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Database: PDB
Entry: 4DH5
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Original site: 4DH5 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       27-JAN-12   4DH5              
TITLE     ROOM TEMPERATURE X-RAY STRUCTURE OF CAMP DEPENDENT PROTEIN KINASE A   
TITLE    2 CATALYTIC SUBUNIT WITH HIGH MG2+, ADP, PHOSPHATE, AND IP20           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;             
COMPND   9 CHAIN: I;                                                            
COMPND  10 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,         
COMPND  11 MUSCLE/BRAIN ISOFORM;                                                
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 OTHER_DETAILS: PEPTIDIC INHIBITOR IP20 WAS CHEMICALLY SYNTHESIZED    
KEYWDS    PROTEIN KINASE, PHOSPHOTRANSFER, PEPTIDIC INHIBITOR, TRANSFERASE-     
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.Y.KOVALEVSKY,P.LANGAN                                               
REVDAT   2   23-JAN-13 4DH5    1       JRNL                                     
REVDAT   1   27-JUN-12 4DH5    0                                                
JRNL        AUTH   A.Y.KOVALEVSKY,H.JOHNSON,B.L.HANSON,M.J.WALTMAN,S.Z.FISHER,  
JRNL        AUTH 2 S.TAYLOR,P.LANGAN                                            
JRNL        TITL   LOW- AND ROOM-TEMPERATURE X-RAY STRUCTURES OF PROTEIN KINASE 
JRNL        TITL 2 A TERNARY COMPLEXES SHED NEW LIGHT ON ITS ACTIVITY.          
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  68   854 2012              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   22751671                                                     
JRNL        DOI    10.1107/S0907444912014886                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 19474                          
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) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 978                             
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
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            : 2938                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 211                                     
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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) : NULL                            
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4DH5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070322.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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 FR-E DW                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NONE                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19474                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.400                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES (PH=6.5), 50 MM MG2CL, 5 MM    
REMARK 280  DTT AND 12-15% PEG4000, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 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       29.45000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.74500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.81500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.74500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.45000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.81500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     GLY A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     SER A    14                                                      
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    ASN A  36       63.71     38.21                                   
REMARK 500    ASP A  41        3.10    -67.74                                   
REMARK 500    ILE A  46      -61.53   -105.68                                   
REMARK 500    PHE A  54      -63.54   -100.09                                   
REMARK 500    ASP A 166       40.67   -142.40                                   
REMARK 500    LYS A 168      156.10    178.69                                   
REMARK 500    ASP A 184       85.13     61.40                                   
REMARK 500    ALA A 240     -176.07   -174.54                                   
REMARK 500    LEU A 273       45.42    -91.97                                   
REMARK 500    LYS A 319       75.33   -104.31                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  45         0.29    SIDE CHAIN                              
REMARK 500    ARG A  56         0.10    SIDE CHAIN                              
REMARK 500    ARG A  93         0.09    SIDE CHAIN                              
REMARK 500    ARG A 133         0.26    SIDE CHAIN                              
REMARK 500    ARG A 137         0.10    SIDE CHAIN                              
REMARK 500    ARG A 144         0.07    SIDE CHAIN                              
REMARK 500    ARG A 190         0.13    SIDE CHAIN                              
REMARK 500    ARG A 256         0.12    SIDE CHAIN                              
REMARK 500    ARG A 308         0.11    SIDE CHAIN                              
REMARK 500    ARG A 336         0.13    SIDE CHAIN                              
REMARK 500    ARG I  15         0.29    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU A 277        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1088        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A1101        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH A1104        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH A1178        DISTANCE =  7.62 ANGSTROMS                       
REMARK 525    HOH A1180        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A1192        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH A1193        DISTANCE =  5.07 ANGSTROMS                       
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 A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PO4 A 404   O4                                                     
REMARK 620 2 ASP A 184   OD2  88.2                                              
REMARK 620 3 ADP A 403   O3B 109.4  83.7                                        
REMARK 620 4 ASN A 171   OD1  81.8  93.4 168.2                                  
REMARK 620 5 ADP A 403   O2A 158.7  74.2  81.0  87.3                            
REMARK 620 6 HOH A1002   O   108.3 163.5  91.8  87.8  89.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PO4 A 404   O3                                                     
REMARK 620 2 ADP A 403   O1B 108.5                                              
REMARK 620 3 ASP A 184   OD2  87.8  70.3                                        
REMARK 620 4 ASP A 184   OD1 134.8  76.7  50.7                                  
REMARK 620 5 HOH A1001   O   131.7  93.8 140.5  91.2                            
REMARK 620 6 HOH A1003   O    89.3 152.6  90.4  76.1  89.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 404                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DH1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DH3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DH7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DH8   RELATED DB: PDB                                   
DBREF  4DH5 A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4DH5 I    5    24  UNP    P63248   IPKA_MOUSE       6     25             
