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Database: PDB
Entry: 2QVS
LinkDB: 2QVS
Original site: 2QVS 
HEADER    TRANSFERASE/TRANSFERASE REGULATOR       08-AUG-07   2QVS              
TITLE     CRYSTAL STRUCTURE OF TYPE IIA HOLOENZYME 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: E;                                                            
COMPND   5 SYNONYM: PKA C-ALPHA;                                                
COMPND   6 EC: 2.7.11.11;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA                
COMPND  10 REGULATORY SUBUNIT;                                                  
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSET;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: PRKAR2A;                                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PRSET                                     
KEYWDS    CRYSTAL STRUCTURE, CAMP-DEPENDENT PROTEIN KINASE, TYPE IIA            
KEYWDS   2 HOLOENZYME, ISOFORM DIVERSITY, ALTERNATIVE SPLICING, ATP-            
KEYWDS   3 BINDING, CYTOPLASM, LIPOPROTEIN, MYRISTATE, NUCLEOTIDE-              
KEYWDS   4 BINDING, NUCLEUS, PHOSPHORYLATION, SERINE/THREONINE-PROTEIN          
KEYWDS   5 KINASE, TRANSFERASE, ACETYLATION, CAMP-BINDING,                      
KEYWDS   6 TRANSFERASE/TRANSFERASE REGULATOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.WU,S.H.J.BROWN,S.VON DAAKE,S.S.TAYLOR                               
REVDAT   2   24-FEB-09 2QVS    1       VERSN                                    
REVDAT   1   23-OCT-07 2QVS    0                                                
JRNL        AUTH   J.WU,S.H.J.BROWN,S.VON DAAKE,S.S.TAYLOR                      
JRNL        TITL   PKA TYPE IIALPHA HOLOENZYME REVEALS A                        
JRNL        TITL 2 COMBINATORIAL STRATEGY FOR ISOFORM DIVERSITY.                
JRNL        REF    SCIENCE                       V. 318   274 2007              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   17932298                                                     
JRNL        DOI    10.1126/SCIENCE.1146447                                      
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)   (%) : 78.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 26790                          
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                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1309                            
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) (%) : 95.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 54                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.035                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4878                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 181                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.82000                                             
REMARK   3    B22 (A**2) : 3.65000                                              
REMARK   3    B33 (A**2) : 0.17000                                              
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) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.29                            
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) : 0.38                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.28                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.96                            
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 2QVS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044117.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 200.0                              
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
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                  : NULL                               
REMARK 200  OPTICS                         : KOHZU: DOUBLE CRYSTAL SI(111)      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33730                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.1000                            
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     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.45400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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   (%): 61.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M SODIUM FORMATE, PH 5.5, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295.5K                         
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       43.95000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.45000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.95000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.45000            
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: 3510 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 E     1                                                      
