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Database: PDB
Entry: 4DFZ
LinkDB: 4DFZ
Original site: 4DFZ 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       24-JAN-12   4DFZ              
TITLE     CRYSTAL STRUCTURE OF MYRISTOYLATED K7C 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 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;             
COMPND  11 CHAIN: I;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 6-25;                                         
COMPND  13 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,         
COMPND  14 MUSCLE/BRAIN ISOFORM;                                                
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 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   2   02-JAN-13 4DFZ    1       JRNL                                     
REVDAT   1   06-JUN-12 4DFZ    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) : 37.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 28927                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1529                            
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) : 2042                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 114                          
REMARK   3   BIN FREE R VALUE                    : 0.2730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2984                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 281                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.00000                                              
REMARK   3    B22 (A**2) : 0.12000                                              
REMARK   3    B33 (A**2) : -1.13000                                             
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): 0.194         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.163         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.113         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.116         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3098 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4183 ; 0.887 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   376 ; 4.439 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   147 ;35.734 ;23.878       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   535 ;13.042 ;15.028       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;16.846 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   443 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2345 ; 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):  1858 ; 0.222 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2987 ; 0.431 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1240 ; 0.630 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1194 ; 1.076 ; 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     4        E   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.4749  -5.3260 -24.0440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0061 T22:   0.0085                                     
REMARK   3      T33:   0.0407 T12:  -0.0037                                     
REMARK   3      T13:  -0.0075 T23:  -0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6912 L22:   1.2231                                     
REMARK   3      L33:   2.1095 L12:   0.2097                                     
REMARK   3      L13:  -0.0048 L23:  -0.6980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0378 S12:  -0.0675 S13:   0.0259                       
REMARK   3      S21:   0.0676 S22:  -0.0459 S23:  -0.0345                       
REMARK   3      S31:  -0.0405 S32:  -0.0018 S33:   0.0081                       
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):  -3.3961   6.3757 -32.2543              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0314 T22:   0.0277                                     
REMARK   3      T33:   0.0436 T12:   0.0055                                     
REMARK   3      T13:   0.0063 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2151 L22:  10.5663                                     
REMARK   3      L33:   8.4412 L12:  -0.7392                                     
REMARK   3      L13:  -0.4204 L23:  -7.4471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1443 S12:  -0.1140 S13:  -0.1150                       
REMARK   3      S21:   0.0822 S22:   0.1946 S23:   0.2769                       
REMARK   3      S31:   0.2056 S32:  -0.2358 S33:  -0.0503                       
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   734                          
REMARK   3    RESIDUE RANGE :   I   101        I   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2865  -5.4944 -23.7954              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0817 T22:   0.0810                                     
REMARK   3      T33:   0.1429 T12:  -0.0009                                     
REMARK   3      T13:  -0.0047 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4372 L22:   0.6762                                     
REMARK   3      L33:   1.4307 L12:   0.0545                                     
REMARK   3      L13:   0.1323 L23:  -0.5135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0475 S12:  -0.0494 S13:  -0.0035                       
REMARK   3      S21:   0.0480 S22:  -0.0325 S23:   0.0003                       
REMARK   3      S31:  -0.0632 S32:  -0.0185 S33:  -0.0150                       
