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Database: PDB
Entry: 1JBP
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HEADER    TRANSFERASE                             06-JUN-01   1JBP              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN  
TITLE    2 KINASE COMPLEXED WITH A SUBSTRATE PEPTIDE, ADP AND DETERGENT         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT;    
COMPND   3 CHAIN: E;                                                            
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.1.37;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, MUSCLE/BRAIN FORM;
COMPND   9 CHAIN: S;                                                            
COMPND  10 FRAGMENT: RESIDUES 5-24;                                             
COMPND  11 SYNONYM: PKI-ALPHA;                                                  
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE  
SOURCE  10 OF THE PEPTIDE IS NATURALLY FOUND IN MUS MUSCULUS (MOUSE).           
KEYWDS    PROTEIN-SUBSTRATE COMPLEX, TRANSFERASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    MADHUSUDAN,E.A.TRAFNY,N.H.XUONG,J.A.ADAMS,L.F.TEN EYCK,S.S.TAYLOR,    
AUTHOR   2 J.M.SOWADSKI                                                         
REVDAT   4   04-OCT-17 1JBP    1       REMARK                                   
REVDAT   3   24-FEB-09 1JBP    1       VERSN                                    
REVDAT   2   01-APR-03 1JBP    1       JRNL                                     
REVDAT   1   27-JUN-01 1JBP    0                                                
JRNL        AUTH   MADHUSUDAN,E.A.TRAFNY,N.H.XUONG,J.A.ADAMS,L.F.TEN EYCK,      
JRNL        AUTH 2 S.S.TAYLOR,J.M.SOWADSKI                                      
JRNL        TITL   CAMP-DEPENDENT PROTEIN KINASE: CRYSTALLOGRAPHIC INSIGHTS     
JRNL        TITL 2 INTO SUBSTRATE RECOGNITION AND PHOSPHOTRANSFER.              
JRNL        REF    PROTEIN SCI.                  V.   3   176 1994              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   8003955                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN EYCK,N.XUONG,          
REMARK   1  AUTH 2 S.S.TAYLOR,J.M.SOWADSKI                                      
REMARK   1  TITL   2.0 A REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF  
REMARK   1  TITL 2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE       
REMARK   1  TITL 3 INHIBITOR AND DETERGENT                                      
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  49   357 1993              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444993000502                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.ZHENG,E.A.TRAFNY,D.R.KNIGHTON,N.XUONG,S.S.TAYLOR,          
REMARK   1  AUTH 2 L.F.TEN EYCK,J.M.SOWADSKI                                    
REMARK   1  TITL   2.2 A REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF  
REMARK   1  TITL 2 CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH MNATP AND A     
REMARK   1  TITL 3 PEPTIDE INHIBITOR                                            
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  49   362 1993              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444993000423                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 21349                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2866                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 168                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.019 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.463 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JBP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000013594.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-92                          
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : XUONG-HAMLIN MULTIWIRE             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : UCSD-SYSTEM                        
REMARK 200  DATA SCALING SOFTWARE          : UCSD-SYSTEM                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21349                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05500                            
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) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ATP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION,HANGING DROP,PH          
REMARK 280  8.0,277K, 10MM DITHIOTHREITOL, 8% DOW POLYETHYLENE GLYCOL 400,      
REMARK 280  METHANOL, BICINE, VAPOR DIFFUSION, HANGING DROP                     
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       36.98000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.50000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.05500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.50000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.98000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.05500            
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: 3330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, S                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY 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 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  11    CG   CD   OE1  OE2                                  
REMARK 470     SER E  14    OG                                                  
REMARK 470     LYS E  16    CG   CD   CE   NZ                                   
REMARK 470     GLU E  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  21    CG   CD   CE   NZ                                   
REMARK 470     GLU E  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  28    CG   CD   CE   NZ                                   
REMARK 470     GLU E  31    CG   CD   OE1  OE2                                  
REMARK 470     ARG E  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER E  53    OG                                                  
REMARK 470     GLU E  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  83    CG   CD   CE   NZ                                   
REMARK 470     GLU E 242    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E 270    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP E 276    CG   OD1  OD2                                       
REMARK 470     LYS E 279    CG   CD   CE   NZ                                   
REMARK 470     GLU E 311    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 317    CG   CD   CE   NZ                                   
REMARK 470     PHE E 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS E 319    CG   CD   CE   NZ                                   
REMARK 470     GLU E 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 334    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E 339    CG1  CG2  CD1                                       
REMARK 470     ASN E 340    CG   OD1  ND2                                       
REMARK 470     LYS E 345    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU E  13   CD    GLU E  13   OE2     0.083                       
REMARK 500    GLU E  91   CD    GLU E  91   OE2     0.069                       
REMARK 500    GLU E 121   CD    GLU E 121   OE2     0.095                       
REMARK 500    GLU E 170   CD    GLU E 170   OE2     0.073                       
REMARK 500    GLU E 248   CD    GLU E 248   OE2     0.071                       
REMARK 500    GLU E 349   CD    GLU E 349   OE2     0.068                       
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    GLN E  12   N   -  CA  -  C   ANGL. DEV. = -18.6 DEGREES          