REMARK 465     ASN E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     ALA E     4                                                      
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     LYS E   319                                                      
REMARK 465     GLY E   320                                                      
REMARK 465     PRO E   321                                                      
REMARK 465     GLY E   322                                                      
REMARK 465     ASP E   323                                                      
REMARK 465     THR E   324                                                      
REMARK 465     SER E   325                                                      
REMARK 465     ASN E   326                                                      
REMARK 465     PHE E   327                                                      
REMARK 465     ASP E   328                                                      
REMARK 465     ASP E   329                                                      
REMARK 465     TYR E   330                                                      
REMARK 465     GLU E   331                                                      
REMARK 465     ASN B   110                                                      
REMARK 465     ASP B   111                                                      
REMARK 465     PRO B   112                                                      
REMARK 465     ARG B   113                                                      
REMARK 465     LEU B   393                                                      
REMARK 465     ASP B   394                                                      
REMARK 465     LEU B   395                                                      
REMARK 465     MET B   396                                                      
REMARK 465     ASP B   397                                                      
REMARK 465     PRO B   398                                                      
REMARK 465     GLY B   399                                                      
REMARK 465     GLN B   400                                                      
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     GLN E  42    CG   CD   OE1  NE2                                  
REMARK 470     PHE E  43    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP E  44    CG   OD1  OD2                                       
REMARK 470     ARG E  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E  46    CG1  CG2  CD1                                       
REMARK 470     LYS E  47    CG   CD   CE   NZ                                   
REMARK 470     THR E  48    OG1  CG2                                            
REMARK 470     LEU E  49    CG   CD1  CD2                                       
REMARK 470     THR E  51    OG1  CG2                                            
REMARK 470     SER E  53    OG                                                  
REMARK 470     PHE E  54    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG E  56    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL E  57    CG1  CG2                                            
REMARK 470     MET E  58    CG   SD   CE                                        
REMARK 470     VAL E  60    CG1  CG2                                            
REMARK 470     LYS E  61    CG   CD   CE   NZ                                   
REMARK 470     LYS E  63    CG   CD   CE   NZ                                   
REMARK 470     GLU E  64    CG   CD   OE1  OE2                                  
REMARK 470     SER E  65    OG                                                  
REMARK 470     MET E  71    CG   SD   CE                                        
REMARK 470     LYS E  72    CG   CD   CE   NZ                                   
REMARK 470     ILE E  73    CG1  CG2  CD1                                       
REMARK 470     LEU E  74    CG   CD1  CD2                                       
REMARK 470     ASP E  75    CG   OD1  OD2                                       
REMARK 470     LYS E  76    CG   CD   CE   NZ                                   
REMARK 470     GLN E  77    CG   CD   OE1  NE2                                  
REMARK 470     LYS E  78    CG   CD   CE   NZ                                   
REMARK 470     VAL E  79    CG1  CG2                                            
REMARK 470     VAL E  80    CG1  CG2                                            
REMARK 470     LYS E  81    CG   CD   CE   NZ                                   
REMARK 470     LEU E  82    CG   CD1  CD2                                       
REMARK 470     LYS E 111    CG   CD   CE   NZ                                   
REMARK 470     ASP E 112    CG   OD1  OD2                                       
