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Database: PDB
Entry: 3IDB
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Original site: 3IDB 
HEADER    TRANSFERASE                             20-JUL-09   3IDB              
TITLE     CRYSTAL STRUCTURE OF (108-268)RIIB:C HOLOENZYME OF CAMP-DEPENDENT     
TITLE    2 PROTEIN KINASE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ISOFORM 1 (C-ALPHA-1): UNP RESIDUES 2-351;                 
COMPND   5 SYNONYM: PKA C-ALPHA;                                                
COMPND   6 EC: 2.7.11.11;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: (108-268)RIIB:C HOLOENZYME OF CAMP-DEPENDENT PROTEIN  
COMPND   9 KINASE;                                                              
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE II-BETA REGULATORY      
COMPND  12 SUBUNIT;                                                             
COMPND  13 CHAIN: B;                                                            
COMPND  14 FRAGMENT: UNP RESIDUES 108-268;                                      
COMPND  15 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: PKACA, PRKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PRSET;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  12 ORGANISM_COMMON: RAT;                                                
SOURCE  13 ORGANISM_TAXID: 10116;                                               
SOURCE  14 GENE: PRKAR2B;                                                       
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PRSET                                     
KEYWDS    PKA, CAMP, SPR, AFFINITY, KINASE, LINKER, RII HOLOENZYME, ALTERNATIVE 
KEYWDS   2 SPLICING, ATP-BINDING, CYTOPLASM, LIPOPROTEIN, MYRISTATE,            
KEYWDS   3 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, SERINE/THREONINE-       
KEYWDS   4 PROTEIN KINASE, TRANSFERASE, ACETYLATION, CAMP-BINDING               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.H.J.BROWN,J.WU,C.KIM,K.ALBERTO,S.S.TAYLOR                           
REVDAT   3   24-JUL-19 3IDB    1       REMARK LINK                              
REVDAT   2   10-NOV-09 3IDB    1       JRNL                                     
REVDAT   1   29-SEP-09 3IDB    0                                                
JRNL        AUTH   S.H.BROWN,J.WU,C.KIM,K.ALBERTO,S.S.TAYLOR                    
JRNL        TITL   NOVEL ISOFORM-SPECIFIC INTERFACES REVEALED BY PKA RIIBETA    
JRNL        TITL 2 HOLOENZYME STRUCTURES.                                       
JRNL        REF    J.MOL.BIOL.                   V. 393  1070 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19748511                                                     
JRNL        DOI    10.1016/J.JMB.2009.09.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 88992                          
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 + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 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   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3926                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 398                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.46000                                              
REMARK   3    B22 (A**2) : 3.16000                                              
REMARK   3    B33 (A**2) : -3.62000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.32000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3IDB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054268.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
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) : 1.5200                             
REMARK 200  MONOCHROMATOR                  : KOHZU: DOUBLE CRYSTAL SI(111)      
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   : 88992                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.620                              
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     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ATP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 3350, 40 MM BIS-TRIS PH 7.5,      
REMARK 280  0.05 MM NA ACETATE, VAPOR DIFFUSION UNDER OIL (VDUO),               
REMARK 280  TEMPERATURE 298.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       86.66050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.86650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       86.66050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.86650            
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: 2710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.9 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     GLU B   124                                                      
REMARK 465     ASP B   125                                                      
REMARK 465     ASP B   126                                                      
REMARK 465     ALA B   127                                                      
REMARK 465     GLU B   128                                                      
REMARK 465     SER B   129                                                      
REMARK 465     ARG B   130                                                      
REMARK 465     GLU B   266                                                      
REMARK 465     SER B   267                                                      
REMARK 465     PHE B   268                                                      
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 A  16    CG   CD   CE   NZ                                   
REMARK 470     LYS A  28    CG   CD   CE   NZ                                   
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 285    CG   CD   CE   NZ                                   
