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Database: PDB
Entry: 2OKR
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HEADER    TRANSFERASE                             17-JAN-07   2OKR              
TITLE     CRYSTAL STRUCTURE OF THE P38A-MAPKAP KINASE 2 HETERODIMER             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;                       
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA, MAP             
COMPND   5 KINASE P38 ALPHA, CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY             
COMPND   6 DRUG-BINDING PROTEIN, CSAID-BINDING PROTEIN, CSBP, MAX-              
COMPND   7 INTERACTING PROTEIN 2, MAP KINASE MXI2, SAPK2A;                      
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: MAP KINASE-ACTIVATED PROTEIN KINASE 2;                     
COMPND  12 CHAIN: C, F;                                                         
COMPND  13 FRAGMENT: RESIDUES 370-393;                                          
COMPND  14 SYNONYM: MAPK-ACTIVATED PROTEIN KINASE 2, MAPKAP KINASE 2,           
COMPND  15 MAPKAPK-2, MK2;                                                      
COMPND  16 EC: 2.7.11.1;                                                        
COMPND  17 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: MAPK14, CSBP, CSBP1, CSBP2, MXI2;                              
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 EXPRESSION_SYSTEM_PLASMID: PVL1392;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HOMO                
SOURCE  14 SAPIENS (HUMANS)                                                     
KEYWDS    KINASE, NLS, NES, HETERODIMER, DOCKING GROOVE, TRANSFERASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.TER HAAR                                                            
REVDAT   4   24-FEB-09 2OKR    1       VERSN                                    
REVDAT   3   24-APR-07 2OKR    1       JRNL                                     
REVDAT   2   20-FEB-07 2OKR    1       JRNL                                     
REVDAT   1   06-FEB-07 2OKR    0                                                
JRNL        AUTH   E.TER HAAR,P.PRABAKHAR,X.LIU,C.LEPRE                         
JRNL        TITL   CRYSTAL STRUCTURE OF THE P38ALPHA-MAPKAP KINASE 2            
JRNL        TITL 2 HETERODIMER.                                                 
JRNL        REF    J.BIOL.CHEM.                  V. 282  9733 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17255097                                                     
JRNL        DOI    10.1074/JBC.M611165200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : AUTOBUSTER                                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.48                           
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)   (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 60104                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2981                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.12                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.38                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2371                       
REMARK   3   BIN FREE R VALUE                    : 0.2644                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 468                          
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            : 5792                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 197                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.89618                                              
REMARK   3    B22 (A**2) : 4.89618                                              
REMARK   3    B33 (A**2) : -9.79236                                             
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) : 0.29                            
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.19                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
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  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 2OKR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041258.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60104                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.780                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.060                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.48                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1LEZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 250 MM SODIUM              
