GenomeNet

Database: PDB
Entry: 3PVB
LinkDB: 3PVB
Original site: 3PVB 
HEADER    TRANSFERASE                             06-DEC-10   3PVB              
TITLE     CRYSTAL STRUCTURE OF (73-244)RIA: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: UNP RESIDUES 7-351;                                        
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 I-ALPHA REGULATORY      
COMPND  10 SUBUNIT;                                                             
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 85-244;                                       
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  10 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;            
SOURCE  11 ORGANISM_TAXID: 9913;                                                
SOURCE  12 GENE: PRKAR1A;                                                       
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PRSET                                 
KEYWDS    KINASE, RIA HOLOENZYME, TETRAMERIC PROTEIN KINASE A, TRANSFERASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.BOETTCHER,J.WU,C.KIM,J.YANG,J.BRUYSTENS,N.CHEUNG,J.K.PENNYPACKER, 
AUTHOR   2 D.A.BLUMENTHAL,A.P.KORNEV,S.S.TAYLOR                                 
REVDAT   2   19-JUN-13 3PVB    1       JRNL   VERSN                             
REVDAT   1   02-FEB-11 3PVB    0                                                
JRNL        AUTH   A.J.BOETTCHER,J.WU,C.KIM,J.YANG,J.BRUYSTENS,N.CHEUNG,        
JRNL        AUTH 2 J.K.PENNYPACKER,D.A.BLUMENTHAL,A.P.KORNEV,S.S.TAYLOR         
JRNL        TITL   CRYSTAL STRUCTURE OF (73-244)RIA:C HOLOENZYME OF             
JRNL        TITL 2 CAMP-DEPENDENT PROTEIN KINASE                                
JRNL        REF    STRUCTURE                     V.  19   265 2011              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   21300294                                                     
JRNL        DOI    10.1016/J.STR.2010.12.005                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 27860                          
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) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3992                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 15                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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 3PVB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062855.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27860                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2QCS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE RIA(73-244):C COMPLEX WAS            
REMARK 280  CRYSTALLIZED IN 0.1M MES PH 6.0 AND 12% PEG 20,000 BY USING A       
REMARK 280  DOUGLAS INSTRUMENTS ORYX8 CRYSTALLOGRAPHY ROBOT AS 1:1 PROTEIN      
REMARK 280  SOLUTION:CRYSTALLIZING SOLUTION, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 298.0 K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.40200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       46.70100            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       46.70100            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       93.40200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: ONE MOLECULE PER ASYMMETRICAL UNIT                           
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   7    CG   CD   CE   NZ                                   
REMARK 470     LYS A   8    CG   CD   CE   NZ                                   
REMARK 470     GLU A  11    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  12    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  16    CG   CD   CE   NZ                                   
REMARK 470     ARG A  56    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  76    CG   CD   CE   NZ                                   
REMARK 470     LYS A  81    CG   CD   CE   NZ                                   
REMARK 470     LYS A 105    CG   CD   CE   NZ                                   
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     SER A 263    OG                                                  
REMARK 470     ARG A 270    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 295    CG   CD   CE   NZ                                   
REMARK 470     LYS A 309    CG   CD   CE   NZ                                   
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 470     GLU A 334    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     ASN B  86    CG   OD1  ND2                                       
REMARK 470     LYS B  90    CG   CD   CE   NZ                                   
REMARK 470     GLU B 106    CG   CD   OE1  OE2                                  
REMARK 470     SER B 110    OG                                                  
REMARK 470     LYS B 121    CG   CD   CE   NZ                                   
REMARK 470     LYS B 128    CG   CD   CE   NZ                                   