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 470     GLU A 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 334    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     ASN B 119    CG   OD1  ND2                                       
REMARK 470     GLU B 122    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 123    CA   C    O    CB   CG   CD   OE1                   
REMARK 470     GLU B 123    OE2                                                 
REMARK 470     ILE B 131    CG1  CG2  CD1                                       
REMARK 470     LYS B 148    CG   CD   CE   NZ                                   
REMARK 470     ASP B 149    CG   OD1  OD2                                       
REMARK 470     LYS B 154    CG   CD   CE   NZ                                   
REMARK 470     LYS B 174    CG   CD   CE   NZ                                   
REMARK 470     ILE B 192    CG1  CG2  CD1                                       
REMARK 470     LYS B 202    CG   CD   CE   NZ                                   
REMARK 470     CYS B 203    SG                                                  
REMARK 470     ASP B 204    CG   OD1  OD2                                       
REMARK 470     VAL B 206    CG1  CG2                                            
REMARK 470     LYS B 256    CG   CD   CE   NZ                                   
REMARK 470     TYR B 265    CA   C    O    CB   CG   CD1  CD2                   
REMARK 470     TYR B 265    CE1  CE2  CZ   OH                                   
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 A  41        3.77    -69.32                                   
REMARK 500    ASP A 166       45.12   -153.00                                   
REMARK 500    ASP A 184       79.28     59.70                                   
REMARK 500    LEU A 273       36.81    -88.87                                   
REMARK 500    TYR B 118      100.48   -162.49                                   
REMARK 500    GLU B 122       59.15   -112.49                                   
REMARK 500    ASN B 215       -4.51     64.52                                   
REMARK 500    MET B 264      -60.63     69.44                                   
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                              MN A 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 171   OD1                                                    
REMARK 620 2 ASP A 184   OD2  93.7                                              
REMARK 620 3 ANP A 450   O2G 119.5  85.5                                        
REMARK 620 4 ANP A 450   O2A 100.6  94.6 139.9                                  
REMARK 620 5 HOH A 500   O    86.5 177.7  92.4  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 184   OD1                                                    
REMARK 620 2 ASP A 184   OD2  55.9                                              
REMARK 620 3 ANP A 450   O2B  83.3  82.4                                        
REMARK 620 4 ANP A 450   O1G 150.1  95.2  85.1                                  
REMARK 620 5 HOH A 501   O    99.4 155.4  96.4 109.2                            
REMARK 620 6 HOH A 502   O    93.5  90.9 173.3  95.0  89.9                      
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 MN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 450                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3IDC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF (102-265)RIIB:C HOLOENZYME OF CAMP-DEPENDENT    
REMARK 900 PROTEIN KINASE                                                       
REMARK 900 RELATED ID: 1CX4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A DELETION MUTANT OF THE TYPE II BETA           
REMARK 900 REGULATORY SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE                  
REMARK 900 RELATED ID: 1RGS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A DELETION MUTANT OF THE TYPE I ALPHA           
REMARK 900 REGULATORY SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE                  
REMARK 900 RELATED ID: 2QCS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PKA RIA:C HOLOENZYME                            
REMARK 900 RELATED ID: 2QVS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PKA RIIA:C HOLOENZYME                           
DBREF  3IDB A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  3IDB B  108   268  UNP    P12369   KAP3_RAT       108    268             
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 LYS 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 PHE 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  161  THR ARG ARG ALA SER VAL CYS ALA GLU ALA TYR ASN PRO          
SEQRES   2 B  161  ASP GLU GLU GLU ASP ASP ALA GLU SER ARG ILE ILE HIS          
SEQRES   3 B  161  PRO LYS THR ASP ASP GLN ARG ASN ARG LEU GLN GLU ALA          
SEQRES   4 B  161  CYS LYS ASP ILE LEU LEU PHE LYS ASN LEU ASP PRO GLU          
SEQRES   5 B  161  GLN MET SER GLN VAL LEU ASP ALA MET PHE GLU LYS LEU          
SEQRES   6 B  161  VAL LYS GLU GLY GLU HIS VAL ILE ASP GLN GLY ASP ASP          
SEQRES   7 B  161  GLY ASP ASN PHE TYR VAL ILE ASP ARG GLY THR PHE ASP          
SEQRES   8 B  161  ILE TYR VAL LYS CYS ASP GLY VAL GLY ARG CYS VAL GLY          
SEQRES   9 B  161  ASN TYR ASP ASN ARG GLY SER PHE GLY GLU LEU ALA LEU          
SEQRES  10 B  161  MET TYR ASN THR PRO ARG ALA ALA THR ILE THR ALA THR          
SEQRES  11 B  161  SER PRO GLY ALA LEU TRP GLY LEU ASP ARG VAL THR PHE          
SEQRES  12 B  161  ARG ARG ILE ILE VAL LYS ASN ASN ALA LYS LYS ARG LYS          
SEQRES  13 B  161  MET TYR GLU SER PHE                                          
MODRES 3IDB TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 3IDB SEP A  338  SER  PHOSPHOSERINE                                      