REMARK 470     ASN E 113    CG   OD1  ND2                                       
REMARK 470     SER E 114    OG                                                  
REMARK 470     ASN E 115    CG   OD1  ND2                                       
REMARK 470     LEU E 116    CG   CD1  CD2                                       
REMARK 470     TYR E 117    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET E 118    CG   SD   CE                                        
REMARK 470     VAL E 119    CG1  CG2                                            
REMARK 470     GLU E 332    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 334    CG   CD   OE1  OE2                                  
REMARK 470     ILE E 335    CG1  CG2  CD1                                       
REMARK 470     ARG E 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E 339    CG1  CG2  CD1                                       
REMARK 470     LYS E 345    CG   CD   CE   NZ                                   
REMARK 470     GLU E 349    CG   CD   OE1  OE2                                  
REMARK 470     SER B 308    OG                                                  
REMARK 470     LYS B 309    CG   CD   CE   NZ                                   
REMARK 470     THR B 310    OG1  CG2                                            
REMARK 470     LYS B 311    CG   CD   CE   NZ                                   
REMARK 470     SER B 312    OG                                                  
REMARK 470     ASN B 313    CG   OD1  ND2                                       
REMARK 470     LYS B 314    CG   CD   CE   NZ                                   
REMARK 470     ASN B 315    CG   OD1  ND2                                       
REMARK 470     ASN B 318    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL E  80   CB  -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    LYS E  81   N   -  CA  -  CB  ANGL. DEV. =  16.4 DEGREES          
REMARK 500    LYS E  81   CA  -  C   -  N   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ASN E 113   CB  -  CA  -  C   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    SER E 114   CB  -  CA  -  C   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    SER E 114   N   -  CA  -  CB  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    SER E 114   CA  -  C   -  O   ANGL. DEV. =  18.9 DEGREES          
REMARK 500    ASN E 115   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    ASN E 115   N   -  CA  -  C   ANGL. DEV. =  23.8 DEGREES          
REMARK 500    SER E 114   CA  -  C   -  N   ANGL. DEV. = -21.6 DEGREES          
REMARK 500    LEU E 116   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    LEU E 116   CA  -  C   -  O   ANGL. DEV. =  23.2 DEGREES          
REMARK 500    LEU E 116   CA  -  C   -  N   ANGL. DEV. = -23.6 DEGREES          
REMARK 500    LYS B 314   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    LYS B 314   N   -  CA  -  C   ANGL. DEV. =  20.7 DEGREES          
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    THR E  32       62.36   -164.49                                   
REMARK 500    ASN E  36       85.65     11.41                                   
REMARK 500    THR E  37      -75.10    -84.71                                   
REMARK 500    ASP E  44     -111.55    -86.74                                   
REMARK 500    ARG E  45      138.95    172.40                                   
REMARK 500    ILE E  46     -118.91   -126.54                                   
REMARK 500    LYS E  47     -169.69    -67.34                                   
REMARK 500    THR E  48       61.16   -150.31                                   
REMARK 500    THR E  51     -109.64    -99.09                                   
REMARK 500    SER E  53       11.86   -161.92                                   
REMARK 500    LYS E  63      -97.16    -78.02                                   
REMARK 500    VAL E  79     -159.77    -61.92                                   
REMARK 500    VAL E  80      -28.07     71.61                                   
REMARK 500    LYS E  81     -133.27    -95.65                                   
REMARK 500    LEU E  82     -139.73     53.26                                   
REMARK 500    HIS E  87        1.50    -57.12                                   
REMARK 500    ASP E 112      107.95    160.60                                   
REMARK 500    ASN E 113      -27.78     53.29                                   
REMARK 500    ASN E 115      109.86     37.98                                   
REMARK 500    LEU E 116       89.98     87.83                                   
REMARK 500    ASP E 166       33.61   -150.39                                   
REMARK 500    LYS E 168      150.15    176.81                                   
REMARK 500    ASP E 184       91.61     66.05                                   