REMARK 470     LYS B 132    CG   CD   CE   NZ                                   
REMARK 470     LYS B 240    CG   CD   CE   NZ                                   
REMARK 470     ARG B 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 242    CG   CD   CE   NZ                                   
REMARK 470     MET B 243    CG   SD   CE                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    PHE A   185     N    PHE A   187              2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A  98   CB  -  CA  -  C   ANGL. DEV. = -18.7 DEGREES          
REMARK 500    ALA A 233   CB  -  CA  -  C   ANGL. DEV. =  11.8 DEGREES          
REMARK 500    PRO B 117   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ALA B 215   N   -  CA  -  CB  ANGL. DEV. = -12.0 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    LYS A   7       -5.01    169.82                                   
REMARK 500    LYS A   8      -88.80     -5.30                                   
REMARK 500    PRO A  33      159.17    -44.52                                   
REMARK 500    ASN A  36       83.99     53.13                                   
REMARK 500    ALA A  38     -145.86   -167.71                                   
REMARK 500    PHE A  54      -37.06   -137.76                                   
REMARK 500    LEU A  59       54.56   -116.37                                   
REMARK 500    PHE A 102       56.98    -91.09                                   
REMARK 500    ARG A 165      -18.82     62.24                                   
REMARK 500    ASP A 184       82.89     63.11                                   
REMARK 500    PRO A 202      -60.33    -13.41                                   
REMARK 500    PRO A 207      -60.51    -27.54                                   
REMARK 500    ALA A 233      -55.45   -145.34                                   
REMARK 500    PRO A 243      -70.46    -40.32                                   
REMARK 500    PRO A 258     -158.93    -74.85                                   
REMARK 500    LYS A 279       32.72   -144.13                                   
REMARK 500    ASN A 283       11.15   -144.18                                   
REMARK 500    LEU A 284     -145.75    -80.26                                   
REMARK 500    ALA A 298      -54.40     -6.85                                   
REMARK 500    PHE A 314       89.02   -163.11                                   
REMARK 500    THR A 324       35.22    -76.45                                   
REMARK 500    CYS A 343      114.63     60.33                                   
REMARK 500    THR A 348      -56.58    -27.40                                   
REMARK 500    ASN B  86       62.42    166.73                                   
REMARK 500    PRO B  87       32.52   -147.74                                   
REMARK 500    VAL B  88       93.14     75.65                                   
REMARK 500    PRO B 117      131.85     -8.57                                   
REMARK 500    GLN B 165      150.47    -44.25                                   
REMARK 500    ASP B 170      -58.19    151.81                                   
REMARK 500    TRP B 188      105.62    -43.05                                   
REMARK 500    SER B 197      151.21    178.44                                   
REMARK 500    GLU B 200       21.28    -57.32                                   
REMARK 500    TYR B 205        2.09   -165.85                                   
REMARK 500    ALA B 211      154.00    178.19                                   
REMARK 500    LYS B 216      -65.71    -17.15                                   
REMARK 500    THR B 217     -168.27   -116.16                                   
REMARK 500    LYS B 240       70.14   -112.72                                   
REMARK 500    LYS B 242      121.51   -178.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER A 212        25.0      L          L   OUTSIDE RANGE           
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 ANP A 400   N3B 138.5                                              
REMARK 620 3 ANP A 400   O2A  89.3  73.7                                        
REMARK 620 4 ANP A 400   O2G 122.3  67.2 140.8                                  
REMARK 620 N                    1     2     3                                   
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 ANP A 400   O1G                                                    
REMARK 620 2 ASP A 184   OD1 125.9                                              
REMARK 620 3 ASP A 184   OD2  94.3  52.5                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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                            
DBREF  3PVB A    6   350  UNP    P05132   KAPCA_MOUSE      7    351             
DBREF  3PVB B   84   243  UNP    P00514   KAP0_BOVIN      85    244             
SEQRES   1 A  345  ALA LYS LYS GLY SEP GLU GLN GLU SER VAL LYS GLU PHE          
