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Database: PDB
Entry: 1L3R
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HEADER    TRANSFERASE                             28-FEB-02   1L3R              
TITLE     CRYSTAL STRUCTURE OF A TRANSITION STATE MIMIC OF THE                  
TITLE    2 CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC             
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: E;                                                            
COMPND   5 SYNONYM: PKA C-ALPHA;                                                
COMPND   6 EC: 2.7.1.37;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,                   
COMPND  10 MUSCLE/BRAIN FORM;                                                   
COMPND  11 CHAIN: I;                                                            
COMPND  12 FRAGMENT: RESIDUES 5-24;                                             
COMPND  13 SYNONYM: PKI-ALPHA;                                                  
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 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           
SOURCE  10 SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN MUS MUSCULUS           
SOURCE  11 (MOUSE).                                                             
KEYWDS    PROTEIN KINASE, PROTEIN-ALF3 COMPLEX, TRANSITION STATE                
KEYWDS   2 MIMIC, TRANSFERASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    MADHUSUDAN,P.AKAMINE,N.-H.XUONG,S.S.TAYLOR                            
REVDAT   4   24-FEB-09 1L3R    1       VERSN                                    
REVDAT   3   01-APR-03 1L3R    1       JRNL                                     
REVDAT   2   27-MAR-02 1L3R    1       JRNL                                     
REVDAT   1   20-MAR-02 1L3R    0                                                
JRNL        AUTH   MADHUSUDAN,P.AKAMINE,N.H.XUONG,S.S.TAYLOR                    
JRNL        TITL   CRYSTAL STRUCTURE OF A TRANSITION STATE MIMIC OF             
JRNL        TITL 2 THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN              
JRNL        TITL 3 KINASE.                                                      
JRNL        REF    NAT.STRUCT.BIOL.              V.   9   273 2002              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11896404                                                     
JRNL        DOI    10.1038/NSB780                                               
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             
REMARK   1  TITL 2 SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED           
REMARK   1  TITL 3 WITH A PEPTIDE 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             
REMARK   1  TITL 2 SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED           
REMARK   1  TITL 3 WITH MNATP AND A 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   1 REFERENCE 3                                                          
REMARK   1  AUTH   MADHUSUDAN,E.A.TRAFNY,N.H.XUONG,J.A.ADAMS,                   
REMARK   1  AUTH 2 L.F.TEN EYCK,S.S.TAYLOR,J.M.SOWADSKI                         
REMARK   1  TITL   CAMP-DEPENDENT PROTEIN KINASE: CRYSTALLOGRAFIC               
REMARK   1  TITL 2 INSIGHTS INTO SUBSTRATE RECOGNITION AND                      
REMARK   1  TITL 3 PHOSPHOTRANSFER                                              
REMARK   1  REF    PROTEIN SCI.                  V.   3   176 1994              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 30443                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1819                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900                       
REMARK   3   BIN FREE R VALUE                    : 0.3170                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2886                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 241                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.96800                                              
REMARK   3    B22 (A**2) : -10.94100                                            
REMARK   3    B33 (A**2) : 9.97300                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.28                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : PHOSPHO_RESI.PARAM                             
REMARK   3  PARAMETER FILE  3  : DNA-RNA.PARAM                                  
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1L3R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015617.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : 58 CM LONG, PT-COATED, FUSED       
REMARK 200                                   SILICA, VERTICAL FOCUSMIRROR,      
REMARK 200                                   CYCLINDRICALLY BENT TRIANGULAR     
REMARK 200                                   SI(111) ASYMMETRIC CUT,            
REMARK 200                                   HORIZONTAL FOCUS MONOCHROMATOR     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30443                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.5000                            
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) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.40900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1JBP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, BICINE, METHANOL, AMMONIUM          
