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Database: PDB
Entry: 4DG3
LinkDB: 4DG3
Original site: 4DG3 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       24-JAN-12   4DG3              
TITLE     CRYSTAL STRUCTURE OF R336A MUTANT OF CAMP-DEPENDENT PROTEIN KINASE    
TITLE    2 WITH UNPHOSPHORYLATED TURN MOTIF.                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: E;                                                            
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;             
COMPND  10 CHAIN: A;                                                            
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                                                      
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;                                               
SOURCE  13 OTHER_DETAILS: SYNTHESIZED                                           
KEYWDS    PROTEIN KINASE, PHOSPHOTRANSFERASE, SERINE/THREONINE PROTEIN KINASE,  
KEYWDS   2 REGULATORY SUBUNIT, PKI, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE    
KEYWDS   3 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.STEICHEN,J.YANG,S.S.TAYLOR                                        
REVDAT   1   13-FEB-13 4DG3    0                                                
JRNL        AUTH   J.M.STEICHEN,J.YANG,S.S.TAYLOR                               
JRNL        TITL   TURN MOTIF PHOSPHORYLATION REGULATES PROCESSING OF           
JRNL        TITL 2 CAMP-DEPENDENT PROTEIN KINASE                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 35158                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1862                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2565                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.03                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 113                          
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2889                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 249                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.56000                                             
REMARK   3    B22 (A**2) : 2.35000                                              
REMARK   3    B33 (A**2) : -1.79000                                             
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): 0.132         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.125         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.077         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.976         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2994 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4057 ; 1.135 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   354 ; 5.199 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   144 ;34.310 ;23.958       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   508 ;12.693 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;16.587 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   431 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2264 ; 0.004 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    14        E   126                          
REMARK   3    RESIDUE RANGE :   E   328        E   350                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.0753  15.5905  -5.7273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0433 T22:   0.1055                                     
REMARK   3      T33:   0.0553 T12:   0.0584                                     
REMARK   3      T13:  -0.0207 T23:  -0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4659 L22:   1.9968                                     
REMARK   3      L33:   3.8185 L12:  -0.5546                                     
REMARK   3      L13:  -0.9407 L23:  -0.0862                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0122 S12:   0.0666 S13:   0.1863                       
REMARK   3      S21:  -0.0242 S22:   0.0181 S23:   0.0539                       
REMARK   3      S31:  -0.3102 S32:  -0.3279 S33:  -0.0303                       
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 :   E   127        E   327                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.2759  -6.8346  -0.7348              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0920 T22:   0.0447                                     
REMARK   3      T33:   0.0512 T12:  -0.0477                                     
REMARK   3      T13:   0.0214 T23:  -0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7449 L22:   2.2166                                     
REMARK   3      L33:   3.3028 L12:  -0.3248                                     
REMARK   3      L13:   0.1908 L23:  -0.7746                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0308 S12:  -0.0312 S13:  -0.2568                       
REMARK   3      S21:  -0.1065 S22:  -0.0134 S23:   0.1440                       
REMARK   3      S31:   0.5326 S32:  -0.2365 S33:   0.0442                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4DG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070284.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-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   : 37095                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.340                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.47500                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-14% MPD, 100 MM TRIS, 10 MM DTT. 11-   
REMARK 280  13% METHANOL ADDED TO WELL BEFORE SEALING, PH 8.0, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277.15K                        
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       36.14500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.15500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.34500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.15500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.14500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.34500            
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: 3230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET E   -20                                                      
REMARK 465     GLY E   -19                                                      
REMARK 465     SER E   -18                                                      
REMARK 465     SER E   -17                                                      
