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Database: PDB
Entry: 4DIN
LinkDB: 4DIN
Original site: 4DIN 
HEADER    TRANSFERASE/TRANSPORT PROTEIN           31-JAN-12   4DIN              
TITLE     NOVEL LOCALIZATION AND QUATERNARY STRUCTURE OF THE PKA RI BETA        
TITLE    2 HOLOENZYME                                                           
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 TYPE I-BETA REGULATORY       
COMPND   9 SUBUNIT;                                                             
COMPND  10 CHAIN: B;                                                            
COMPND  11 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 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PRKAR1B;                                                       
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ISOFORM DIVERSITY, RIB2:C2 TETRAMERIC COMPLEX, TRANSFERASE-TRANSPORT  
KEYWDS   2 PROTEIN COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ILOUZ,J.BUBIS,J.WU,Y.Y.YIM,M.S.DEAL,A.P.KORNEV,Y.MA,D.K.BLUMENTHAL, 
AUTHOR   2 S.S.TAYLOR                                                           
REVDAT   2   12-DEC-12 4DIN    1       JRNL                                     
REVDAT   1   04-JUL-12 4DIN    0                                                
JRNL        AUTH   R.ILOUZ,J.BUBIS,J.WU,Y.Y.YIM,M.S.DEAL,A.P.KORNEV,Y.MA,       
JRNL        AUTH 2 D.K.BLUMENTHAL,S.S.TAYLOR                                    
JRNL        TITL   LOCALIZATION AND QUATERNARY STRUCTURE OF THE PKA RI BETA     
JRNL        TITL 2 HOLOENZYME                                                   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109 12443 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22797896                                                     
JRNL        DOI    10.1073/PNAS.1209538109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.3 WITH DEN REFINEMENT                          
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2517.000                       
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 67.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 9613                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.293                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 495                             
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.83                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 30.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 406                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3676                       
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 22                           
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            : 5393                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 156.49                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 44.26900                                             
REMARK   3    B22 (A**2) : 44.26900                                             
REMARK   3    B33 (A**2) : -88.53900                                            
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) : 0.003                           
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) : 11.521; 15.000               
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 17.819; 20.000               
REMARK   3   SIDE-CHAIN BOND              (A**2) : 16.915; 20.000               
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 23.637; 25.000               
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 143.40                                               
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 4DIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070376.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16198                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 9.300                              
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2QCS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M AMMONIUM SULFATE,  0.1M SODIUM     
REMARK 280  ACETATE PH 5.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+1/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+2/3                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.88200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       97.76400            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       48.88200            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       97.76400            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       48.88200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       97.76400            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       48.88200            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       97.76400            