REMARK 280  ACETATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  277K                                                                
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       36.34000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.27500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.27500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.34000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.85000            
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: 3920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 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     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     SEP E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     GLN E    12                                                      
REMARK 465     GLU E    13                                                      
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     ASN E   2    CG   OD1  ND2                                       
REMARK 470     SER E  14    OG                                                  
REMARK 470     VAL E  15    CG1  CG2                                            
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  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 105    CG   CD   CE   NZ                                   
REMARK 470     LYS E 285    CG   CD   CE   NZ                                   
REMARK 470     ASN E 286    CG   OD1  ND2                                       
REMARK 470     LYS E 309    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 334    CG   CD   OE1  OE2                                  
REMARK 470     ILE E 339    CG1  CG2  CD1                                       
REMARK 470     LYS E 345    CG   CD   CE   NZ                                   
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  41        3.94    -68.91                                   
REMARK 500    ILE E  46      -60.36   -102.22                                   
REMARK 500    ASP E 166       44.24   -148.51                                   
REMARK 500    ASP E 184       81.19     57.18                                   
REMARK 500    LEU E 273       48.28    -86.11                                   
REMARK 500    LYS E 319       33.72    -72.39                                   
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 392  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP E 381   O2A                                                    
REMARK 620 2 HOH E 578   O    88.2                                              
REMARK 620 3 ADP E 381   O3B  81.4  93.2                                        
REMARK 620 4 AF3 E 400  AL   131.6  98.0  50.4                                  
REMARK 620 5 AF3 E 400   F1  167.8  89.7  86.7  37.1                            
REMARK 620 6 ASP E 184   OD2  87.2 174.0  82.4  82.3  94.1                      
REMARK 620 7 ASN E 171   OD1  95.2  90.5 175.0 132.4  96.8  93.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 391  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 184   OD2                                                    
REMARK 620 2 ADP E 381   O2B  77.3                                              
REMARK 620 3 HOH E 576   O   160.4  96.2                                        
REMARK 620 4 AF3 E 400   F2   96.1  96.7 103.0                                  
REMARK 620 5 HOH E 577   O    93.7 171.0  92.6  83.4                            
REMARK 620 6 ASP E 184   OD1  57.9  86.5 103.6 152.6  89.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 E 400  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 166   OD1                                                    
REMARK 620 2 SER I  21   OG   42.9                                              
REMARK 620 3  MG E 391  MG    68.7 102.4                                        
REMARK 620 4 ADP E 381   O3B 119.9 162.6  66.5                                  
REMARK 620 5 ASP E 184   OD2  67.6 110.4  40.4  52.4                            
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 MG E 391                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 392                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 381                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 E 400                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 382                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1APM   RELATED DB: PDB                                   
REMARK 900 1APM CONTAINS THE SAME PROTEIN COMPLEX WITH PEPTIDE                  
REMARK 900 INHIBITOR AND DETERGENT                                              
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 1ATP CONTAINS THE SAME PROTEIN COMPLEXED WITH MNATP AND              
REMARK 900 PEPTIDE INHIBITOR                                                    
REMARK 900 RELATED ID: 1JBP   RELATED DB: PDB                                   
REMARK 900 1JBP CONTAINS THE SAME PROTEIN COMPLEXED WITH ADP AND THE            
REMARK 900 SAME PEPTIDE SUBSTRATE                                               
DBREF  1L3R E    1   350  UNP    P05132   KAPCA_MOUSE      1    350             
DBREF  1L3R I    5    24  UNP    P27776   IPKA_MOUSE       5     24             
SEQADV 1L3R SEP E   10  UNP  P05132    SER    10 MODIFIED RESIDUE               
