GenomeNet

Database: PDB
Entry: 3L9L
LinkDB: 3L9L
Original site: 3L9L 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       05-JAN-10   3L9L              
TITLE     CRYSTAL STRUCTURE OF PKA WITH COMPOUND 36                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A, B;                                                         
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: C, D;                                                         
COMPND  10 FRAGMENT: SEQUENCE DATABASE RESIDUES 6-25;                           
COMPND  11 SYNONYM: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, MUSCLE/BRAIN       
COMPND  12 ISOFORM, PKI-ALPHA;                                                  
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: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: PKIA, PRKACN1;                                                 
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PKB, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.HUANG                                                               
REVDAT   2   16-NOV-11 3L9L    1       VERSN  HETATM                            
REVDAT   1   19-JAN-11 3L9L    0                                                
JRNL        AUTH   Q.ZENG,J.G.ALLEN,M.P.BOURBEAU,X.WANG,G.YAO,S.TADESSE,        
JRNL        AUTH 2 J.T.RIDER,C.C.YUAN,F.T.HONG,M.R.LEE,S.ZHANG,J.A.LOFGREN,     
JRNL        AUTH 3 D.J.FREEMAN,S.YANG,C.LI,E.TOMINEY,X.HUANG,D.HOFFMAN,         
JRNL        AUTH 4 H.K.YAMANE,C.FOTSCH,C.DOMINGUEZ,R.HUNGATE,X.ZHANG            
JRNL        TITL   AZOLE-BASED INHIBITORS OF AKT/PKB FOR THE TREATMENT OF       
JRNL        TITL 2 CANCER.                                                      
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  20  1559 2010              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   20137943                                                     
JRNL        DOI    10.1016/J.BMCL.2010.01.067                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 50774                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2580                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5851                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 753                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3L9L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB057005.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E DW                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58036                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 2.450                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.530                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1ATP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M LICL, 20-30% PEG6K, PH 8.0,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       59.01950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.21200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       59.01950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       57.21200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 1840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 548  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 623  LIES ON A SPECIAL POSITION.                          
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     ASP C    24                                                      
REMARK 465     MET B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     HIS D    23                                                      
REMARK 465     ASP D    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     GLU A  11    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  12    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  13    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 279    CG   CD   CE   NZ                                   
REMARK 470     ARG A 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  12    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  13    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  16    CG   CD   CE   NZ                                   
REMARK 470     GLU B  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  28    CG   CD   CE   NZ                                   
REMARK 470     GLU B 333    CG   CD   OE1  OE2                                  
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    HOH B   474     O    HOH B   610              2.16            
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    PRO B 321   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  38     -177.53   -170.61                                   
REMARK 500    ASN A  99      107.12   -162.50                                   
REMARK 500    ASP A 166       41.29   -152.22                                   
REMARK 500    ASP A 184       98.79     67.14                                   
REMARK 500    PRO A 202      -60.55    -29.04                                   
REMARK 500    ASP A 276       89.29    -68.07                                   
REMARK 500    LEU A 277        7.39    -60.16                                   
REMARK 500    PRO B  33      178.70    -56.41                                   
REMARK 500    ASN B  36       79.11     34.10                                   
REMARK 500    ASN B  99      117.46   -160.23                                   
REMARK 500    ASP B 112     -165.07   -129.78                                   
REMARK 500    ASP B 166       38.98   -149.51                                   
REMARK 500    LYS B 168      155.57    179.08                                   
REMARK 500    ASP B 184       93.91     70.23                                   
REMARK 500    ASN B 216     -159.27   -130.45                                   
REMARK 500    LEU B 273       48.85    -86.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 777        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH A 992        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH B 370        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH B 701        DISTANCE =  5.28 ANGSTROMS                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     HOH B  370                                                       
REMARK 615     HOH B  534                                                       
REMARK 615     HOH B  714                                                       
REMARK 615     HOH B  883                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE L9L A 351                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE L9L B 351                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3L9M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PKAB3 WITH COMPOUND 18                          
REMARK 900 RELATED ID: 3L9N   RELATED DB: PDB                                   
DBREF  3L9L A    0   350  UNP    P17612   KAPCA_HUMAN      1    351             
DBREF  3L9L C    5    24  UNP    P61925   IPKA_HUMAN       6     25             
DBREF  3L9L B    0   350  UNP    P17612   KAPCA_HUMAN      1    351             
DBREF  3L9L D    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 C   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 C   20  ARG ARG ASN ALA ILE HIS ASP                                  
SEQRES   1 B  351  MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN          
SEQRES   2 B  351  GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP          
SEQRES   3 B  351  PHE LEU LYS LYS TRP GLU SER PRO ALA GLN ASN THR ALA          
SEQRES   4 B  351  HIS LEU ASP GLN PHE GLU ARG ILE LYS THR LEU GLY THR          
SEQRES   5 B  351  GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU          