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: 5690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     MET B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     CYS B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     GLU B    59                                                      
REMARK 465     ASN B    60                                                      
REMARK 465     ARG B    61                                                      
REMARK 465     GLN B    62                                                      
REMARK 465     ILE B    63                                                      
REMARK 465     LEU B    64                                                      
REMARK 465     ALA B    65                                                      
REMARK 465     ARG B    66                                                      
REMARK 465     GLN B    67                                                      
REMARK 465     LYS B    68                                                      
REMARK 465     SER B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     SER B    71                                                      
REMARK 465     GLN B    72                                                      
REMARK 465     SER B    73                                                      
REMARK 465     ASP B    74                                                      
REMARK 465     SER B    75                                                      
REMARK 465     HIS B    76                                                      
REMARK 465     ASP B    77                                                      
REMARK 465     GLU B    78                                                      
REMARK 465     GLU B    79                                                      
REMARK 465     VAL B    80                                                      
REMARK 465     VAL B   379                                                      
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     SER A  10    OG                                                  
REMARK 470     GLU A  11    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  16    CG   CD   CE   NZ                                   
REMARK 470     GLU A  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     GLU A  24    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  25    CG   OD1  OD2                                       
REMARK 470     LYS A  81    CD   CE   NZ                                        
REMARK 470     ARG A  93    CZ   NH1  NH2                                       
REMARK 470     LYS A 105    CD   CE   NZ                                        
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     ARG A 256    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 309    CE   NZ                                             
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     PHE A 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 470     GLU A 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 334    CG   CD   OE1                                       
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     LYS B  14    CG   CD   CE   NZ                                   
REMARK 470     LEU B  18    CG   CD1  CD2                                       
REMARK 470     TYR B  19    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL B  20    CG1  CG2                                            
REMARK 470     HIS B  23    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE B  25    CG1  CG2  CD1                                       
REMARK 470     GLN B  26    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  27    CG   CD   OE1  NE2                                  
REMARK 470     VAL B  28    CG1  CG2                                            
REMARK 470     LEU B  29    CG   CD1  CD2                                       
REMARK 470     LYS B  30    CG   CD   CE   NZ                                   
REMARK 470     ASP B  31    CG   OD1  OD2                                       
REMARK 470     CYS B  32    SG                                                  
REMARK 470     CYS B  37    SG                                                  
REMARK 470     ILE B  38    CG1  CG2  CD1                                       
REMARK 470     SER B  39    OG                                                  
REMARK 470     LYS B  40    CG   CD   CE   NZ                                   
REMARK 470     GLU B  42    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B  44    CG   CD                                             
REMARK 470     MET B  45    CG   SD   CE                                        
REMARK 470     LYS B  46    CG   CD   CE   NZ                                   
REMARK 470     SER B  81    OG                                                  
REMARK 470     THR B  83    OG1  CG2                                            
REMARK 470     ASN B  86    CG   OD1  ND2                                       
REMARK 470     LYS B  90    CG   CD   CE   NZ                                   