REMARK 465     HIS E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     HIS E   -11                                                      
REMARK 465     SER E   -10                                                      
REMARK 465     SER E    -9                                                      
REMARK 465     GLY E    -8                                                      
REMARK 465     LEU E    -7                                                      
REMARK 465     VAL E    -6                                                      
REMARK 465     PRO E    -5                                                      
REMARK 465     ARG E    -4                                                      
REMARK 465     GLY E    -3                                                      
REMARK 465     SER E    -2                                                      
REMARK 465     HIS E    -1                                                      
REMARK 465     MET E     0                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     ASN E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     ALA E     6                                                      
REMARK 465     LYS E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     GLN E    12                                                      
REMARK 465     GLU E    13                                                      
REMARK 465     ASP A    24                                                      
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  16    CD   CE   NZ                                        
REMARK 470     GLU E  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  21    CE   NZ                                             
REMARK 470     LYS E  28    CG   CD   CE   NZ                                   
REMARK 470     ARG E 256    NE   CZ   NH1  NH2                                  
REMARK 470     LYS E 285    CG   CD   CE   NZ                                   
REMARK 470     LYS E 317    CE   NZ                                             
REMARK 470     PHE E 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS E 319    CG   CD   CE   NZ                                   
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   NH2  ARG E   308     O    HOH E   642              2.00            
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    ARG A  15   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A  15   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 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    PHE E  54       18.67   -160.78                                   
REMARK 500    ASP E 112     -164.59   -126.94                                   
REMARK 500    ASP E 166       42.87   -149.23                                   
REMARK 500    ASP E 184       77.98     61.62                                   
REMARK 500    ASN E 216     -159.76   -136.02                                   
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                              MG E 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP E 401   O3G                                                    
REMARK 620 2 ANP E 401   O1B  89.3                                              
REMARK 620 3 ASP E 184   OD2  96.3  91.0                                        
REMARK 620 4 ASP E 184   OD1 155.6  88.4  59.5                                  
REMARK 620 5 HOH E 701   O   107.4  91.3 156.3  97.0                            
REMARK 620 6 HOH E 694   O    91.4 178.0  87.1  90.2  90.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP E 401   O2A                                                    
REMARK 620 2 ASN E 171   OD1  99.0                                              
REMARK 620 3 ANP E 401   O2G 150.6 110.2                                        
REMARK 620 4 ASP E 184   OD2  92.3  94.7  89.1                                  
REMARK 620 5 HOH E 715   O    86.7  90.9  89.1 174.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 403                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC SUBUNIT OF CAMP-DEPENDENT             
REMARK 900 PROTEIN KINASE COMPLEXED WITH ATP AND IP20.                          
DBREF  4DG3 E    0   350  UNP    P05132   KAPCA_MOUSE      1    351             
DBREF  4DG3 A    5    24  UNP    P63248   IPKA_MOUSE       6     25             
SEQADV 4DG3 MET E  -20  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 GLY E  -19  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 SER E  -18  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 SER E  -17  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 HIS E  -16  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 HIS E  -15  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 HIS E  -14  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 HIS E  -13  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 HIS E  -12  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 HIS E  -11  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 SER E  -10  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 SER E   -9  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 GLY E   -8  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 LEU E   -7  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 VAL E   -6  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 PRO E   -5  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 ARG E   -4  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 GLY E   -3  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 SER E   -2  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 HIS E   -1  UNP  P05132              EXPRESSION TAG                 
SEQADV 4DG3 ALA E  336  UNP  P05132    ARG   337 ENGINEERED MUTATION            
SEQRES   1 E  371  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 E  371  LEU VAL PRO ARG GLY SER HIS MET GLY ASN ALA ALA ALA          
SEQRES   3 E  371  ALA LYS LYS GLY SER GLU GLN GLU SER VAL LYS GLU PHE          
SEQRES   4 E  371  LEU ALA LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU          
SEQRES   5 E  371  THR PRO SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP          
SEQRES   6 E  371  ARG ILE LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL          
SEQRES   7 E  371  MET LEU VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA          
SEQRES   8 E  371  MET LYS ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS          
SEQRES   9 E  371  GLN ILE GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN          
