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Database: PDB
Entry: 4DG2
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Original site: 4DG2 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       24-JAN-12   4DG2              
TITLE     CRYSTAL STRUCTURE OF MYRISTOYLATED WT CATALYTIC SUBUNIT OF CAMP-      
TITLE    2 DEPENDENT PROTEIN KINASE IN COMPLEX WITH SP20                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: E;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 2-351;                                        
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 INHIBITOR ALPHA;             
COMPND  10 CHAIN: I;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 6-25;                                         
COMPND  12 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,         
COMPND  13 MUSCLE/BRAIN ISOFORM;                                                
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090                                                
KEYWDS    PROTEIN KINASE, MYRISTOYLATED, PHOSPHOTRANSFERASE OF SER/THR, MG,     
KEYWDS   2 PKI, PKA REGULATORY SUBUNITS, PHOSPHORYLATED ON S139, T197, S338,    
KEYWDS   3 MYRISTOYLATED ON G1, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.BASTIDAS,J.M.STEICHEN,S.S.TAYLOR                                  
REVDAT   3   02-JAN-13 4DG2    1       JRNL                                     
REVDAT   2   25-JUL-12 4DG2    1       REMARK                                   
REVDAT   1   06-JUN-12 4DG2    0                                                
JRNL        AUTH   A.C.BASTIDAS,M.S.DEAL,J.M.STEICHEN,M.M.KESHWANI,Y.GUO,       
JRNL        AUTH 2 S.S.TAYLOR                                                   
JRNL        TITL   ROLE OF N-TERMINAL MYRISTYLATION IN THE STRUCTURE AND        
JRNL        TITL 2 REGULATION OF CAMP-DEPENDENT PROTEIN KINASE.                 
JRNL        REF    J.MOL.BIOL.                   V. 422   215 2012              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   22617327                                                     
JRNL        DOI    10.1016/J.JMB.2012.05.021                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 81.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24598                          
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1310                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1760                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2140                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.2510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2987                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 308                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.39000                                              
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : -1.44000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.226         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.168         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.102         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.063         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3083 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4162 ; 0.866 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   372 ; 4.383 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   148 ;35.823 ;23.986       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   536 ;12.802 ;15.028       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;17.499 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   442 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2330 ; 0.003 ; 0.021       
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):  1844 ; 0.232 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2964 ; 0.446 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1239 ; 0.598 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1196 ; 1.022 ; 4.500       
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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     5        E   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5360   5.3970 -24.0760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0072 T22:   0.0084                                     
REMARK   3      T33:   0.0342 T12:  -0.0003                                     
REMARK   3      T13:   0.0120 T23:   0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6299 L22:   1.5369                                     
REMARK   3      L33:   2.6666 L12:   0.2652                                     
REMARK   3      L13:   0.0096 L23:   0.8567                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0307 S12:  -0.0459 S13:  -0.0042                       
REMARK   3      S21:   0.0719 S22:  -0.0488 S23:   0.0469                       
REMARK   3      S31:   0.0340 S32:   0.0127 S33:   0.0182                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     5        I    24                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.4900  -6.0210 -32.4200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0630 T22:   0.0488                                     
REMARK   3      T33:   0.0591 T12:   0.0217                                     
REMARK   3      T13:  -0.0090 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6749 L22:  10.4797                                     
REMARK   3      L33:  13.5178 L12:  -1.1096                                     
REMARK   3      L13:   0.8087 L23:   9.7888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1103 S12:  -0.2097 S13:   0.2035                       
REMARK   3      S21:  -0.2621 S22:   0.0949 S23:  -0.4301                       