SEQRES   6 B  351  THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN          
SEQRES   7 B  351  LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN          
SEQRES   8 B  351  GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU          
SEQRES   9 B  351  VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU          
SEQRES  10 B  351  TYR MET VAL MET GLU TYR VAL PRO GLY GLY GLU MET PHE          
SEQRES  11 B  351  SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS          
SEQRES  12 B  351  ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU          
SEQRES  13 B  351  TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS          
SEQRES  14 B  351  PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN          
SEQRES  15 B  351  VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG          
SEQRES  16 B  351  THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO          
SEQRES  17 B  351  GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP          
SEQRES  18 B  351  TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA          
SEQRES  19 B  351  GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE          
SEQRES  20 B  351  TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER          
SEQRES  21 B  351  HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU          
SEQRES  22 B  351  LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS          
SEQRES  23 B  351  ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA          
SEQRES  24 B  351  THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU          
SEQRES  25 B  351  ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR          
SEQRES  26 B  351  SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL          
SEQRES  27 B  351  SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE SER GLU PHE          
SEQRES   1 D   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 D   20  ARG ARG ASN ALA ILE HIS ASP                                  
MODRES 3L9L TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 3L9L SEP A  338  SER  PHOSPHOSERINE                                      
MODRES 3L9L TPO B  197  THR  PHOSPHOTHREONINE                                   
MODRES 3L9L SEP B  338  SER  PHOSPHOSERINE                                      
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    TPO  B 197      11                                                       
HET    SEP  B 338      10                                                       
HET    L9L  A 351      30                                                       
HET    L9L  B 351      30                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     L9L 5-[2-({(2S)-2-AMINO-3-[4-(TRIFLUOROMETHYL)                       
HETNAM   2 L9L  PHENYL]PROPYL}AMINO)-1,3-THIAZOL-5-YL]-1,3-DIHYDRO-2H-          
HETNAM   3 L9L  INDOL-2-ONE                                                     
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   5  L9L    2(C21 H19 F3 N4 O S)                                         
FORMUL   7  HOH   *753(H2 O)                                                    
HELIX    1   1 GLU A   11  SER A   32  1                                  22    
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  VAL A   98  1                                  15    
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 GLY A  344  SER A  348  5                                   5    
HELIX   17  17 THR C    5  ALA C   12  1                                   8    
HELIX   18  18 GLN B   12  SER B   32  1                                  21    
HELIX   19  19 HIS B   39  ASP B   41  5                                   3    
HELIX   20  20 LYS B   76  LEU B   82  1                                   7    
HELIX   21  21 GLN B   84  GLN B   96  1                                  13    
HELIX   22  22 GLU B  127  GLY B  136  1                                  10    
HELIX   23  23 SER B  139  LEU B  160  1                                  22    
HELIX   24  24 LYS B  168  GLU B  170  5                                   3    
HELIX   25  25 THR B  201  LEU B  205  5                                   5    
HELIX   26  26 ALA B  206  LEU B  211  1                                   6    
HELIX   27  27 LYS B  217  GLY B  234  1                                  18    
HELIX   28  28 GLN B  242  GLY B  253  1                                  12    
HELIX   29  29 SER B  262  LEU B  273  1                                  12    
HELIX   30  30 VAL B  288  ASN B  293  1                                   6    
HELIX   31  31 HIS B  294  ALA B  298  5                                   5    
HELIX   32  32 ASP B  301  GLN B  307  1                                   7    
HELIX   33  33 GLY B  344  SER B  348  5                                   5    
HELIX   34  34 THR D    5  ALA D   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  LEU A  59   N  LYS A  47           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  MET A  71   N  MET A  58           
SHEET    4   A 5 ASN A 115  GLU A 121 -1  O  MET A 120   N  ALA A  70           
SHEET    5   A 5 LEU A 106  LYS A 111 -1  N  PHE A 108   O  VAL A 119           
SHEET    1   B 2 LEU A 162  ILE A 163  0                                        
SHEET    2   B 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1   C 2 LEU A 172  ILE A 174  0                                        
SHEET    2   C 2 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
SHEET    1   D 5 PHE B  43  GLY B  52  0                                        
SHEET    2   D 5 GLY B  55  HIS B  62 -1  O  LEU B  59   N  LYS B  47           
SHEET    3   D 5 HIS B  68  ASP B  75 -1  O  MET B  71   N  MET B  58           
SHEET    4   D 5 ASN B 115  GLU B 121 -1  O  MET B 120   N  ALA B  70           
SHEET    5   D 5 LEU B 106  LYS B 111 -1  N  PHE B 110   O  TYR B 117           
SHEET    1   E 2 LEU B 162  ILE B 163  0                                        
SHEET    2   E 2 LYS B 189  ARG B 190 -1  O  LYS B 189   N  ILE B 163           
SHEET    1   F 2 LEU B 172  ILE B 174  0                                        
SHEET    2   F 2 ILE B 180  VAL B 182 -1  O  GLN B 181   N  LEU B 173           
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.32  
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  1.34  
LINK         C   TRP B 196                 N   TPO B 197     1555   1555  1.33  
LINK         C   TPO B 197                 N   LEU B 198     1555   1555  1.32  
LINK         C   VAL B 337                 N   SEP B 338     1555   1555  1.33  
LINK         C   SEP B 338                 N   ILE B 339     1555   1555  1.34  
SITE     1 AC1 16 LEU A  49  PHE A  54  ALA A  70  LYS A  72                    
SITE     2 AC1 16 GLU A 121  TYR A 122  VAL A 123  GLU A 127                    
SITE     3 AC1 16 GLU A 170  ASN A 171  LEU A 173  ASP A 184                    
SITE     4 AC1 16 PHE A 327  HOH A 392  HOH A 445  HOH A 474                    
SITE     1 AC2 19 LEU B  49  GLY B  50  PHE B  54  ALA B  70                    
SITE     2 AC2 19 LYS B  72  MET B 120  GLU B 121  TYR B 122                    
SITE     3 AC2 19 VAL B 123  GLU B 127  GLU B 170  ASN B 171                    
SITE     4 AC2 19 LEU B 173  THR B 183  ASP B 184  PHE B 327                    
SITE     5 AC2 19 HOH B 365  HOH B 389  HOH B 528                               
CRYST1  118.039  114.424   71.807  90.00 125.79  90.00 C 1 2 1       8          
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      0.008472  0.000000  0.006107        0.00000                         
SCALE2      0.000000  0.008739  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017167        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system