REMARK 500    ASP E  25   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP E  25   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ASP E 112   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG E 133   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG E 133   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ILE E 163   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG E 165   C   -  N   -  CA  ANGL. DEV. = -19.7 DEGREES          
REMARK 500    ASP E 175   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP E 175   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ASP E 241   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP E 267   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP E 267   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP E 290   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ASP E 301   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP E 323   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP E 323   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    TYR S 363   CB  -  CG  -  CD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TYR S 363   CB  -  CG  -  CD1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP S 365   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP S 380   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 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    GLN E  12     -157.09    -69.98                                   
REMARK 500    GLU E  13      -55.44     62.86                                   
REMARK 500    ASN E  36       57.04     35.62                                   
REMARK 500    ILE E  46      -66.00    -98.36                                   
REMARK 500    SER E  53      -72.12    -26.52                                   
REMARK 500    PHE E  54       25.02   -143.81                                   
REMARK 500    ASN E  99      106.81   -165.99                                   
REMARK 500    ASP E 166       45.86   -143.68                                   
REMARK 500    LYS E 168      145.44    179.01                                   
REMARK 500    ASP E 184       83.81     60.97                                   
REMARK 500    ASN E 216     -157.31   -131.41                                   
REMARK 500    LEU E 273       35.37    -80.60                                   
REMARK 500    ILE E 339       51.84   -104.55                                   
REMARK 500    ASN E 340      124.38   -178.70                                   
REMARK 500    LYS E 342      -72.48    -64.50                                   
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 ADP E 381                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OCT E 382                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1APM   RELATED DB: PDB                                   
REMARK 900 1APM CONTAINS THE SAME PROTEIN COMPLEXED WITH PEPTIDE INHIBITOR AND  
REMARK 900 DETERGENT                                                            
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 1ATP CONTAINS THE SAME PROTEIN COMPLEXED WITH MNATP AND PEPTIDE      
REMARK 900 INHIBITOR                                                            
DBREF  1JBP E    1   350  UNP    P05132   KAPCA_MOUSE      1    350             
DBREF  1JBP S  361   380  UNP    P27776   IPKA_MOUSE       5     24             
SEQADV 1JBP SEP E   10  UNP  P05132    SER    10 MODIFIED RESIDUE               
SEQADV 1JBP TPO E  197  UNP  P05132    THR   197 MODIFIED RESIDUE               
SEQADV 1JBP GLU E  242  UNP  P05132    GLN   242 CONFLICT                       
SEQADV 1JBP SEP E  338  UNP  P05132    SER   338 MODIFIED RESIDUE               
SEQADV 1JBP ALA S  376  UNP  P27776    ASN    20 ENGINEERED                     
SEQADV 1JBP SER S  377  UNP  P27776    ALA    21 ENGINEERED                     
SEQRES   1 E  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP 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 SER 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 GLU 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 S   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 S   20  ARG ARG ALA SER ILE HIS ASP                                  
MODRES 1JBP SEP E   10  SER  PHOSPHOSERINE                                      
MODRES 1JBP TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 1JBP SEP E  338  SER  PHOSPHOSERINE                                      
HET    SEP  E  10      10                                                       
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET    ADP  E 381      27                                                       
HET    OCT  E 382       8                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     OCT N-OCTANE                                                         
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  ADP    C10 H15 N5 O10 P2                                            
FORMUL   4  OCT    C8 H18                                                       
FORMUL   5  HOH   *168(H2 O)                                                    
HELIX    1   1 GLU E   13  THR E   32  1                                  20    
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  VAL E   98  1                                  15    
HELIX    5   5 GLU E  127  GLY E  136  1                                  10    
HELIX    6   6 SER 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 GLU 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 LYS E  295  THR E  300  5                                   6    
HELIX   15  15 ASP E  301  GLN E  307  1                                   7    
HELIX   16  16 THR S  361  ALA S  368  1                                   8    
SHEET    1   A 5 PHE E  43  THR E  51  0                                        
SHEET    2   A 5 GLY E  55  HIS E  62 -1  O  VAL E  57   N  LEU E  49           
SHEET    3   A 5 HIS E  68  ASP E  75 -1  O  TYR E  69   N  VAL E  60           
SHEET    4   A 5 ASN E 115  GLU E 121 -1  O  LEU E 116   N  LEU E  74           
SHEET    5   A 5 LEU E 106  LYS E 111 -1  N  GLU E 107   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 S 378  HIS S 379 -1  N  ILE S 378   O  GLY E 200           
LINK         N   SEP E  10                 C   GLY E   9     1555   1555  1.33  
LINK         C   SEP E  10                 N   GLU E  11     1555   1555  1.35  
LINK         N   TPO E 197                 C   TRP E 196     1555   1555  1.33  
LINK         C   TPO E 197                 N   LEU E 198     1555   1555  1.32  
LINK         N   SEP E 338                 C   VAL E 337     1555   1555  1.32  
LINK         C   SEP E 338                 N   ILE E 339     1555   1555  1.31  
SITE     1 AC1 20 LEU E  49  THR E  51  GLY E  52  SER E  53                    
SITE     2 AC1 20 GLY E  55  VAL E  57  ALA E  70  LYS E  72                    
SITE     3 AC1 20 VAL E 104  GLU E 121  VAL E 123  GLU E 127                    
SITE     4 AC1 20 GLU E 170  ASN E 171  LEU E 173  THR E 183                    
SITE     5 AC1 20 ASP E 184  PHE E 327  HOH E 487  ARG S 374                    
SITE     1 AC2  1 GLU E 155                                                     
CRYST1   73.960   76.110   81.000  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      0.013521  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013139  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012346        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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