SEQRES   2 A  345  LEU ALA LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU          
SEQRES   3 A  345  THR PRO SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP          
SEQRES   4 A  345  ARG ILE LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL          
SEQRES   5 A  345  MET LEU VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA          
SEQRES   6 A  345  MET LYS ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS          
SEQRES   7 A  345  GLN ILE GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN          
SEQRES   8 A  345  ALA VAL ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER          
SEQRES   9 A  345  PHE LYS ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR          
SEQRES  10 A  345  VAL ALA GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE          
SEQRES  11 A  345  GLY ARG PHE SEP GLU PRO HIS ALA ARG PHE TYR ALA ALA          
SEQRES  12 A  345  GLN ILE VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP          
SEQRES  13 A  345  LEU ILE TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE          
SEQRES  14 A  345  ASP GLN GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE          
SEQRES  15 A  345  ALA LYS ARG VAL LYS GLY ARG THR TRP TPO LEU CYS GLY          
SEQRES  16 A  345  THR PRO GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS          
SEQRES  17 A  345  GLY TYR ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL          
SEQRES  18 A  345  LEU ILE TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE          
SEQRES  19 A  345  ALA ASP GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER          
SEQRES  20 A  345  GLY LYS VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU          
SEQRES  21 A  345  LYS ASP LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR          
SEQRES  22 A  345  LYS ARG PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE          
SEQRES  23 A  345  LYS ASN HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA          
SEQRES  24 A  345  ILE TYR GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS          
SEQRES  25 A  345  PHE LYS GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR          
SEQRES  26 A  345  GLU GLU GLU GLU ILE ARG VAL SEP ILE ASN GLU LYS CYS          
SEQRES  27 A  345  GLY LYS GLU PHE THR GLU PHE                                  
SEQRES   1 B  160  PRO PRO ASN PRO VAL VAL LYS GLY ARG ARG ARG ARG GLY          
SEQRES   2 B  160  ALA ILE SER ALA GLU VAL TYR THR GLU GLU ASP ALA ALA          
SEQRES   3 B  160  SER TYR VAL ARG LYS VAL ILE PRO LYS ASP TYR LYS THR          
SEQRES   4 B  160  MET ALA ALA LEU ALA LYS ALA ILE GLU LYS ASN VAL LEU          
SEQRES   5 B  160  PHE SER HIS LEU ASP ASP ASN GLU ARG SER ASP ILE PHE          
SEQRES   6 B  160  ASP ALA MET PHE PRO VAL SER PHE ILE ALA GLY GLU THR          
SEQRES   7 B  160  VAL ILE GLN GLN GLY ASP GLU GLY ASP ASN PHE TYR VAL          
SEQRES   8 B  160  ILE ASP GLN GLY GLU MET ASP VAL TYR VAL ASN ASN GLU          
SEQRES   9 B  160  TRP ALA THR SER VAL GLY GLU GLY GLY SER PHE GLY GLU          
SEQRES  10 B  160  LEU ALA LEU ILE TYR GLY THR PRO ARG ALA ALA THR VAL          
SEQRES  11 B  160  LYS ALA LYS THR ASN VAL LYS LEU TRP GLY ILE ASP ARG          
SEQRES  12 B  160  ASP SER TYR ARG ARG ILE LEU MET GLY SER THR LEU ARG          
SEQRES  13 B  160  LYS ARG LYS MET                                              
MODRES 3PVB SEP A   10  SER  PHOSPHOSERINE                                      
MODRES 3PVB SEP A  139  SER  PHOSPHOSERINE                                      
MODRES 3PVB TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 3PVB SEP A  338  SER  PHOSPHOSERINE                                      
HET    SEP  A  10      10                                                       
HET    SEP  A 139      10                                                       
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    ANP  A 400      31                                                       
HET     MN  A 401       1                                                       
HET     MN  A 402       1                                                       
HET    GOL  B   1       6                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     GOL GLYCEROL                                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  SEP    3(C3 H8 N O6 P)                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  ANP    C10 H17 N6 O12 P3                                            
FORMUL   4   MN    2(MN 2+)                                                     
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7  HOH   *15(H2 O)                                                     
HELIX    1   1 SEP A   10  GLU A   31  1                                  22    
HELIX    2   2 LYS A   76  LEU A   82  1                                   7    
HELIX    3   3 GLN A   84  VAL A   98  1                                  15    
HELIX    4   4 PHE A  129  ARG A  134  1                                   6    
