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Database: PDB
Entry: 3POO
LinkDB: 3POO
Original site: 3POO 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       23-NOV-10   3POO              
TITLE     HUMAN CAMP-DEPENDENT PROTEIN KINASE IN COMPLEX WITH AN INHIBITOR      
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: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 6-25;                                         
COMPND  11 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,         
COMPND  12 MUSCLE/BRAIN ISOFORM;                                                
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PKACA, PRKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES                                                       
KEYWDS    ATP BINDING, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE INHIBITOR       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.KOESTER,A.HEINE,G.KLEBE                                             
REVDAT   1   16-NOV-11 3POO    0                                                
JRNL        AUTH   H.KOESTER,T.CRAAN,A.HEINE,G.KLEBE                            
JRNL        TITL   FRAGMENT BASED DRUG DESIGN ON PKA                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 54627                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2744                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 26.8936 -  3.4449    0.93     5407   289  0.1793 0.2006        
REMARK   3     2  3.4449 -  2.7352    0.98     5486   302  0.1907 0.2130        
REMARK   3     3  2.7352 -  2.3897    0.97     5408   290  0.1869 0.2242        
REMARK   3     4  2.3897 -  2.1713    0.97     5373   287  0.1747 0.1910        
REMARK   3     5  2.1713 -  2.0157    0.98     5391   279  0.1773 0.2076        
REMARK   3     6  2.0157 -  1.8969    0.96     5299   242  0.1781 0.2297        
REMARK   3     7  1.8969 -  1.8019    0.92     5010   291  0.1882 0.2243        
REMARK   3     8  1.8019 -  1.7235    0.91     4992   281  0.2047 0.2114        
REMARK   3     9  1.7235 -  1.6572    0.89     4801   255  0.2205 0.2741        
REMARK   3    10  1.6572 -  1.6000    0.86     4716   228  0.2530 0.2880        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 43.48                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.730           
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) : 3.61240                                              
REMARK   3    B22 (A**2) : -0.82660                                             
REMARK   3    B33 (A**2) : -2.78580                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           2956                                  
REMARK   3   ANGLE     :  0.993           4010                                  
REMARK   3   CHIRALITY :  0.069            430                                  
REMARK   3   PLANARITY :  0.005            510                                  
REMARK   3   DIHEDRAL  : 12.343           1072                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 14:72)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  35.3001  14.4495   4.9984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0032 T22:   0.1539                                     
REMARK   3      T33:   0.1411 T12:  -0.0226                                     
REMARK   3      T13:  -0.0384 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1776 L22:   0.9163                                     
REMARK   3      L33:   0.8382 L12:   0.2925                                     
REMARK   3      L13:  -0.1651 L23:   0.7225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0153 S12:   0.0546 S13:   0.0535                       
REMARK   3      S21:   0.0380 S22:   0.0648 S23:  -0.3407                       
REMARK   3      S31:  -0.0166 S32:   0.3193 S33:  -0.0241                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain A and resid 73:251)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  24.7530   1.6442   3.2476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0533 T22:   0.0492                                     
REMARK   3      T33:   0.0495 T12:   0.0126                                     
REMARK   3      T13:   0.0117 T23:   0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6629 L22:   1.3997                                     
REMARK   3      L33:   1.6286 L12:   0.3757                                     
REMARK   3      L13:  -0.0543 L23:   0.7609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0511 S12:  -0.0161 S13:  -0.0333                       
REMARK   3      S21:   0.1362 S22:  -0.0183 S23:  -0.1343                       
REMARK   3      S31:   0.2539 S32:   0.0681 S33:   0.0592                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain A and resid 252:350)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3887  -3.6551   0.7170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2152 T22:   0.1459                                     
REMARK   3      T33:   0.1673 T12:   0.0395                                     
REMARK   3      T13:   0.0246 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7749 L22:   1.6998                                     
REMARK   3      L33:   2.1081 L12:   0.3281                                     
REMARK   3      L13:  -0.0236 L23:   0.7286                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0627 S12:   0.0443 S13:  -0.1422                       
REMARK   3      S21:   0.1429 S22:   0.0439 S23:  -0.1584                       
REMARK   3      S31:   0.4558 S32:   0.1386 S33:   0.0235                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain B and resid 1005:1022)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9817  -1.9426 -10.4903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2410 T22:   0.1932                                     
REMARK   3      T33:   0.1558 T12:  -0.0448                                     
REMARK   3      T13:   0.0351 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0668 L22:   0.4596                                     
REMARK   3      L33:   0.0986 L12:  -0.0952                                     
REMARK   3      L13:   0.0363 L23:  -0.1595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0126 S12:  -0.0252 S13:  -0.0242                       
REMARK   3      S21:  -0.0082 S22:  -0.1226 S23:  -0.0359                       
REMARK   3      S31:   0.0889 S32:  -0.0502 S33:   0.1143                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3POO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062631.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR KMC   
REMARK 200                                   -2                                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57573                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1OEW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5MM MES, 5MM BISTRIS-PROPANE, 75MM       
REMARK 280  LICL, 1ML DTT, 0.1MM EDTA EQUILIBRATED AGAINST WATER/ETHANOL, PH    
REMARK 280  6.9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K, TEMPERATURE   
REMARK 280  289K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.43500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.85000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.47000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.85000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.43500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.47000            
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: 2070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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     MET A     0                                                      