REMARK 280  FORMATE, PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
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                                                                      
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       40.45333            
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       80.90667            
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: 1740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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: 1790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F                                  
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    -5                                                      
REMARK 465     SER A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     GLU A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     HIS A   174                                                      
REMARK 465     THR A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     ASP A   177                                                      
REMARK 465     GLU A   178                                                      
REMARK 465     MET A   179                                                      
REMARK 465     THR A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     TYR A   182                                                      
REMARK 465     VAL A   183                                                      
REMARK 465     LEU A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     GLN A   355                                                      
REMARK 465     GLU A   356                                                      
REMARK 465     GLU A   357                                                      
REMARK 465     MET A   358                                                      
REMARK 465     GLU A   359                                                      
REMARK 465     SER A   360                                                      
REMARK 465     GLY D    -5                                                      
REMARK 465     SER D    -4                                                      
REMARK 465     HIS D    -3                                                      
REMARK 465     MET D    -2                                                      
REMARK 465     LEU D    -1                                                      
REMARK 465     GLU D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     GLU D     4                                                      
REMARK 465     HIS D   174                                                      
REMARK 465     THR D   175                                                      
REMARK 465     ASP D   176                                                      
REMARK 465     ASP D   177                                                      
REMARK 465     GLU D   178                                                      
REMARK 465     MET D   179                                                      
REMARK 465     THR D   180                                                      
REMARK 465     GLY D   181                                                      
REMARK 465     TYR D   182                                                      
REMARK 465     VAL D   183                                                      
REMARK 465     ALA D   184                                                      
REMARK 465     THR D   185                                                      
REMARK 465     GLU D   356                                                      
REMARK 465     GLU D   357                                                      
REMARK 465     MET D   358                                                      
REMARK 465     GLU D   359                                                      
REMARK 465     SER D   360                                                      
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   4    CG   CD   OE1  OE2                                  
REMARK 470     SER A  32    CB   OG                                             
REMARK 470     ALA A  34    CB                                                  
REMARK 470     TYR A  35    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR A 185    OG1  CG2                                            
REMARK 470     HIS A 199    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ALA A 244    CB                                                  