REMARK   3      S31:  -0.5304 S32:   0.0336 S33:   0.0154                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   501        E   752                          
REMARK   3    RESIDUE RANGE :   I   101        I   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2010   5.3810 -23.9280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1263 T22:   0.1483                                     
REMARK   3      T33:   0.1596 T12:  -0.0032                                     
REMARK   3      T13:   0.0016 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3405 L22:   0.7034                                     
REMARK   3      L33:   1.2425 L12:   0.1191                                     
REMARK   3      L13:  -0.2437 L23:   0.5135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0314 S12:  -0.0454 S13:  -0.0063                       
REMARK   3      S21:   0.0369 S22:  -0.0353 S23:   0.0274                       
REMARK   3      S31:   0.0085 S32:  -0.0059 S33:   0.0038                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4DG2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070283.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : 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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25942                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.900                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MOTHER LIQUOR: 6% MPD      PROTEIN       
REMARK 280  SOLUTION: 50 MM BICINE, 150 MM AMMONIUM ACETATE, 10 MM DTT, 8-10    
REMARK 280  MG/ML 9% MEOH, 1:1 PROTEIN:MOTHER LIQUOR, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 277.15K, PH 8.0                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.24000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.94500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.81500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.94500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.24000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.81500            
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: 2610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS E   8    CG   CD   CE   NZ                                   
REMARK 470     GLU E  13    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  21    CD   CE   NZ                                        
REMARK 470     LYS E  83    CE   NZ                                             
REMARK 470     SEP E 139    P    O1P  O2P  O3P                                  
REMARK 470     ARG E 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 317    CG   CD   CE   NZ                                   
REMARK 470     PHE E 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU E 334    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP E 166       40.43   -147.04                                   
REMARK 500    ASP E 184       88.02     63.45                                   
REMARK 500    ASN E 216     -160.09   -128.26                                   
REMARK 500    LEU E 273       49.84    -88.77                                   
REMARK 500    LYS E 319       32.94    -99.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 534        DISTANCE =  5.02 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT         
REMARK 800  PROTEIN KINASE INHIBITOR ALPHA                                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DG0   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH AMP-PNP AND SP20.                       
REMARK 900 RELATED ID: 4DFX   RELATED DB: PDB                                   
REMARK 900 MYR-K7C CATALYTIC SUBUNIT OF PKA IN COMPLEX WITH SP20 AND            
REMARK 900 AMP-PNP.                                                             
REMARK 900 RELATED ID: 4DFZ   RELATED DB: PDB                                   
REMARK 900 MYR-K7C CATALYTIC SUBUNIT OF PKA IN COMPLEX WITH SP20.               
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 THE CATALYTIC SUBUNIT OF PKA IN COMPLEX WITH ATP AND IP20.           
REMARK 900 RELATED ID: 1CTP   RELATED DB: PDB                                   
REMARK 900 MYRISTOYLATED CATALYTIC SUBUNIT OF PKA BOUND TO IP20.                
REMARK 900 RELATED ID: 1JBP   RELATED DB: PDB                                   
REMARK 900 THE CATALYTIC SUBUNIT OF PKA IN COMPLEX WITH ADP AND SP20.           
DBREF  4DG2 E    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4DG2 I    5    24  UNP    P63248   IPKA_MOUSE       6     25             
SEQADV 4DG2 ALA I   20  UNP  P63248    ASN    21 ENGINEERED MUTATION            
SEQADV 4DG2 SER I   21  UNP  P63248    ALA    22 ENGINEERED MUTATION            
SEQRES   1 E  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 E  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 E  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 E  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 E  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 E  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 E  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 E  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 E  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 E  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 E  350  HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA          
SEQRES  12 E  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 E  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 E  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 E  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 E  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 E  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 E  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 E  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 E  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 E  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 E  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 E  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 E  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 E  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 E  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 E  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 I   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 I   20  ARG ARG ALA SER ILE HIS ASP                                  
