK         O2G ATP E 351                MG    MG E 352     1555   1555  2.14  
LINK         OD1 ASP E 184                MG    MG E 353     1555   1555  2.19  
LINK         OD2 ASP E 184                MG    MG E 353     1555   1555  2.21  
LINK         O3B ATP E 351                MG    MG E 352     1555   1555  2.62  
SITE     1 AC1 30 GLY E  50  GLY E  52  SER E  53  PHE E  54                    
SITE     2 AC1 30 GLY E  55  VAL E  57  ALA E  70  LYS E  72                    
SITE     3 AC1 30 VAL E 104  MET E 120  GLU E 121  VAL E 123                    
SITE     4 AC1 30 GLU E 127  ASP E 166  LYS E 168  GLU E 170                    
SITE     5 AC1 30 ASN E 171  LEU E 173  THR E 183  ASP E 184                    
SITE     6 AC1 30 PHE E 327   MG E 352   MG E 353  HOH E 608                    
SITE     7 AC1 30 HOH E 620  HOH E 724  HOH E 818  ARG I  18                    
SITE     8 AC1 30 ASN I  20  ALA I  21                                          
SITE     1 AC2  4 ASN E 171  ASP E 184  ATP E 351  HOH E 620                    
SITE     1 AC3  4 ASP E 184  ATP E 351  HOH E 608  HOH E 818                    
SITE     1 AC4 61 THR E  51  GLY E  52  SER E  53  GLU E  86                    
SITE     2 AC4 61 LEU E  89  ARG E  93  GLU E 127  PHE E 129                    
SITE     3 AC4 61 ARG E 133  LYS E 168  PRO E 169  GLU E 170                    
SITE     4 AC4 61 PHE E 187  LYS E 189  ARG E 190  VAL E 191                    
SITE     5 AC4 61 LYS E 192  GLY E 200  THR E 201  PRO E 202                    
SITE     6 AC4 61 GLU E 203  LEU E 205  GLU E 230  TYR E 235                    
SITE     7 AC4 61 PRO E 236  PHE E 239  ALA E 240  ASP E 241                    
SITE     8 AC4 61 ILE E 246  TYR E 247  TYR E 330  GLU E 349                    
SITE     9 AC4 61 ATP E 351  HOH E 677  HOH E 761  HOH E 767                    
SITE    10 AC4 61 HOH E 784  HOH E 826  HOH E 878  HOH E 922                    
SITE    11 AC4 61 HOH I 623  HOH I 625  HOH I 626  HOH I 627                    
SITE    12 AC4 61 HOH I 755  HOH I 768  HOH I 779  HOH I 816                    
SITE    13 AC4 61 HOH I 839  HOH I 841  HOH I 845  HOH I 856                    
SITE    14 AC4 61 HOH I 858  HOH I 882  HOH I 888  HOH I 890                    
SITE    15 AC4 61 HOH I 923  HOH I 932  HOH I 966  HOH I 967                    
SITE    16 AC4 61 HOH I 971                                                     
CRYST1   57.758   80.082   97.715  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      0.017314  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012487  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010234        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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