REMARK 470     LYS C1389    CG   CD   CE   NZ                                   
REMARK 470     ARG C1391    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ALA C1392    CB                                                  
REMARK 470     LEU C1393    CB   CG   CD1  CD2                                  
REMARK 470     LYS D  15    CB   CG   CD   CE   NZ                              
REMARK 470     TYR D  35    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR D  35    OH                                                  
REMARK 470     HIS D 199    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ALA D 244    CB                                                  
REMARK 470     LEU D 353    CB   CG   CD1  CD2                                  
REMARK 470     ASP D 354    CG   OD1  OD2                                       
REMARK 470     GLN D 355    CB   CG   CD   OE1  NE2                             
REMARK 470     ARG F1391    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU F1393    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE2  GLN A   264     O    HOH D   365     1565     0.83            
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    ARG A 189   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    LYS D  15   N   -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    THR D  16   N   -  CA  -  CB  ANGL. DEV. = -37.7 DEGREES          
REMARK 500    THR D  16   N   -  CA  -  C   ANGL. DEV. =  24.5 DEGREES          
REMARK 500    ILE D  84   CG1 -  CB  -  CG2 ANGL. DEV. =  17.2 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    ASN A 100      -29.55   -146.85                                   
REMARK 500    ARG A 149      -16.23     95.04                                   
REMARK 500    THR A 203        0.60    -66.22                                   
REMARK 500    LEU A 289       49.73    -93.11                                   
REMARK 500    ASP A 316       46.44   -140.96                                   
REMARK 500    ALA C1390       -1.95    -59.85                                   
REMARK 500    ASN D  14     -136.58     65.51                                   
REMARK 500    THR D  16      -70.11   -128.85                                   
REMARK 500    ASN D 100      -41.88   -143.62                                   
REMARK 500    ARG D 149      -16.59     79.74                                   
REMARK 500    LEU D 289       56.67    -93.84                                   
REMARK 500    ASP D 316       45.27   -140.51                                   
REMARK 500    LEU D 353       98.28    -65.62                                   
REMARK 500    LYS F1388        8.30    -64.75                                   
REMARK 500    ALA F1392       45.92    -75.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN D   14     LYS D   15                  115.16                    
REMARK 500 LYS D   15     THR D   16                  -46.17                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ONL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE P38A-MAPKAP KINASE 2 HETERODIMER            
DBREF  2OKR A    2   360  UNP    Q16539   MK14_HUMAN       1    359             
DBREF  2OKR D    2   360  UNP    Q16539   MK14_HUMAN       1    359             
DBREF  2OKR C 1370  1393  UNP    P49137   MAPK2_HUMAN    370    393             
DBREF  2OKR F 1370  1393  UNP    P49137   MAPK2_HUMAN    370    393             
SEQADV 2OKR GLY A   -5  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR SER A   -4  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR HIS A   -3  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR MET A   -2  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR LEU A   -1  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR GLU A    0  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR MET A    1  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR GLY D   -5  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR SER D   -4  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR HIS D   -3  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR MET D   -2  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR LEU D   -1  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR GLU D    0  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2OKR MET D    1  UNP  Q16539              CLONING ARTIFACT               
SEQRES   1 A  366  GLY SER HIS MET LEU GLU MET SER GLN GLU ARG PRO THR          