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 4DFZ 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 RCSB070280.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-MAY-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   : 30558                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.460                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11700                            
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     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.54500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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   (%): 53.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MOTHER LIQUOR: 6% MPD    PROTEIN: 50     
REMARK 280  MM BICINE, 150 MM AMMONIUM ACETATE, 10 MM DTT, 8-10 MG/ML           
REMARK 280  PROTEIN, 9% MEOH ADDED TO WELL IMMEDIATELY BEFORE SEALING, VAPOR    
REMARK 280  DIFFUSION, 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       24.23000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.03000            
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       59.03000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.23000            
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: 2640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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     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    NE   CZ   NH1  NH2                                  
REMARK 470     LYS E 295    CE   NZ                                             
REMARK 470     LYS E 317    CG   CD   CE   NZ                                   
REMARK 470     GLU E 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 333    CD   OE1  OE2                                       
REMARK 470     GLU E 334    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 345    CD   CE   NZ                                        
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   N    GLY E     1     C2   MYR E   401              1.98            
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    ASP E 166       40.77   -147.80                                   
REMARK 500    ASP E 184       88.27     63.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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: 4DFX   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH SP20 AND AMP-PNP                        
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 CATALYTIC SUBUNIT IN COMPLEX WITH IP20 AND ATP                       
REMARK 900 RELATED ID: 1CTP   RELATED DB: PDB                                   
REMARK 900 MYRISTOYLATED CATALYTIC SUBUNIT IN COMPLEX WITH IP20                 
REMARK 900 RELATED ID: 1JBP   RELATED DB: PDB                                   
REMARK 900 CATALYTIC SUBUNIT IN COMPLEX WITH SP20 AND ADP                       
REMARK 900 RELATED ID: 4DG2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DG0   RELATED DB: PDB                                   
DBREF  4DFZ E    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4DFZ I    5    24  UNP    P63248   IPKA_MOUSE       6     25             
SEQADV 4DFZ CYS E    7  UNP  P05132    LYS     8 ENGINEERED MUTATION            
SEQADV 4DFZ ALA I   20  UNP  P63248    ASN    21 ENGINEERED MUTATION            
SEQADV 4DFZ SER I   21  UNP  P63248    ALA    22 ENGINEERED MUTATION            
SEQRES   1 E  350  GLY ASN ALA ALA ALA ALA CYS 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 4DFZ SEP E  139  SER  PHOSPHOSERINE                                      
MODRES 4DFZ TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 4DFZ 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   *281(H2 O)                                                    
HELIX    1   1 GLY E    1  CYS 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  GLY E  253  1                                  12    
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 120   N  ALA E  70           
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  1.41  
SITE     1 AC1  8 GLY E   1  ASN E   2  ALA E   3  ALA E   4                    
SITE     2 AC1  8 SER E  14  LEU E 152  GLU E 155  ASP I  24                    
SITE     1 AC2 60 ASN E   2  ALA E   3  GLN E  84  GLU E  86                    
SITE     2 AC2 60 ARG E  93  GLU E 127  PHE E 129  SER E 130                    
SITE     3 AC2 60 ARG E 133  ASP E 166  LYS E 168  PRO E 169                    
SITE     4 AC2 60 GLU E 170  PHE E 187  LYS E 189  ARG E 190                    
SITE     5 AC2 60 VAL E 191  LYS E 192  LEU E 198  CYS E 199                    
SITE     6 AC2 60 GLY E 200  GLU E 203  GLU E 230  TYR E 235                    
SITE     7 AC2 60 PRO E 236  PHE E 239  ALA E 240  ASP E 241                    
SITE     8 AC2 60 PRO E 243  TYR E 247  ASP E 328  TYR E 330                    
SITE     9 AC2 60 GLU E 349  MYR E 401  HOH E 507  HOH E 537                    
SITE    10 AC2 60 HOH E 666  HOH E 667  HOH E 711  HOH I 101                    
SITE    11 AC2 60 HOH I 103  HOH I 104  HOH I 105  HOH I 106                    
SITE    12 AC2 60 HOH I 107  HOH I 108  HOH I 110  HOH I 111                    
SITE    13 AC2 60 HOH I 112  HOH I 113  HOH I 114  HOH I 115                    
SITE    14 AC2 60 HOH I 116  HOH I 117  HOH I 118  HOH I 122                    
SITE    15 AC2 60 HOH I 123  HOH I 125  HOH I 126  HOH I 127                    
CRYST1   48.460   79.630  118.060  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      0.020636  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012558  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008470        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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