SEQRES  10 E  371  ALA VAL ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER          
SEQRES  11 E  371  PHE LYS ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR          
SEQRES  12 E  371  VAL ALA GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE          
SEQRES  13 E  371  GLY ARG PHE SEP GLU PRO HIS ALA ARG PHE TYR ALA ALA          
SEQRES  14 E  371  GLN ILE VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP          
SEQRES  15 E  371  LEU ILE TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE          
SEQRES  16 E  371  ASP GLN GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE          
SEQRES  17 E  371  ALA LYS ARG VAL LYS GLY ARG THR TRP TPO LEU CYS GLY          
SEQRES  18 E  371  THR PRO GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS          
SEQRES  19 E  371  GLY TYR ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL          
SEQRES  20 E  371  LEU ILE TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE          
SEQRES  21 E  371  ALA ASP GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER          
SEQRES  22 E  371  GLY LYS VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU          
SEQRES  23 E  371  LYS ASP LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR          
SEQRES  24 E  371  LYS ARG PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE          
SEQRES  25 E  371  LYS ASN HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA          
SEQRES  26 E  371  ILE TYR GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS          
SEQRES  27 E  371  PHE LYS GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR          
SEQRES  28 E  371  GLU GLU GLU GLU ILE ALA VAL SER ILE ASN GLU LYS CYS          
SEQRES  29 E  371  GLY LYS GLU PHE THR GLU PHE                                  
SEQRES   1 A   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 A   20  ARG ARG ASN ALA ILE HIS ASP                                  
MODRES 4DG3 SEP E  139  SER  PHOSPHOSERINE                                      
MODRES 4DG3 TPO E  197  THR  PHOSPHOTHREONINE                                   
HET    SEP  E 139      10                                                       
HET    TPO  E 197      11                                                       
HET    ANP  E 401      31                                                       
HET     MG  E 402       1                                                       
HET     MG  E 403       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  ANP    C10 H17 N6 O12 P3                                            
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  HOH   *249(H2 O)                                                    
HELIX    1   1 SER E   14  THR E   32  1                                  19    
HELIX    2   2 GLN E   39  ASP E   41  5                                   3    
HELIX    3   3 LYS E   76  LEU E   82  1                                   7    
HELIX    4   4 GLN E   84  GLN E   96  1                                  13    
HELIX    5   5 GLU E  127  GLY E  136  1                                  10    
HELIX    6   6 SEP E  139  LEU E  160  1                                  22    
HELIX    7   7 LYS E  168  GLU E  170  5                                   3    
HELIX    8   8 THR E  201  LEU E  205  5                                   5    
HELIX    9   9 ALA E  206  LEU E  211  1                                   6    
HELIX   10  10 LYS E  217  GLY E  234  1                                  18    
HELIX   11  11 GLN E  242  GLY E  253  1                                  12    
HELIX   12  12 SER E  262  LEU E  273  1                                  12    
HELIX   13  13 VAL E  288  ASN E  293  1                                   6    
HELIX   14  14 HIS E  294  ALA E  298  5                                   5    
HELIX   15  15 ASP E  301  GLN E  307  1                                   7    
HELIX   16  16 THR A    6  ALA A   12  1                                   7    
SHEET    1   A 5 PHE E  43  THR E  51  0                                        
SHEET    2   A 5 ARG E  56  HIS E  62 -1  O  LEU E  59   N  LYS E  47           
SHEET    3   A 5 HIS E  68  ASP E  75 -1  O  ILE E  73   N  ARG E  56           
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           
LINK         C   PHE E 138                 N   SEP E 139     1555   1555  1.34  
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         O3G ANP E 401                MG    MG E 403     1555   1555  1.98  
LINK         O2A ANP E 401                MG    MG E 402     1555   1555  1.99  
LINK         OD1 ASN E 171                MG    MG E 402     1555   1555  2.02  
LINK         O1B ANP E 401                MG    MG E 403     1555   1555  2.05  
LINK         O2G ANP E 401                MG    MG E 402     1555   1555  2.10  
LINK         OD2 ASP E 184                MG    MG E 402     1555   1555  2.13  
LINK         OD2 ASP E 184                MG    MG E 403     1555   1555  2.17  
LINK         OD1 ASP E 184                MG    MG E 403     1555   1555  2.24  
LINK        MG    MG E 403                 O   HOH E 701     1555   1555  1.97  
LINK        MG    MG E 402                 O   HOH E 715     1555   1555  2.10  
LINK        MG    MG E 403                 O   HOH E 694     1555   1555  2.12  
SITE     1 AC1 32 ARG A  18  ASN A  20  ALA A  21  HOH A 106                    
SITE     2 AC1 32 HOH A 108  GLY E  55  VAL E  57  ALA E  70                    
SITE     3 AC1 32 LYS E  72  VAL E 104  MET E 120  GLU E 121                    
SITE     4 AC1 32 TYR E 122  VAL E 123  GLU E 127  ASP E 166                    
SITE     5 AC1 32 LYS E 168  GLU E 170  ASN E 171  LEU E 173                    
SITE     6 AC1 32 THR E 183  ASP E 184  PHE E 327   MG E 402                    
SITE     7 AC1 32  MG E 403  HOH E 508  HOH E 509  HOH E 528                    
SITE     8 AC1 32 HOH E 605  HOH E 694  HOH E 701  HOH E 715                    
SITE     1 AC2  4 ASN E 171  ASP E 184  ANP E 401  HOH E 715                    
SITE     1 AC3  4 ASP E 184  ANP E 401  HOH E 694  HOH E 701                    
CRYST1   72.290   76.690   80.310  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      0.013833  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013040  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012452        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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