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET     MN  A 401       1                                                       
HET     MN  A 402       1                                                       
HET    ANP  A 450      31                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  ANP    C10 H17 N6 O12 P3                                            
FORMUL   6  HOH   *398(H2 O)                                                    
HELIX    1   1 LYS A    8  GLN A   12  5                                   5    
HELIX    2   2 VAL A   15  GLU A   31  1                                  17    
HELIX    3   3 GLN A   39  ASP A   41  5                                   3    
HELIX    4   4 LYS A   76  LEU A   82  1                                   7    
HELIX    5   5 GLN A   84  VAL A   98  1                                  15    
HELIX    6   6 GLU A  127  GLY A  136  1                                  10    
HELIX    7   7 SER A  139  LEU A  160  1                                  22    
HELIX    8   8 LYS A  168  GLU A  170  5                                   3    
HELIX    9   9 THR A  201  LEU A  205  5                                   5    
HELIX   10  10 ALA A  206  LEU A  211  1                                   6    
HELIX   11  11 LYS A  217  GLY A  234  1                                  18    
HELIX   12  12 GLN A  242  GLY A  253  1                                  12    
HELIX   13  13 SER A  262  LEU A  273  1                                  12    
HELIX   14  14 VAL A  288  ASN A  293  1                                   6    
HELIX   15  15 HIS A  294  ALA A  298  5                                   5    
HELIX   16  16 ASP A  301  GLN A  307  1                                   7    
HELIX   17  17 GLY A  344  THR A  348  5                                   5    
HELIX   18  18 THR B  136  LYS B  148  1                                  13    
HELIX   19  19 ILE B  150  ASN B  155  1                                   6    
HELIX   20  20 ASP B  157  MET B  168  1                                  12    
HELIX   21  21 GLY B  220  MET B  225  5                                   6    
HELIX   22  22 ARG B  247  LYS B  260  1                                  14    
SHEET    1   A 5 PHE A  43  THR A  51  0                                        
SHEET    2   A 5 ARG A  56  HIS A  62 -1  O  LEU A  59   N  LYS A  47           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  MET A  71   N  MET A  58           
SHEET    4   A 5 ASN A 115  GLU A 121 -1  O  MET A 120   N  ALA A  70           
SHEET    5   A 5 LEU A 106  LYS A 111 -1  N  PHE A 108   O  VAL A 119           
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           
SHEET    1   D 2 CYS A 199  GLY A 200  0                                        
SHEET    2   D 2 VAL B 113  CYS B 114 -1  O  VAL B 113   N  GLY A 200           
SHEET    1   E 4 PHE B 169  VAL B 173  0                                        
SHEET    2   E 4 GLY B 240  ASP B 246 -1  O  LEU B 242   N  LYS B 171           
SHEET    3   E 4 ASN B 188  ARG B 194 -1  N  ASP B 193   O  ALA B 241           
SHEET    4   E 4 SER B 218  PHE B 219 -1  O  PHE B 219   N  TYR B 190           
SHEET    1   F 4 HIS B 178  ILE B 180  0                                        
SHEET    2   F 4 THR B 233  ALA B 236 -1  O  ILE B 234   N  VAL B 179           
SHEET    3   F 4 THR B 196  CYS B 203 -1  N  ASP B 198   O  THR B 235           
SHEET    4   F 4 VAL B 206  ASP B 214 -1  O  VAL B 210   N  ILE B 199           
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.33  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.32  
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  
LINK         OD1 ASN A 171                MN    MN A 401     1555   1555  2.05  
LINK         OD1 ASP A 184                MN    MN A 402     1555   1555  2.34  
LINK         OD2 ASP A 184                MN    MN A 402     1555   1555  2.37  
LINK         OD2 ASP A 184                MN    MN A 401     1555   1555  2.13  
LINK        MN    MN A 401                 O2G ANP A 450     1555   1555  2.19  
LINK        MN    MN A 401                 O2A ANP A 450     1555   1555  2.09  
LINK        MN    MN A 402                 O2B ANP A 450     1555   1555  2.12  
LINK        MN    MN A 402                 O1G ANP A 450     1555   1555  2.05  
LINK        MN    MN A 401                 O   HOH A 500     1555   1555  2.29  
LINK        MN    MN A 402                 O   HOH A 501     1555   1555  2.09  
LINK        MN    MN A 402                 O   HOH A 502     1555   1555  2.16  
SITE     1 AC1  4 ASN A 171  ASP A 184  ANP A 450  HOH A 500                    
SITE     1 AC2  4 ASP A 184  ANP A 450  HOH A 501  HOH A 502                    
SITE     1 AC3 30 LEU A  49  GLY A  52  VAL A  57  ALA A  70                    
SITE     2 AC3 30 LYS A  72  VAL A 104  MET A 120  GLU A 121                    
SITE     3 AC3 30 VAL A 123  GLU A 127  ASP A 166  LYS A 168                    
SITE     4 AC3 30 GLU A 170  ASN A 171  LEU A 173  THR A 183                    
SITE     5 AC3 30 ASP A 184  PHE A 327   MN A 401   MN A 402                    
SITE     6 AC3 30 HOH A 500  HOH A 506  HOH A 507  HOH A 509                    
SITE     7 AC3 30 HOH A 511  HOH A 574  ARG B 109  ALA B 111                    
SITE     8 AC3 30 SER B 112  HOH B 504                                          
CRYST1  173.321   65.733   47.155  90.00  99.95  90.00 C 1 2 1       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      0.005770  0.000000  0.001012        0.00000                         
SCALE2      0.000000  0.015213  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021531        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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