SEQRES   1 A  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 A  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 A  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 A  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 A  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 A  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 A  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 A  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 A  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 A  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 A  350  HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA          
SEQRES  12 A  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 A  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 A  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 A  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 A  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 A  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 A  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 A  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 A  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 A  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 A  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 A  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 A  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 A  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 A  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 A  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 4DH5 SEP A  139  SER  PHOSPHOSERINE                                      
MODRES 4DH5 TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 4DH5 SEP A  338  SER  PHOSPHOSERINE                                      
HET    SEP  A 139      10                                                       
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET     MG  A 401       1                                                       
HET     MG  A 402       1                                                       
HET    ADP  A 403      27                                                       
HET    PO4  A 404       5                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     PO4 PHOSPHATE ION                                                    
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  PO4    O4 P 3-                                                      
FORMUL   7  HOH   *211(H2 O)                                                    
HELIX    1   1 VAL A   15  THR A   32  1                                  18    
HELIX    2   2 GLN A   39  ASP A   41  5                                   3    
HELIX    3   3 LYS A   76  LEU A   82  1                                   7    
HELIX    4   4 GLN A   84  GLN A   96  1                                  13    
HELIX    5   5 GLU A  127  GLY A  136  1                                  10    
HELIX    6   6 SEP A  139  LEU A  160  1                                  22    
HELIX    7   7 LYS A  168  GLU A  170  5                                   3    
HELIX    8   8 THR A  201  LEU A  205  5                                   5    
HELIX    9   9 ALA A  206  LEU A  211  1                                   6    
HELIX   10  10 LYS A  217  GLY A  234  1                                  18    
HELIX   11  11 GLN A  242  GLY A  253  1                                  12    
HELIX   12  12 SER A  262  LEU A  273  1                                  12    
HELIX   13  13 VAL A  288  ASN A  293  1                                   6    
HELIX   14  14 HIS A  294  ALA A  298  5                                   5    
HELIX   15  15 ASP A  301  GLN A  307  1                                   7    
HELIX   16  16 THR I    6  ALA I   12  1                                   7    
SHEET    1   A 5 PHE A  43  THR A  51  0                                        
SHEET    2   A 5 ARG A  56  HIS A  62 -1  O  LEU A  59   N  LYS A  47           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  MET A  71   N  MET A  58           
SHEET    4   A 5 ASN A 115  GLU A 121 -1  O  MET A 118   N  LYS A  72           
SHEET    5   A 5 LEU A 106  LYS A 111 -1  N  GLU A 107   O  VAL A 119           
SHEET    1   B 2 LEU A 162  ILE A 163  0                                        
SHEET    2   B 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1   C 2 LEU A 172  ILE A 174  0                                        
SHEET    2   C 2 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
LINK         C   PHE A 138                 N   SEP A 139     1555   1555  1.33  
LINK         C   SEP A 139                 N   GLU A 140     1555   1555  1.33  
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.33  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.33  
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.33  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
LINK        MG    MG A 402                 O4  PO4 A 404     1555   1555  1.99  
LINK        MG    MG A 401                 O3  PO4 A 404     1555   1555  2.14  
LINK        MG    MG A 401                 O1B ADP A 403     1555   1555  2.23  
LINK         OD2 ASP A 184                MG    MG A 402     1555   1555  2.26  
LINK        MG    MG A 402                 O3B ADP A 403     1555   1555  2.32  
LINK         OD1 ASN A 171                MG    MG A 402     1555   1555  2.37  
LINK        MG    MG A 402                 O2A ADP A 403     1555   1555  2.40  
LINK         OD2 ASP A 184                MG    MG A 401     1555   1555  2.40  
LINK         OD1 ASP A 184                MG    MG A 401     1555   1555  2.67  
LINK        MG    MG A 401                 O   HOH A1001     1555   1555  2.13  
LINK        MG    MG A 402                 O   HOH A1002     1555   1555  2.13  
LINK        MG    MG A 401                 O   HOH A1003     1555   1555  2.27  
SITE     1 AC1  5 ASP A 184  ADP A 403  PO4 A 404  HOH A1001                    
SITE     2 AC1  5 HOH A1003                                                     
SITE     1 AC2  5 ASN A 171  ASP A 184  ADP A 403  PO4 A 404                    
SITE     2 AC2  5 HOH A1002                                                     
SITE     1 AC3 25 GLY A  52  GLY A  55  VAL A  57  ALA A  70                    
SITE     2 AC3 25 LYS A  72  VAL A 104  MET A 120  GLU A 121                    
SITE     3 AC3 25 TYR A 122  VAL A 123  GLU A 127  GLU A 170                    
SITE     4 AC3 25 ASN A 171  LEU A 173  THR A 183  ASP A 184                    
SITE     5 AC3 25 PHE A 327   MG A 401   MG A 402  PO4 A 404                    
SITE     6 AC3 25 HOH A1002  HOH A1148  HOH A1152  HOH A1158                    
SITE     7 AC3 25 ARG I  18                                                     
SITE     1 AC4 12 ASP A 166  LYS A 168  ASN A 171  ASP A 184                    
SITE     2 AC4 12 THR A 201   MG A 401   MG A 402  ADP A 403                    
SITE     3 AC4 12 HOH A1084  HOH A1158  ASN I  20  ALA I  21                    
CRYST1   58.900   79.630   99.490  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      0.016978  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012558  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010051        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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