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Database: PDB
Entry: 1RDQ
LinkDB: 1RDQ
Original site: 1RDQ 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       05-NOV-03   1RDQ              
TITLE     HYDROLYSIS OF ATP IN THE CRYSTAL OF Y204A MUTANT OF CAMP-DEPENDENT    
TITLE    2 PROTEIN KINASE                                                       
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 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM;       
COMPND  10 CHAIN: I;                                                            
COMPND  11 FRAGMENT: RESIDUES 5-24;                                             
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: HOUSE 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 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE  
SOURCE  11 OF THE PROTEIN IS NATURALLY FOUND IN MUS MUSCULUS (MOUSE)            
KEYWDS    CAMP-DEPENDENT PROTEIN KINASE, CATALYTIC MECHANISM, ATP HYDROLYSIS,   
KEYWDS   2 TWO NUCLEOTIDE STATES, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.YANG,L.F.TEN EYCK,N.H.XUONG,S.S.TAYLOR                              
REVDAT   5   31-JAN-18 1RDQ    1       JRNL                                     
REVDAT   4   22-JAN-14 1RDQ    1       REMARK                                   
REVDAT   3   13-JUL-11 1RDQ    1       VERSN                                    
REVDAT   2   24-FEB-09 1RDQ    1       VERSN                                    
REVDAT   1   13-APR-04 1RDQ    0                                                
JRNL        AUTH   J.YANG,L.F.TEN EYCK,N.H.XUONG,S.S.TAYLOR                     
JRNL        TITL   CRYSTAL STRUCTURE OF A CAMP-DEPENDENT PROTEIN KINASE MUTANT  
JRNL        TITL 2 AT 1.26A: NEW INSIGHTS INTO THE CATALYTIC MECHANISM.         
JRNL        REF    J.MOL.BIOL.                   V. 336   473 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   14757059                                                     
JRNL        DOI    10.1016/J.JMB.2003.11.044                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   MADHUSUDAN,P.AKAMINE,N.H.XUONG,S.S.TAYLOR                    
REMARK   1  TITL   CRYSTAL STRUCTURE OF A TRANSITION STATE MIMIC OF THE         
REMARK   1  TITL 2 CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE           
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   9   273 2002              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   1  DOI    10.1038/NSB780                                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.ZHENG,D.R.KNIGHTON,L.F.TEN EYCK,R.KARLSSON,N.H.XUONG,      
REMARK   1  AUTH 2 S.S.TAYLOR,SOWADSKI J.M.                                     
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT 
REMARK   1  TITL 2 PROTEIN KINASE COMPLEXED WITH MGATP AND PEPTIDE INHIBITOR    
REMARK   1  REF    BIOCHEMISTRY                  V.  32  2154 1993              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   P.AKAMINE,MADHUSUDAN,J.WU,N.H.XUONG,L.F.TEN EYCK,S.S.TAYLOR  
REMARK   1  TITL   DYNAMIC FEATURES OF CAMP-DEPENDENT PROTEIN KINASE REVEALED   
REMARK   1  TITL 2 BY APOENZYME CRYSTAL STRUCTURE                               
REMARK   1  REF    J.MOL.BIOL.                   V. 327   159 2003              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1016/S0022-2836(02)01446-8                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.26 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  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.4                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.132                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.162                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 5630                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 122674                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2891                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 79                                            
REMARK   3   SOLVENT ATOMS      : 439                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.060                   
REMARK   3   ANGLE DISTANCES                      (A) : NULL                    
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL                    
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: USED CNS SOLVE 1.0, THEN SHELXL97 FOR     
REMARK   3  ANISOTROPIC REFINEMENT. THE R FACTOR VALUES USED FOR REFINEMENT     
REMARK   3  SHELL ARE ISOTROPIC B                                               
REMARK   4                                                                      
REMARK   4 1RDQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000020669.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
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                  : NULL                               
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   : 114998                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.25300                            
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: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1APM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, BICINE, AMMONIUM ACETATE, PH 8.0,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K                   
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       28.88000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.86950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.75650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.86950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.88000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.75650            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER                         