REMARK 500    PHE E 185       33.08    -98.74                                   
REMARK 500    ASN E 216     -121.38   -153.13                                   
REMARK 500    LEU E 273       53.75    -93.70                                   
REMARK 500    GLU E 333     -162.89   -162.36                                   
REMARK 500    LYS E 342     -105.31    -95.34                                   
REMARK 500    CYS E 343       19.54    -52.05                                   
REMARK 500    GLU E 346      -37.82   -166.41                                   
REMARK 500    GLU B 107      102.40    164.93                                   
REMARK 500    GLU B 108      110.02    -12.85                                   
REMARK 500    LYS B 137      -49.59    -28.79                                   
REMARK 500    ASP B 159       -4.51     83.58                                   
REMARK 500    ASP B 187     -138.81     63.35                                   
REMARK 500    ASP B 280      132.24    -35.74                                   
REMARK 500    SER B 299      143.26   -174.62                                   
REMARK 500    SER B 308       77.04    -55.40                                   
REMARK 500    LYS B 309      -43.77   -130.09                                   
REMARK 500    THR B 310       50.57    -69.57                                   
REMARK 500    SER B 312      -85.90    157.53                                   
REMARK 500    ASN B 313       81.89   -176.65                                   
REMARK 500    LYS B 314       74.29     69.36                                   
REMARK 500    ASN B 315      179.13    135.19                                   
REMARK 500    GLN B 319     -123.79   -157.86                                   
REMARK 500    ASN B 340       56.05   -141.81                                   
REMARK 500    SER B 391      -79.69    -46.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 427        DISTANCE =  5.86 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1U7E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RIA(91-244):C COMPLEX OF CAMP-                  
REMARK 900 DEPENDENT PROTEIN KINASE                                             
REMARK 900 RELATED ID: 1CX4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE TYPE II BETA REGULATORY SUBUNIT OF          
REMARK 900 CAMP-DEPENDENT PROTEIN KINASE                                        
REMARK 900 RELATED ID: 1RGS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE TYPE IA REGULATORY SUBUNIT OF CAMP          
REMARK 900 -DEPENDENT PROTEIN KINASE                                            
DBREF  2QVS E    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  2QVS B   91   400  UNP    P12367   KAP2_MOUSE      92    401             
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 ARG 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 B  310  THR ARG ARG VAL SER VAL CYS ALA GLU THR PHE ASN PRO          
SEQRES   2 B  310  ASP GLU GLU GLU GLU ASP ASN ASP PRO ARG VAL VAL HIS          
SEQRES   3 B  310  PRO LYS THR ASP GLU GLN ARG CYS ARG LEU GLN GLU ALA          
SEQRES   4 B  310  CYS LYS ASP ILE LEU LEU PHE LYS ASN LEU ASP GLN GLU          
SEQRES   5 B  310  GLN LEU SER GLN VAL LEU ASP ALA MET PHE GLU LYS ILE          
SEQRES   6 B  310  VAL LYS THR ASP GLU HIS VAL ILE ASP GLN GLY ASP ASP          
SEQRES   7 B  310  GLY ASP ASN PHE TYR VAL ILE GLU ARG GLY THR TYR ASP          
SEQRES   8 B  310  ILE LEU VAL THR LYS ASP ASN GLN THR ARG SER VAL GLY          
SEQRES   9 B  310  GLN TYR ASP ASN ARG GLY SER PHE GLY GLU LEU ALA LEU          
SEQRES  10 B  310  MET TYR ASN THR PRO ARG ALA ALA THR ILE ILE ALA THR          
SEQRES  11 B  310  SER GLU GLY SER LEU TRP GLY LEU ASP ARG VAL THR PHE          
SEQRES  12 B  310  ARG ARG ILE ILE VAL LYS ASN ASN ALA LYS LYS ARG LYS          
SEQRES  13 B  310  MET PHE GLU SER PHE ILE GLU SER VAL PRO LEU PHE LYS          
SEQRES  14 B  310  SER LEU GLU MET SER GLU ARG MET LYS ILE VAL ASP VAL          
SEQRES  15 B  310  ILE GLY GLU LYS ILE TYR LYS ASP GLY GLU ARG ILE ILE          
SEQRES  16 B  310  ALA GLN GLY GLU LYS ALA ASP SER PHE TYR ILE ILE GLU          
SEQRES  17 B  310  SER GLY GLU VAL SER ILE LEU ILE ARG SER LYS THR LYS          
SEQRES  18 B  310  SER ASN LYS ASN GLY GLY ASN GLN GLU VAL GLU ILE ALA          
SEQRES  19 B  310  HIS CYS HIS LYS GLY GLN TYR PHE GLY GLU LEU ALA LEU          
SEQRES  20 B  310  VAL THR ASN LYS PRO ARG ALA ALA SER ALA TYR GLY VAL          
SEQRES  21 B  310  GLY ASP VAL LYS CYS LEU VAL MET ASP VAL GLN ALA PHE          
SEQRES  22 B  310  GLU ARG LEU LEU GLY PRO CYS MET ASP ILE MET LYS ARG          
SEQRES  23 B  310  ASN ILE SER HIS TYR GLU GLU GLN LEU VAL LYS MET PHE          
SEQRES  24 B  310  GLY SER ASN LEU ASP LEU MET ASP PRO GLY GLN                  
MODRES 2QVS TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 2QVS SEP E  338  SER  PHOSPHOSERINE                                      