REMARK 470     LYS B 114    CD   CE   NZ                                        
REMARK 470     TYR B 120    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 121    CD   CE   NZ                                        
REMARK 470     LYS B 128    CE   NZ                                             
REMARK 470     GLN B 177    CD   OE1  NE2                                       
REMARK 470     LYS B 279    CE   NZ                                             
REMARK 470     THR B 378    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    PRO B   271     O    CYS B   345              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL B 272   CB  -  CA  -  C   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    GLN B 273   N   -  CA  -  CB  ANGL. DEV. =  11.8 DEGREES          
REMARK 500    SER B 305   CB  -  CA  -  C   ANGL. DEV. =  13.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  12      -31.96    178.77                                   
REMARK 500    SER A  14      -39.28    -34.41                                   
REMARK 500    PRO A  33     -156.94    -65.85                                   
REMARK 500    SER A  34      -80.50   -115.93                                   
REMARK 500    GLN A  35     -173.89     80.87                                   
REMARK 500    ASN A  36     -120.51     38.53                                   
REMARK 500    THR A  37      -18.36     81.33                                   
REMARK 500    ALA A  38     -162.57    158.74                                   
REMARK 500    ASP A  41      -12.50    -49.35                                   
REMARK 500    ILE A  46      -87.19    -58.98                                   
REMARK 500    PHE A  54      -86.03   -116.19                                   
REMARK 500    HIS A  62      130.27    -34.90                                   
REMARK 500    GLU A  64      -77.89    -69.22                                   
REMARK 500    ASN A  67     -172.70    -61.69                                   
REMARK 500    ALA A  70       78.49   -117.59                                   
REMARK 500    GLN A  96        0.36    -68.33                                   
REMARK 500    PHE A 102       39.22    -96.60                                   
REMARK 500    GLU A 107      -72.06    -72.12                                   
REMARK 500    PHE A 110     -166.50   -167.14                                   
REMARK 500    ASP A 112     -116.84   -131.37                                   
REMARK 500    TYR A 164      -78.02    -64.69                                   
REMARK 500    ARG A 165       51.46     71.93                                   
REMARK 500    ASP A 166       23.84   -179.57                                   
REMARK 500    ASP A 175     -138.18    -70.82                                   
REMARK 500    GLN A 177        2.92    -65.19                                   
REMARK 500    TYR A 179     -154.58   -103.68                                   
REMARK 500    ASP A 184      102.02     51.22                                   
REMARK 500    LYS A 189      146.28   -170.75                                   
REMARK 500    LYS A 192       59.63   -101.75                                   
REMARK 500    TRP A 196      -37.61   -131.34                                   
REMARK 500    ASN A 216     -157.88   -132.34                                   
REMARK 500    VAL A 255      126.36   -176.46                                   
REMARK 500    ARG A 256       54.31   -100.46                                   
REMARK 500    HIS A 260      -15.27   -143.60                                   
REMARK 500    ARG A 270      -70.63    -57.93                                   
REMARK 500    LEU A 273       32.17    -72.83                                   
REMARK 500    THR A 278       -9.33    -57.88                                   
REMARK 500    ASN A 283      -33.67   -140.32                                   
REMARK 500    LEU A 284     -174.57    -59.37                                   
REMARK 500    PRO A 316     -178.96    -60.07                                   
REMARK 500    LYS A 319       57.79   -104.98                                   
REMARK 500    ASN A 326       -7.95    -56.54                                   
REMARK 500    PHE A 327     -149.68    -98.81                                   
REMARK 500    GLU A 334      106.29    -42.87                                   
REMARK 500    CYS A 343       83.54     55.05                                   
REMARK 500    LYS B  14      -87.60   -173.83                                   
REMARK 500    GLU B  17       -6.45   -157.80                                   
REMARK 500    LEU B  18      100.79    -55.52                                   
REMARK 500    HIS B  23       29.95    174.16                                   