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: 4680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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     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 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    CG   CD   CE   NZ                                   
REMARK 470     LYS E  21    CG   CD   CE   NZ                                   
REMARK 470     GLU E  24    CD   OE1  OE2                                       
REMARK 470     LYS E  78    CD   CE   NZ                                        
REMARK 470     LYS E  81    CD   CE   NZ                                        
REMARK 470     LYS E  83    CE   NZ                                             
REMARK 470     GLN E 176    CG   CD   OE1  NE2                                  
REMARK 470     GLU E 248    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 254    CE   NZ                                             
REMARK 470     ARG E 256    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS E 285    CG   CD   CE   NZ                                   
REMARK 470     LYS E 295    CD   CE   NZ                                        
REMARK 470     ILE E 315    CG1  CG2  CD1                                       
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 333    CD   OE1  OE2                                       
REMARK 470     GLU E 334    CG   CD   OE1  OE2                                  
REMARK 470     ASN I 520    CG   OD1  ND2                                       
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 E 137   CD  -  NE  -  CZ  ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ARG E 144   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG E 190   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG E 336   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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    ALA E   4      137.87    -39.22                                   
REMARK 500    ASP E 166       49.50   -148.95                                   
REMARK 500    ASP E 184       81.19     64.74                                   
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 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN E 171   OD1                                                    
REMARK 620 2 ASP E 184   OD2  96.0                                              
REMARK 620 3 ADP E 599   O2A  92.4  89.1                                        
REMARK 620 4 ATP E 600   O2A  93.7  88.8   1.3                                  
REMARK 620 5 ADP E 599   O3B 175.9  87.8  86.1  84.8                            
REMARK 620 6 ATP E 600   O3B 176.6  86.9  89.6  88.3   3.6                      
REMARK 620 7 ATP E 600   O2G 109.6  86.0 157.9 156.6  72.2  68.7                
REMARK 620 8 HOH E1146   O    86.3 177.7  90.5  90.7  89.9  90.9  93.6          
REMARK 620 9 PO4 E 598   O4  100.3  87.9 167.3 165.9  81.4  77.9   9.4  92.1    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 184   OD1                                                    
REMARK 620 2 ASP E 184   OD2  59.2                                              
REMARK 620 3 PO4 E 598   O2  148.2  89.5                                        
REMARK 620 4 HOH E1028   O    97.3 155.6 114.4                                  
REMARK 620 5 ADP E 599   O1B  90.1  87.7  94.1  85.5                            
REMARK 620 6 ATP E 600   O1B  88.2  87.6  96.3  84.7   2.2                      
REMARK 620 7 ATP E 600   O3G 153.4  94.2   7.0 109.1  89.1  91.3                
REMARK 620 8 HOH E1029   O    85.2  92.3  91.4  92.2 174.5 172.3  96.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 598                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 599                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD E 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 700                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ATP   RELATED DB: PDB                                   
REMARK 900 THE WILD TYPE PROTEIN WITH SAME LIGANDS ATP AND INHIBITORY PEPTIDE   
DBREF  1RDQ E    1   350  UNP    P05132   KAPCA_MOUSE      1    350             
DBREF  1RDQ I  505   524  PDB    1RDQ     1RDQ           505    524             
SEQADV 1RDQ TPO E  197  UNP  P05132    THR   197 MODIFIED RESIDUE               
SEQADV 1RDQ ALA E  204  UNP  P05132    TYR   204 ENGINEERED                     
SEQADV 1RDQ SEP E  338  UNP  P05132    SER   338 MODIFIED RESIDUE               
SEQRES   1 E  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 E  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 E  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 E  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 E  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 E  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 E  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 E  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 E  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 E  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 E  350  HIS LEU ARG ARG ILE GLY ARG PHE 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 ALA 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 ASN ALA ILE HIS ASP                                  
MODRES 1RDQ TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 1RDQ SEP E  338  SER  PHOSPHOSERINE                                      
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET    PO4  E 598       5                                                       