SEQRES   2 A  366  PHE TYR ARG GLN GLU LEU ASN LYS THR ILE TRP GLU VAL          
SEQRES   3 A  366  PRO GLU ARG TYR GLN ASN LEU SER PRO VAL GLY SER GLY          
SEQRES   4 A  366  ALA TYR GLY SER VAL CYS ALA ALA PHE ASP THR LYS THR          
SEQRES   5 A  366  GLY LEU ARG VAL ALA VAL LYS LYS LEU SER ARG PRO PHE          
SEQRES   6 A  366  GLN SER ILE ILE HIS ALA LYS ARG THR TYR ARG GLU LEU          
SEQRES   7 A  366  ARG LEU LEU LYS HIS MET LYS HIS GLU ASN VAL ILE GLY          
SEQRES   8 A  366  LEU LEU ASP VAL PHE THR PRO ALA ARG SER LEU GLU GLU          
SEQRES   9 A  366  PHE ASN ASP VAL TYR LEU VAL THR HIS LEU MET GLY ALA          
SEQRES  10 A  366  ASP LEU ASN ASN ILE VAL LYS CYS GLN LYS LEU THR ASP          
SEQRES  11 A  366  ASP HIS VAL GLN PHE LEU ILE TYR GLN ILE LEU ARG GLY          
SEQRES  12 A  366  LEU LYS TYR ILE HIS SER ALA ASP ILE ILE HIS ARG ASP          
SEQRES  13 A  366  LEU LYS PRO SER ASN LEU ALA VAL ASN GLU ASP CYS GLU          
SEQRES  14 A  366  LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG HIS THR ASP          
SEQRES  15 A  366  ASP GLU MET THR GLY TYR VAL ALA THR ARG TRP TYR ARG          
SEQRES  16 A  366  ALA PRO GLU ILE MET LEU ASN TRP MET HIS TYR ASN GLN          
SEQRES  17 A  366  THR VAL ASP ILE TRP SER VAL GLY CYS ILE MET ALA GLU          
SEQRES  18 A  366  LEU LEU THR GLY ARG THR LEU PHE PRO GLY THR ASP HIS          
SEQRES  19 A  366  ILE ASP GLN LEU LYS LEU ILE LEU ARG LEU VAL GLY THR          
SEQRES  20 A  366  PRO GLY ALA GLU LEU LEU LYS LYS ILE SER SER GLU SER          
SEQRES  21 A  366  ALA ARG ASN TYR ILE GLN SER LEU THR GLN MET PRO LYS          
SEQRES  22 A  366  MET ASN PHE ALA ASN VAL PHE ILE GLY ALA ASN PRO LEU          
SEQRES  23 A  366  ALA VAL ASP LEU LEU GLU LYS MET LEU VAL LEU ASP SER          
SEQRES  24 A  366  ASP LYS ARG ILE THR ALA ALA GLN ALA LEU ALA HIS ALA          
SEQRES  25 A  366  TYR PHE ALA GLN TYR HIS ASP PRO ASP ASP GLU PRO VAL          
SEQRES  26 A  366  ALA ASP PRO TYR ASP GLN SER PHE GLU SER ARG ASP LEU          
SEQRES  27 A  366  LEU ILE ASP GLU TRP LYS SER LEU THR TYR ASP GLU VAL          
SEQRES  28 A  366  ILE SER PHE VAL PRO PRO PRO LEU ASP GLN GLU GLU MET          
SEQRES  29 A  366  GLU SER                                                      
SEQRES   1 C   24  ILE LYS ILE LYS LYS ILE GLU ASP ALA SER ASN PRO LEU          
SEQRES   2 C   24  LEU LEU LYS ARG ARG LYS LYS ALA ARG ALA LEU                  
SEQRES   1 D  366  GLY SER HIS MET LEU GLU MET SER GLN GLU ARG PRO THR          
SEQRES   2 D  366  PHE TYR ARG GLN GLU LEU ASN LYS THR ILE TRP GLU VAL          
SEQRES   3 D  366  PRO GLU ARG TYR GLN ASN LEU SER PRO VAL GLY SER GLY          
SEQRES   4 D  366  ALA TYR GLY SER VAL CYS ALA ALA PHE ASP THR LYS THR          
SEQRES   5 D  366  GLY LEU ARG VAL ALA VAL LYS LYS LEU SER ARG PRO PHE          
SEQRES   6 D  366  GLN SER ILE ILE HIS ALA LYS ARG THR TYR ARG GLU LEU          
SEQRES   7 D  366  ARG LEU LEU LYS HIS MET LYS HIS GLU ASN VAL ILE GLY          
SEQRES   8 D  366  LEU LEU ASP VAL PHE THR PRO ALA ARG SER LEU GLU GLU          
SEQRES   9 D  366  PHE ASN ASP VAL TYR LEU VAL THR HIS LEU MET GLY ALA          
SEQRES  10 D  366  ASP LEU ASN ASN ILE VAL LYS CYS GLN LYS LEU THR ASP          
SEQRES  11 D  366  ASP HIS VAL GLN PHE LEU ILE TYR GLN ILE LEU ARG GLY          
SEQRES  12 D  366  LEU LYS TYR ILE HIS SER ALA ASP ILE ILE HIS ARG ASP          
SEQRES  13 D  366  LEU LYS PRO SER ASN LEU ALA VAL ASN GLU ASP CYS GLU          
SEQRES  14 D  366  LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG HIS THR ASP          
SEQRES  15 D  366  ASP GLU MET THR GLY TYR VAL ALA THR ARG TRP TYR ARG          
SEQRES  16 D  366  ALA PRO GLU ILE MET LEU ASN TRP MET HIS TYR ASN GLN          
SEQRES  17 D  366  THR VAL ASP ILE TRP SER VAL GLY CYS ILE MET ALA GLU          
SEQRES  18 D  366  LEU LEU THR GLY ARG THR LEU PHE PRO GLY THR ASP HIS          
SEQRES  19 D  366  ILE ASP GLN LEU LYS LEU ILE LEU ARG LEU VAL GLY THR          
SEQRES  20 D  366  PRO GLY ALA GLU LEU LEU LYS LYS ILE SER SER GLU SER          
SEQRES  21 D  366  ALA ARG ASN TYR ILE GLN SER LEU THR GLN MET PRO LYS          
SEQRES  22 D  366  MET ASN PHE ALA ASN VAL PHE ILE GLY ALA ASN PRO LEU          
SEQRES  23 D  366  ALA VAL ASP LEU LEU GLU LYS MET LEU VAL LEU ASP SER          
SEQRES  24 D  366  ASP LYS ARG ILE THR ALA ALA GLN ALA LEU ALA HIS ALA          
SEQRES  25 D  366  TYR PHE ALA GLN TYR HIS ASP PRO ASP ASP GLU PRO VAL          
SEQRES  26 D  366  ALA ASP PRO TYR ASP GLN SER PHE GLU SER ARG ASP LEU          