REMARK 500    ILE B  25     -106.27   -108.37                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     107 RAMACHANDRAN OUTLIERS.                        
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 A 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 171   OD1                                                    
REMARK 620 2 ATP A 400   O2A 100.3                                              
REMARK 620 3 ASP A 184   OD2  71.5 101.3                                        
REMARK 620 4 ATP A 400   O3G 125.6 112.9  60.9                                  
REMARK 620 N                    1     2     3                                   
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 ATP A 400   O3G                                                    
REMARK 620 2 ATP A 400   O2B  85.6                                              
REMARK 620 3 ASP A 184   OD1 122.2  76.0                                        
REMARK 620 4 ASP A 184   OD2  71.2  84.9  53.2                                  
REMARK 620 5 ATP A 400   O2G  56.9  75.1 151.1 125.0                            
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 ATP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QCS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RIA:C HOLOENZYME OF CAMP-DEPENDENT              
REMARK 900 PROTEIN KINASE                                                       
DBREF  4DIN A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4DIN B   -1   379  UNP    P31321   KAP1_HUMAN       1    381             
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 SER 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 B  381  MET ALA SER PRO PRO ALA CYS PRO SER GLU GLU ASP GLU          
SEQRES   2 B  381  SER LEU LYS GLY CYS GLU LEU TYR VAL GLN LEU HIS GLY          
SEQRES   3 B  381  ILE GLN GLN VAL LEU LYS ASP CYS ILE VAL HIS LEU CYS          
SEQRES   4 B  381  ILE SER LYS PRO GLU ARG PRO MET LYS PHE LEU ARG GLU          
SEQRES   5 B  381  HIS PHE GLU LYS LEU GLU LYS GLU GLU ASN ARG GLN ILE          
SEQRES   6 B  381  LEU ALA ARG GLN LYS SER ASN SER GLN SER ASP SER HIS          
SEQRES   7 B  381  ASP GLU GLU VAL SER PRO THR PRO PRO ASN PRO VAL VAL          
SEQRES   8 B  381  LYS ALA ARG ARG ARG ARG GLY GLY VAL SER ALA GLU VAL          
SEQRES   9 B  381  TYR THR GLU GLU ASP ALA VAL SER TYR VAL ARG LYS VAL          
SEQRES  10 B  381  ILE PRO LYS ASP TYR LYS THR MET THR ALA LEU ALA LYS          
SEQRES  11 B  381  ALA ILE SER LYS ASN VAL LEU PHE ALA HIS LEU ASP ASP          
SEQRES  12 B  381  ASN GLU ARG SER ASP ILE PHE ASP ALA MET PHE PRO VAL          
SEQRES  13 B  381  THR HIS ILE ALA GLY GLU THR VAL ILE GLN GLN GLY ASN          
SEQRES  14 B  381  GLU GLY ASP ASN PHE TYR VAL VAL ASP GLN GLY GLU VAL          
SEQRES  15 B  381  ASP VAL TYR VAL ASN GLY GLU TRP VAL THR ASN ILE SER          
SEQRES  16 B  381  GLU GLY GLY SER PHE GLY GLU LEU ALA LEU ILE TYR GLY          
SEQRES  17 B  381  THR PRO ARG ALA ALA THR VAL LYS ALA LYS THR ASP LEU          
SEQRES  18 B  381  LYS LEU TRP GLY ILE ASP ARG ASP SER TYR ARG ARG ILE          
SEQRES  19 B  381  LEU MET GLY SER THR LEU ARG LYS ARG LYS MET TYR GLU          
SEQRES  20 B  381  GLU PHE LEU SER LYS VAL SER ILE LEU GLU SER LEU GLU          
SEQRES  21 B  381  LYS TRP GLU ARG LEU THR VAL ALA ASP ALA LEU GLU PRO          
SEQRES  22 B  381  VAL GLN PHE GLU ASP GLY GLU LYS ILE VAL VAL GLN GLY          
SEQRES  23 B  381  GLU PRO GLY ASP ASP PHE TYR ILE ILE THR GLU GLY THR          
SEQRES  24 B  381  ALA SER VAL LEU GLN ARG ARG SER PRO ASN GLU GLU TYR          
SEQRES  25 B  381  VAL GLU VAL GLY ARG LEU GLY PRO SER ASP TYR PHE GLY          
SEQRES  26 B  381  GLU ILE ALA LEU LEU LEU ASN ARG PRO ARG ALA ALA THR          
SEQRES  27 B  381  VAL VAL ALA ARG GLY PRO LEU LYS CYS VAL LYS LEU ASP          
SEQRES  28 B  381  ARG PRO ARG PHE GLU ARG VAL LEU GLY PRO CYS SER GLU          
SEQRES  29 B  381  ILE LEU LYS ARG ASN ILE GLN ARG TYR ASN SER PHE ILE          
SEQRES  30 B  381  SER LEU THR VAL                                              
MODRES 4DIN TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 4DIN SEP A  338  SER  PHOSPHOSERINE                                      
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    ATP  A 400      31                                                       
HET     MG  A 401       1                                                       
HET     MG  A 402       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  ATP    C10 H16 N5 O13 P3                                            
FORMUL   4   MG    2(MG 2+)                                                     
HELIX    1   1 GLU A   13  THR A   32  1                                  20    
HELIX    2   2 LYS A   76  VAL A   80  1                                   5    
HELIX    3   3 GLN A   84  GLN A   96  1                                  13    
HELIX    4   4 GLU A  127  ILE A  135  1                                   9    
HELIX    5   5 SER A  139  LEU A  160  1                                  22    