MODRES 4DG2 SEP E  139  SER  PHOSPHOSERINE                                      
MODRES 4DG2 TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 4DG2 SEP E  338  SER  PHOSPHOSERINE                                      
HET    SEP  E 139       6                                                       
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET    MYR  E 401      15                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     MYR MYRISTIC ACID                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  MYR    C14 H28 O2                                                   
FORMUL   4  HOH   *308(H2 O)                                                    
HELIX    1   1 GLY E    1  LYS E    7  1                                   7    
HELIX    2   2 GLU E   11  THR E   32  1                                  22    
HELIX    3   3 GLN E   39  ASP E   41  5                                   3    
HELIX    4   4 LYS E   76  LEU E   82  1                                   7    
HELIX    5   5 GLN E   84  GLN E   96  1                                  13    
HELIX    6   6 GLU E  127  GLY E  136  1                                  10    
HELIX    7   7 SEP E  139  LEU E  160  1                                  22    
HELIX    8   8 LYS E  168  GLU E  170  5                                   3    
HELIX    9   9 THR E  201  LEU E  205  5                                   5    
HELIX   10  10 ALA E  206  LEU E  211  1                                   6    
HELIX   11  11 LYS E  217  GLY E  234  1                                  18    
HELIX   12  12 GLN E  242  SER E  252  1                                  11    
HELIX   13  13 SER E  262  LEU E  273  1                                  12    
HELIX   14  14 VAL E  288  ASN E  293  1                                   6    
HELIX   15  15 HIS E  294  ALA E  298  5                                   5    
HELIX   16  16 ASP E  301  GLN E  307  1                                   7    
HELIX   17  17 THR I    6  ALA I   12  1                                   7    
SHEET    1   A 5 PHE E  43  THR E  51  0                                        
SHEET    2   A 5 GLY E  55  HIS E  62 -1  O  LEU E  59   N  LYS E  47           
SHEET    3   A 5 HIS E  68  ASP E  75 -1  O  MET E  71   N  MET E  58           
SHEET    4   A 5 ASN E 115  GLU E 121 -1  O  MET E 118   N  LYS E  72           
SHEET    5   A 5 LEU E 106  LYS E 111 -1  N  PHE E 108   O  VAL E 119           
SHEET    1   B 2 LEU E 162  ILE E 163  0                                        
SHEET    2   B 2 LYS E 189  ARG E 190 -1  O  LYS E 189   N  ILE E 163           
SHEET    1   C 2 LEU E 172  ILE E 174  0                                        
SHEET    2   C 2 ILE E 180  VAL E 182 -1  O  GLN E 181   N  LEU E 173           
SHEET    1   D 2 CYS E 199  GLY E 200  0                                        
SHEET    2   D 2 ILE I  22  HIS I  23 -1  O  ILE I  22   N  GLY E 200           
LINK         C   PHE E 138                 N   SEP E 139     1555   1555  1.33  
LINK         C   SEP E 139                 N   GLU E 140     1555   1555  1.33  
LINK         C   TRP E 196                 N   TPO E 197     1555   1555  1.33  
LINK         C   TPO E 197                 N   LEU E 198     1555   1555  1.33  
LINK         C   VAL E 337                 N   SEP E 338     1555   1555  1.33  
LINK         C   SEP E 338                 N   ILE E 339     1555   1555  1.33  
LINK         N   GLY E   1                 C1  MYR E 401     1555   1555  1.50  
SITE     1 AC1  7 GLY E   1  ASN E   2  ALA E   3  ALA E   4                    
SITE     2 AC1  7 SER E  14  LEU E 152  ASP I  24                               
SITE     1 AC2 61 GLY E   1  ASN E   2  ALA E   3  GLN E  84                    
SITE     2 AC2 61 GLU E  86  ARG E  93  GLU E 127  PHE E 129                    
SITE     3 AC2 61 SER E 130  ARG E 133  ASP E 166  LYS E 168                    
SITE     4 AC2 61 PRO E 169  GLU E 170  PHE E 187  LYS E 189                    
SITE     5 AC2 61 ARG E 190  VAL E 191  LYS E 192  LEU E 198                    
SITE     6 AC2 61 CYS E 199  GLY E 200  PRO E 202  GLU E 203                    
SITE     7 AC2 61 GLU E 230  GLY E 234  TYR E 235  PRO E 236                    
SITE     8 AC2 61 PHE E 239  ASP E 241  ASP E 328  TYR E 330                    
SITE     9 AC2 61 GLU E 349  MYR E 401  HOH E 507  HOH E 543                    
SITE    10 AC2 61 HOH E 544  HOH E 665  HOH E 679  HOH E 680                    
SITE    11 AC2 61 HOH E 731  HOH I 103  HOH I 104  HOH I 106                    
SITE    12 AC2 61 HOH I 108  HOH I 110  HOH I 111  HOH I 112                    
SITE    13 AC2 61 HOH I 113  HOH I 114  HOH I 115  HOH I 117                    
SITE    14 AC2 61 HOH I 119  HOH I 120  HOH I 121  HOH I 122                    
SITE    15 AC2 61 HOH I 125  HOH I 126  HOH I 127  HOH I 130                    
SITE    16 AC2 61 HOH I 131                                                     
CRYST1   48.480   79.630  117.890  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020627  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012558  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008482        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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