HET     MG  E 601       1                                                       
HET     MG  E 602       1                                                       
HET    ADP  E 599      27                                                       
HET    ATP  E 600      31                                                       
HET    MRD  E 800       8                                                       
HET    GOL  E 700       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  ADP    C10 H15 N5 O10 P2                                            
FORMUL   7  ATP    C10 H16 N5 O13 P3                                            
FORMUL   8  MRD    C6 H14 O2                                                    
FORMUL   9  GOL    C3 H8 O3                                                     
FORMUL  10  HOH   *439(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 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 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  505  ALA I  512  1                                   8    
SHEET    1   A 5 PHE E  43  THR E  51  0                                        
SHEET    2   A 5 ARG E  56  HIS E  62 -1  O  VAL E  57   N  GLY E  50           
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           
SHEET    1   D 2 CYS E 199  GLY E 200  0                                        
SHEET    2   D 2 ILE I 522  HIS I 523 -1  O  ILE I 522   N  GLY E 200           
LINK         C   TRP E 196                 N   TPO E 197     1555   1555  1.34  
LINK         C   TPO E 197                 N   LEU E 198     1555   1555  1.33  
LINK         C   VAL E 337                 N   SEP E 338     1555   1555  1.31  
LINK         C   SEP E 338                 N   ILE E 339     1555   1555  1.33  
LINK         OD1 ASN E 171                MG    MG E 601     1555   1555  2.06  
LINK         OD1 ASP E 184                MG    MG E 602     1555   1555  2.23  
LINK         OD2 ASP E 184                MG    MG E 602     1555   1555  2.20  
LINK         OD2 ASP E 184                MG    MG E 601     1555   1555  2.03  
LINK         O2 APO4 E 598                MG    MG E 602     1555   1555  1.95  
LINK        MG    MG E 601                 O2AAADP E 599     1555   1555  1.97  
LINK        MG    MG E 601                 O2ABATP E 600     1555   1555  1.89  
LINK        MG    MG E 601                 O3BAADP E 599     1555   1555  2.11  
LINK        MG    MG E 601                 O3BBATP E 600     1555   1555  2.31  
LINK        MG    MG E 601                 O2GBATP E 600     1555   1555  2.13  
LINK        MG    MG E 601                 O   HOH E1146     1555   1555  2.01  
LINK        MG    MG E 602                 O   HOH E1028     1555   1555  2.07  
LINK        MG    MG E 602                 O1BAADP E 599     1555   1555  2.09  
LINK        MG    MG E 602                 O1BBATP E 600     1555   1555  2.03  
LINK        MG    MG E 602                 O3GBATP E 600     1555   1555  2.05  
LINK        MG    MG E 602                 O   HOH E1029     1555   1555  2.10  
LINK         O4 APO4 E 598                MG    MG E 601     1555   1555  1.74  
SITE     1 AC1 13 SER E  53  PHE E  54  ASP E 166  LYS E 168                    
SITE     2 AC1 13 ASN E 171  ASP E 184  THR E 201  ADP E 599                    
SITE     3 AC1 13  MG E 601   MG E 602  HOH E1029  HOH E1146                    
SITE     4 AC1 13 ALA I 521                                                     
SITE     1 AC2  6 ASN E 171  ASP E 184  PO4 E 598  ADP E 599                    
SITE     2 AC2  6 ATP E 600  HOH E1146                                          
SITE     1 AC3  6 ASP E 184  PO4 E 598  ADP E 599  ATP E 600                    
SITE     2 AC3  6 HOH E1028  HOH E1029                                          
SITE     1 AC4 26 GLY E  50  GLY E  52  SER E  53  PHE E  54                    
SITE     2 AC4 26 GLY E  55  VAL E  57  ALA E  70  LYS E  72                    
SITE     3 AC4 26 VAL E 104  MET E 120  GLU E 121  VAL E 123                    
SITE     4 AC4 26 GLU E 127  GLU E 170  ASN E 171  LEU E 173                    
SITE     5 AC4 26 THR E 183  ASP E 184  PHE E 327  PO4 E 598                    
SITE     6 AC4 26  MG E 601   MG E 602  HOH E1028  HOH E1035                    
SITE     7 AC4 26 HOH E1146  ARG I 518                                          
SITE     1 AC5 29 GLY E  50  GLY E  52  SER E  53  PHE E  54                    
SITE     2 AC5 29 GLY E  55  VAL E  57  ALA E  70  LYS E  72                    
SITE     3 AC5 29 VAL E 104  MET E 120  GLU E 121  VAL E 123                    
SITE     4 AC5 29 GLU E 127  ASP E 166  LYS E 168  GLU E 170                    
SITE     5 AC5 29 ASN E 171  LEU E 173  THR E 183  ASP E 184                    
SITE     6 AC5 29 PHE E 327   MG E 601   MG E 602  HOH E1020                    
SITE     7 AC5 29 HOH E1028  HOH E1029  HOH E1035  HOH E1146                    
SITE     8 AC5 29 ARG I 518                                                     
SITE     1 AC6  5 VAL E  15  PHE E  18  LEU E 152  GLU E 155                    
SITE     2 AC6  5 TYR E 306                                                     
SITE     1 AC7  8 ASP E  44  ARG E  45  PRO E 141  HOH E1147                    
SITE     2 AC7  8 HOH E1171  HOH E1275  HOH E1315  HOH E1408                    
CRYST1   57.760   79.513   97.739  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      0.017313  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012577  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010231        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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