HELIX    6   6 LYS A  168  GLU A  170  5                                   3    
HELIX    7   7 ALA A  206  LEU A  211  1                                   6    
HELIX    8   8 LYS A  217  GLY A  234  1                                  18    
HELIX    9   9 GLN A  242  VAL A  251  1                                  10    
HELIX   10  10 SER A  262  LEU A  273  1                                  12    
HELIX   11  11 ASP A  276  ARG A  280  5                                   5    
HELIX   12  12 VAL A  288  ASN A  293  1                                   6    
HELIX   13  13 HIS A  294  ALA A  298  5                                   5    
HELIX   14  14 ASP A  301  GLN A  307  1                                   7    
HELIX   15  15 GLY A  344  THR A  348  5                                   5    
HELIX   16  16 THR B  104  SER B  110  1                                   7    
HELIX   17  17 ASP B  119  SER B  131  1                                  13    
HELIX   18  18 ASP B  140  MET B  151  1                                  12    
HELIX   19  19 GLY B  199  ILE B  204  5                                   6    
HELIX   20  20 ARG B  226  VAL B  251  1                                  26    
HELIX   21  21 TRP B  260  ASP B  267  1                                   8    
HELIX   22  22 ILE B  325  LEU B  329  5                                   5    
HELIX   23  23 ARG B  350  GLY B  358  1                                   9    
HELIX   24  24 PRO B  359  ARG B  366  1                                   8    
HELIX   25  25 ASN B  367  SER B  376  1                                  10    
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 TYR A  69  ASP A  75 -1  O  ILE A  73   N  ARG A  56           
SHEET    4   A 5 ASN A 115  GLU A 121 -1  O  MET A 120   N  ALA A  70           
SHEET    5   A 5 PHE A 110  LYS A 111 -1  N  PHE A 110   O  TYR A 117           
SHEET    1   B 2 LEU A 172  LEU A 173  0                                        
SHEET    2   B 2 GLN A 181  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
SHEET    1   C 3 PHE B 152  THR B 155  0                                        
SHEET    2   C 3 LYS B 220  ASP B 225 -1  O  GLY B 223   N  PHE B 152           
SHEET    3   C 3 ASN B 171  VAL B 174 -1  N  VAL B 174   O  TRP B 222           
SHEET    1   D 3 GLU B 187  SER B 193  0                                        
SHEET    2   D 3 GLU B 179  VAL B 184 -1  N  VAL B 182   O  THR B 190           
SHEET    3   D 3 THR B 212  ALA B 215 -1  O  LYS B 214   N  ASP B 181           
SHEET    1   E 3 TYR B 321  PHE B 322  0                                        
SHEET    2   E 3 ASP B 289  GLU B 295 -1  N  TYR B 291   O  PHE B 322           
SHEET    3   E 3 LYS B 344  ASP B 349 -1  O  LEU B 348   N  PHE B 290           
SHEET    1   F 3 GLU B 312  LEU B 316  0                                        
SHEET    2   F 3 ALA B 298  LEU B 301 -1  N  VAL B 300   O  GLY B 314           
SHEET    3   F 3 THR B 336  ALA B 339 -1  O  VAL B 338   N  SER B 299           
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         OD1 ASN A 171                MG    MG A 401     1555   1555  1.98  
LINK         O3G ATP A 400                MG    MG A 402     1555   1555  2.10  
LINK         O2B ATP A 400                MG    MG A 402     1555   1555  2.22  
LINK         O2A ATP A 400                MG    MG A 401     1555   1555  2.22  
LINK         OD1 ASP A 184                MG    MG A 402     1555   1555  2.25  
LINK         OD2 ASP A 184                MG    MG A 401     1555   1555  2.58  
LINK         OD2 ASP A 184                MG    MG A 402     1555   1555  2.60  
LINK         O3G ATP A 400                MG    MG A 401     1555   1555  2.85  
LINK         O2G ATP A 400                MG    MG A 402     1555   1555  2.90  
SITE     1 AC1 26 LEU A  49  GLY A  50  THR A  51  GLY A  52                    
SITE     2 AC1 26 SER A  53  PHE A  54  VAL A  57  ALA A  70                    
SITE     3 AC1 26 LYS A  72  MET A 120  GLU A 121  VAL A 123                    
SITE     4 AC1 26 GLU A 127  ASP A 166  LYS A 168  GLU A 170                    
SITE     5 AC1 26 ASN A 171  LEU A 173  THR A 183  ASP A 184                    
SITE     6 AC1 26 PHE A 327   MG A 401   MG A 402  ARG B  94                    
SITE     7 AC1 26 GLY B  96  GLY B  97                                          
SITE     1 AC2  4 LYS A 168  ASN A 171  ASP A 184  ATP A 400                    
SITE     1 AC3  3 ASP A 166  ASP A 184  ATP A 400                               
CRYST1  172.194  172.194  146.646  90.00  90.00 120.00 P 64 2 2     12          
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      0.005807  0.003353  0.000000        0.00000                         
SCALE2      0.000000  0.006706  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006819        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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