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     LYS A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     GLY A   322                                                      
REMARK 465     ASP B    24                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS 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     LYS A  28    CG   CD   CE   NZ                                   
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 217    CG   CD   CE   NZ                                   
REMARK 470     ILE A 244    CG1  CG2  CD1                                       
REMARK 470     GLN A 245    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 285    CG   CD   CE   NZ                                   
REMARK 470     LYS A 295    CG   CD   CE   NZ                                   
REMARK 470     LYS A 309    CG   CD   CE   NZ                                   
REMARK 470     GLU A 311    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     PHE A 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 334    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  99      105.22   -160.34                                   
REMARK 500    ASP A 166       42.06   -148.80                                   
REMARK 500    ASP A 184       86.58     59.44                                   
REMARK 500    LEU A 273       49.92    -87.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S69 A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BUD A 3001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3NX8   RELATED DB: PDB                                   
REMARK 900 HUMAN CAMP DEPENDENT PROTEIN KINASE IN COMPLEX WITH PHENOL           
REMARK 900 RELATED ID: 3OOG   RELATED DB: PDB                                   
REMARK 900 HUMAN CAMP-DEPENDENT PROTEIN KINASE IN COMPLEX WITH A SMALL          
REMARK 900 FRAGMENT                                                             
REMARK 900 RELATED ID: 3OVV   RELATED DB: PDB                                   
REMARK 900 HUMAN CAMP DEPENDENT PROTEIN KINASE IN COMPLEX WITH AN               
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 3OXT   RELATED DB: PDB                                   
REMARK 900 HUMAN CAMP DEPENDENT PROTEIN KINASE IN COMPLEX WITH AN               
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 3OWP   RELATED DB: PDB                                   
REMARK 900 HUMAN CAMP DEPENDENT PROTEIN KINASE IN COMPLEX WITH AN               
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 3P0M   RELATED DB: PDB                                   
REMARK 900 HUMAN CAMP DEPENDENT PROTEIN KINASE IN COMPLEX WITH AN               
REMARK 900 INHIBITOR                                                            
DBREF  3POO A    0   350  UNP    P17612   KAPCA_HUMAN      1    351             
DBREF  3POO B    5    24  UNP    P61925   IPKA_HUMAN       6     25             
SEQRES   1 A  351  MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN          
SEQRES   2 A  351  GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP          
SEQRES   3 A  351  PHE LEU LYS LYS TRP GLU SER PRO ALA GLN ASN THR ALA          
SEQRES   4 A  351  HIS LEU ASP GLN PHE GLU ARG ILE LYS THR LEU GLY THR          
SEQRES   5 A  351  GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU          
SEQRES   6 A  351  THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN          
SEQRES   7 A  351  LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN          
SEQRES   8 A  351  GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU          
SEQRES   9 A  351  VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU          
SEQRES  10 A  351  TYR MET VAL MET GLU TYR VAL PRO GLY GLY GLU MET PHE          
SEQRES  11 A  351  SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS          
SEQRES  12 A  351  ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU          
SEQRES  13 A  351  TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS          
SEQRES  14 A  351  PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN          
SEQRES  15 A  351  VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG          
SEQRES  16 A  351  THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO          
SEQRES  17 A  351  GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP          
SEQRES  18 A  351  TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA          
SEQRES  19 A  351  GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE          
SEQRES  20 A  351  TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER          
SEQRES  21 A  351  HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU          
SEQRES  22 A  351  LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS          
SEQRES  23 A  351  ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA          
SEQRES  24 A  351  THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU          
SEQRES  25 A  351  ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR          
SEQRES  26 A  351  SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL          
SEQRES  27 A  351  SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE SER GLU PHE          
SEQRES   1 B   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 B   20  ARG ARG ASN ALA ILE HIS ASP                                  
MODRES 3POO TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 3POO SEP A  338  SER  PHOSPHOSERINE                                      
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    S69  A2001      23                                                       
HET    BUD  A3001       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     S69 N'-[(E)-(2,4-DIHYDROXY-6-METHYLPHENYL)METHYLIDENE]-2-            
HETNAM   2 S69  (3-METHOXYPHENYL)ACETOHYDRAZIDE                                 
HETNAM     BUD (2S,3S)-BUTANE-2,3-DIOL                                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  S69    C17 H18 N2 O4                                                
FORMUL   4  BUD    C4 H10 O2                                                    
FORMUL   5  HOH   *248(H2 O)                                                    
HELIX    1   1 SER A   14  SER A   32  1                                  19    
HELIX    2   2 HIS 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 SER 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 B    5  ALA B   12  1                                   8    
SHEET    1   A 5 PHE A  43  GLY A  52  0                                        
SHEET    2   A 5 GLY A  55  HIS A  62 -1  O  VAL A  57   N  LEU A  49           
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 120   N  ALA A  70           
SHEET    5   A 5 LEU A 106  LYS A 111 -1  N  PHE A 110   O  TYR A 117           
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   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  
SITE     1 AC1 16 GLY A  52  SER A  53  PHE A  54  GLY A  55                    
SITE     2 AC1 16 VAL A  57  ALA A  70  LYS A  72  MET A 120                    
SITE     3 AC1 16 GLU A 121  TYR A 122  VAL A 123  LEU A 173                    
SITE     4 AC1 16 THR A 183  ASP A 184  HOH A5112  HOH A5122                    
SITE     1 AC2  6 THR A  51  GLY A  52  HOH A5127  HOH A5146                    
SITE     2 AC2  6 ARG B  19  ASN B  20                                          
CRYST1   72.870   74.940   79.700  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      0.013723  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013344  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012547        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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