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  HOH   *181(H2 O)                                                    
HELIX    1   1 GLU E   13  GLU E   31  1                                  19    
HELIX    2   2 GLN E   39  PHE E   43  5                                   5    
HELIX    3   3 ILE E   85  VAL E   98  1                                  14    
HELIX    4   4 MET E  128  GLY E  136  1                                   9    
HELIX    5   5 SER E  139  LEU E  160  1                                  22    
HELIX    6   6 LYS E  168  GLU E  170  5                                   3    
HELIX    7   7 THR E  201  LEU E  205  5                                   5    
HELIX    8   8 ALA E  206  LEU E  211  1                                   6    
HELIX    9   9 LYS E  217  GLY E  234  1                                  18    
HELIX   10  10 GLN E  242  GLY E  253  1                                  12    
HELIX   11  11 SER E  262  LEU E  273  1                                  12    
HELIX   12  12 VAL E  288  ASN E  293  1                                   6    
HELIX   13  13 HIS E  294  ALA E  298  5                                   5    
HELIX   14  14 ASP E  301  GLN E  307  1                                   7    
HELIX   15  15 LYS E  342  GLU E  346  5                                   5    
HELIX   16  16 THR B  119  LYS B  131  1                                  13    
HELIX   17  17 ILE B  133  ASN B  138  1                                   6    
HELIX   18  18 ASP B  140  MET B  151  1                                  12    
HELIX   19  19 GLY B  203  MET B  208  5                                   6    
HELIX   20  20 ARG B  230  SER B  254  1                                  25    
HELIX   21  21 VAL B  255  LYS B  259  5                                   5    
HELIX   22  22 GLU B  262  ILE B  273  1                                  12    
HELIX   23  23 GLY B  333  VAL B  338  5                                   6    
HELIX   24  24 VAL B  360  GLY B  368  1                                   9    
HELIX   25  25 PRO B  369  ASN B  377  1                                   9    
HELIX   26  26 HIS B  380  GLY B  390  1                                  11    
SHEET    1   A 4 ARG E  56  LYS E  61  0                                        
SHEET    2   A 4 HIS E  68  ILE E  73 -1  O  TYR E  69   N  VAL E  60           
SHEET    3   A 4 TYR E 117  GLU E 121 -1  O  MET E 120   N  ALA E  70           
SHEET    4   A 4 LEU E 106  PHE E 110 -1  N  PHE E 108   O  VAL E 119           
SHEET    1   B 3 GLY E 126  GLU E 127  0                                        
SHEET    2   B 3 LEU E 172  ILE E 174 -1  O  ILE E 174   N  GLY E 126           
SHEET    3   B 3 ILE E 180  VAL E 182 -1  O  GLN E 181   N  LEU E 173           
SHEET    1   C 2 LEU E 162  ILE E 163  0                                        
SHEET    2   C 2 LYS E 189  ARG E 190 -1  O  LYS E 189   N  ILE E 163           
SHEET    1   D 2 CYS E 199  GLY E 200  0                                        
SHEET    2   D 2 VAL B  96  CYS B  97 -1  O  VAL B  96   N  GLY E 200           
SHEET    1   E 4 PHE B 152  VAL B 156  0                                        
SHEET    2   E 4 GLY B 223  ASP B 229 -1  O  GLY B 227   N  PHE B 152           
SHEET    3   E 4 ASN B 171  ARG B 177 -1  N  VAL B 174   O  TRP B 226           
SHEET    4   E 4 SER B 201  PHE B 202 -1  O  PHE B 202   N  TYR B 173           
SHEET    1   F 4 HIS B 161  ILE B 163  0                                        
SHEET    2   F 4 THR B 216  ALA B 219 -1  O  ILE B 217   N  VAL B 162           
SHEET    3   F 4 THR B 179  LYS B 186 -1  N  LEU B 183   O  THR B 216           
SHEET    4   F 4 GLN B 189  ASP B 197 -1  O  GLY B 194   N  ILE B 182           
SHEET    1   G 4 GLY B 274  TYR B 278  0                                        
SHEET    2   G 4 SER B 346  ASP B 359 -1  O  VAL B 353   N  TYR B 278           
SHEET    3   G 4 SER B 293  ILE B 306 -1  N  GLU B 301   O  VAL B 350           
SHEET    4   G 4 VAL B 321  HIS B 327 -1  O  VAL B 321   N  ILE B 306           
SHEET    1   H 4 ARG B 283  ILE B 285  0                                        
SHEET    2   H 4 SER B 346  ASP B 359 -1  O  ALA B 347   N  ILE B 284           
SHEET    3   H 4 SER B 293  ILE B 306 -1  N  GLU B 301   O  VAL B 350           
SHEET    4   H 4 TYR B 331  PHE B 332 -1  O  PHE B 332   N  TYR B 295           
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  
CRYST1   87.900   92.900  118.000  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      0.011377  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010764  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008475        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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