HELIX    5   5 SEP A  139  SER A  159  1                                  21    
HELIX    6   6 LYS A  168  LEU A  172  5                                   5    
HELIX    7   7 THR A  201  LEU A  205  5                                   5    
HELIX    8   8 ALA A  206  SER A  212  1                                   7    
HELIX    9   9 LYS A  217  ALA A  232  1                                  16    
HELIX   10  10 GLN A  242  GLY A  253  1                                  12    
HELIX   11  11 SER A  262  LEU A  273  1                                  12    
HELIX   12  12 ASP A  276  ARG A  280  5                                   5    
HELIX   13  13 VAL A  288  ASN A  293  1                                   6    
HELIX   14  14 HIS A  294  ALA A  298  5                                   5    
HELIX   15  15 ASP A  301  ARG A  308  1                                   8    
HELIX   16  16 THR B  104  ALA B  109  1                                   6    
HELIX   17  17 ASP B  119  ILE B  130  1                                  12    
HELIX   18  18 ASP B  140  SER B  145  1                                   6    
HELIX   19  19 SER B  145  MET B  151  1                                   7    
HELIX   20  20 LEU B  201  GLY B  206  1                                   6    
HELIX   21  21 ARG B  226  ARG B  239  1                                  14    
SHEET    1   A 2 PHE A  43  ASP A  44  0                                        
SHEET    2   A 2 LYS A  61  HIS A  62 -1  O  LYS A  61   N  ASP A  44           
SHEET    1   B 5 THR A  48  THR A  51  0                                        
SHEET    2   B 5 ARG A  56  MET A  58 -1  O  VAL A  57   N  LEU A  49           
SHEET    3   B 5 TYR A  69  ASP A  75 -1  O  ILE A  73   N  ARG A  56           
SHEET    4   B 5 ASN A 115  GLU A 121 -1  O  MET A 120   N  ALA A  70           
SHEET    5   B 5 LEU A 106  LYS A 111 -1  N  PHE A 110   O  TYR A 117           
SHEET    1   C 2 CYS A 199  GLY A 200  0                                        
SHEET    2   C 2 ILE B  98  SER B  99 -1  O  ILE B  98   N  GLY A 200           
SHEET    1   D 4 PHE B 152  PHE B 156  0                                        
SHEET    2   D 4 VAL B 219  ASP B 225 -1  O  GLY B 223   N  PHE B 152           
SHEET    3   D 4 ASN B 171  GLY B 178 -1  N  PHE B 172   O  ILE B 224           
SHEET    4   D 4 SER B 197  PHE B 198 -1  O  PHE B 198   N  TYR B 173           
SHEET    1   E 3 TRP B 188  VAL B 192  0                                        
SHEET    2   E 3 MET B 180  TYR B 183 -1  N  VAL B 182   O  THR B 190           
SHEET    3   E 3 THR B 212  LYS B 214 -1  O  THR B 212   N  TYR B 183           
LINK         C   GLY A   9                 N   SEP A  10     1555   1555  1.33  
LINK         C   SEP A  10                 N   GLU A  11     1555   1555  1.33  
LINK         C   PHE A 138                 N   SEP A 139     1555   1555  1.32  
LINK         C   SEP A 139                 N   GLU A 140     1555   1555  1.33  
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.34  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.33  
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.33  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
LINK         OD1 ASN A 171                MN    MN A 401     1555   1555  1.77  
LINK         O1G ANP A 400                MN    MN A 402     1555   1555  2.02  
LINK         N3B ANP A 400                MN    MN A 401     1555   1555  2.04  
LINK         O2A ANP A 400                MN    MN A 401     1555   1555  2.20  
LINK         OD1 ASP A 184                MN    MN A 402     1555   1555  2.22  
LINK         O2G ANP A 400                MN    MN A 401     1555   1555  2.49  
LINK         OD2 ASP A 184                MN    MN A 402     1555   1555  2.61  
SITE     1 AC1 23 GLY A  50  GLY A  52  SER A  53  PHE A  54                    
SITE     2 AC1 23 GLY A  55  VAL A  57  ALA A  70  LYS A  72                    
SITE     3 AC1 23 MET A 120  GLU A 121  VAL A 123  GLU A 127                    
SITE     4 AC1 23 LYS A 168  GLU A 170  ASN A 171  LEU A 173                    
SITE     5 AC1 23 THR A 183  ASP A 184  PHE A 327   MN A 401                    
SITE     6 AC1 23  MN A 402  ARG B  94  ALA B  97                               
SITE     1 AC2  3 ASN A 171  ASP A 184  ANP A 400                               
SITE     1 AC3  3 ASP A 166  ASP A 184  ANP A 400                               
SITE     1 AC4  5 GLU B 200  PRO B 208  ARG B 209  ALA B 210                    
SITE     2 AC4  5 ALA B 211                                                     
CRYST1  116.667  116.667  140.103  90.00  90.00 120.00 P 32 2 1      6          
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      0.008571  0.004949  0.000000        0.00000                         
SCALE2      0.000000  0.009897  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007138        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system