SEQADV 1L3R SEP E  139  UNP  P05132    SER   139 MODIFIED RESIDUE               
SEQADV 1L3R TPO E  197  UNP  P05132    THR   197 MODIFIED RESIDUE               
SEQADV 1L3R SEP E  338  UNP  P05132    SER   338 MODIFIED RESIDUE               
SEQADV 1L3R ALA I   20  UNP  P27776    ASN    20 ENGINEERED                     
SEQADV 1L3R SER I   21  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 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 1L3R SEP E  139  SER  PHOSPHOSERINE                                      
MODRES 1L3R TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 1L3R SEP E  338  SER  PHOSPHOSERINE                                      
HET    SEP  E 139      10                                                       
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET     MG  E 391       1                                                       
HET     MG  E 392       1                                                       
HET    ADP  E 381      27                                                       
HET    AF3  E 400       4                                                       
HET    MPD  E 382       8                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     AF3 ALUMINUM FLUORIDE                                                
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
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   MG    2(MG 2+)                                                     
FORMUL   5  ADP    C10 H15 N5 O10 P2                                            
FORMUL   6  AF3    AL F3                                                        
FORMUL   7  MPD    C6 H14 O2                                                    
FORMUL   8  HOH   *233(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 I    5  SER I   13  1                                   9    
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  MET E  71   N  MET E  58           
SHEET    4   A 5 ASN E 115  GLU E 121 -1  O  MET E 118   N  LYS E  72           
SHEET    5   A 5 LEU E 106  LYS E 111 -1  N  PHE E 110   O  TYR E 117           
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  1.33  
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         O2A ADP E 381                MG    MG E 392     1555   1555  1.88  
LINK        MG    MG E 391                 OD2 ASP E 184     1555   1555  2.32  
LINK        MG    MG E 391                 O2B ADP E 381     1555   1555  2.13  
LINK        MG    MG E 391                 O   HOH E 576     1555   1555  2.12  
LINK        MG    MG E 391                 F2  AF3 E 400     1555   1555  1.97  
LINK        MG    MG E 391                 O   HOH E 577     1555   1555  2.36  
LINK        MG    MG E 391                 OD1 ASP E 184     1555   1555  2.21  
LINK        MG    MG E 392                 O   HOH E 578     1555   1555  2.18  
LINK        MG    MG E 392                 O3B ADP E 381     1555   1555  2.06  
LINK        MG    MG E 392                AL   AF3 E 400     1555   1555  2.99  
LINK        MG    MG E 392                 F1  AF3 E 400     1555   1555  1.97  
LINK        MG    MG E 392                 OD2 ASP E 184     1555   1555  2.00  
LINK        MG    MG E 392                 OD1 ASN E 171     1555   1555  2.11  
LINK        AL   AF3 E 400                 OD1 ASP E 166     1555   1555  3.61  
LINK        AL   AF3 E 400                 OG  SER I  21     1555   1555  2.27  
LINK        AL   AF3 E 400                MG    MG E 391     1555   1555  3.35  
LINK        AL   AF3 E 400                 O3B ADP E 381     1555   1555  2.31  
LINK        AL   AF3 E 400                 OD2 ASP E 184     1555   1555  3.37  
SITE     1 AC1  5 ASP E 184  ADP E 381  AF3 E 400  HOH E 576                    
SITE     2 AC1  5 HOH E 577                                                     
SITE     1 AC2  5 ASN E 171  ASP E 184  ADP E 381  AF3 E 400                    
SITE     2 AC2  5 HOH E 578                                                     
SITE     1 AC3 25 GLY E  50  GLY E  52  SER E  53  PHE E  54                    
SITE     2 AC3 25 GLY E  55  VAL E  57  ALA E  70  LYS E  72                    
SITE     3 AC3 25 VAL E 104  MET E 120  GLU E 121  VAL E 123                    
SITE     4 AC3 25 GLU E 127  GLU E 170  ASN E 171  LEU E 173                    
SITE     5 AC3 25 THR E 183  ASP E 184  PHE E 327   MG E 391                    
SITE     6 AC3 25  MG E 392  AF3 E 400  HOH E 414  HOH E 578                    
SITE     7 AC3 25 ARG I  18                                                     
SITE     1 AC4 13 GLY E  52  SER E  53  PHE E  54  ASP E 166                    
SITE     2 AC4 13 LYS E 168  ASN E 171  ASP E 184  ADP E 381                    
SITE     3 AC4 13  MG E 391   MG E 392  HOH E 577  HOH E 578                    
SITE     4 AC4 13 SER I  21                                                     
SITE     1 AC5  5 PHE E  18  LEU E 152  GLU E 155  TYR E 306                    
SITE     2 AC5  5 HOH E 609                                                     
CRYST1   72.680   75.700   80.550  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      0.013759  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013210  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012415        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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