SEQRES  27 D  366  LEU ILE ASP GLU TRP LYS SER LEU THR TYR ASP GLU VAL          
SEQRES  28 D  366  ILE SER PHE VAL PRO PRO PRO LEU ASP GLN GLU GLU MET          
SEQRES  29 D  366  GLU SER                                                      
SEQRES   1 F   24  ILE LYS ILE LYS LYS ILE GLU ASP ALA SER ASN PRO LEU          
SEQRES   2 F   24  LEU LEU LYS ARG ARG LYS LYS ALA ARG ALA LEU                  
FORMUL   5  HOH   *197(H2 O)                                                    
HELIX    1   1 SER A   61  MET A   78  1                                  18    
HELIX    2   2 LEU A  113  LYS A  118  1                                   6    
HELIX    3   3 THR A  123  ALA A  144  1                                  22    
HELIX    4   4 LYS A  152  SER A  154  5                                   3    
HELIX    5   5 ALA A  184  ARG A  189  5                                   6    
HELIX    6   6 ALA A  190  LEU A  195  1                                   6    
HELIX    7   7 GLN A  202  GLY A  219  1                                  18    
HELIX    8   8 ASP A  227  GLY A  240  1                                  14    
HELIX    9   9 GLY A  243  ILE A  250  1                                   8    
HELIX   10  10 SER A  252  SER A  261  1                                  10    
HELIX   11  11 ASN A  269  PHE A  274  1                                   6    
HELIX   12  12 ASN A  278  LEU A  289  1                                  12    
HELIX   13  13 ASP A  292  ARG A  296  5                                   5    
HELIX   14  14 THR A  298  ALA A  304  1                                   7    
HELIX   15  15 HIS A  305  ALA A  309  5                                   5    
HELIX   16  16 GLN A  325  ARG A  330  5                                   6    
HELIX   17  17 LEU A  333  PHE A  348  1                                  16    
HELIX   18  18 ASN C 1380  ALA C 1390  1                                  11    
HELIX   19  19 SER D   61  MET D   78  1                                  18    
HELIX   20  20 LEU D  113  CYS D  119  1                                   7    
HELIX   21  21 THR D  123  ALA D  144  1                                  22    
HELIX   22  22 LYS D  152  SER D  154  5                                   3    
HELIX   23  23 ALA D  190  LEU D  195  1                                   6    
HELIX   24  24 THR D  203  GLY D  219  1                                  17    
HELIX   25  25 ASP D  227  GLY D  240  1                                  14    
HELIX   26  26 GLY D  243  ILE D  250  1                                   8    
HELIX   27  27 SER D  252  LEU D  262  1                                  11    
HELIX   28  28 ASN D  269  PHE D  274  1                                   6    
HELIX   29  29 ASN D  278  LEU D  289  1                                  12    
HELIX   30  30 ASP D  292  ARG D  296  5                                   5    
HELIX   31  31 THR D  298  ALA D  304  1                                   7    
HELIX   32  32 HIS D  305  ALA D  309  5                                   5    
HELIX   33  33 GLN D  325  ARG D  330  5                                   6    
HELIX   34  34 LEU D  333  SER D  347  1                                  15    
HELIX   35  35 ASN F 1380  ARG F 1391  1                                  12    
SHEET    1   A 2 PHE A   8  LEU A  13  0                                        
SHEET    2   A 2 THR A  16  PRO A  21 -1  O  TRP A  18   N  GLN A  11           
SHEET    1   B 5 TYR A  24  GLY A  31  0                                        
SHEET    2   B 5 SER A  37  ASP A  43 -1  O  PHE A  42   N  GLN A  25           
SHEET    3   B 5 LEU A  48  LEU A  55 -1  O  LEU A  48   N  ASP A  43           
SHEET    4   B 5 VAL A 102  HIS A 107 -1  O  VAL A 102   N  LEU A  55           
SHEET    5   B 5 ASP A  88  PHE A  90 -1  N  ASP A  88   O  VAL A 105           
SHEET    1   C 3 ALA A 111  ASP A 112  0                                        
SHEET    2   C 3 LEU A 156  VAL A 158 -1  O  VAL A 158   N  ALA A 111           
SHEET    3   C 3 LEU A 164  ILE A 166 -1  O  LYS A 165   N  ALA A 157           
SHEET    1   D 2 PHE D   8  GLU D  12  0                                        
SHEET    2   D 2 ILE D  17  PRO D  21 -1  O  TRP D  18   N  GLN D  11           
SHEET    1   E 5 TYR D  24  GLY D  31  0                                        
SHEET    2   E 5 SER D  37  ASP D  43 -1  O  ALA D  40   N  SER D  28           
SHEET    3   E 5 LEU D  48  LEU D  55 -1  O  LYS D  54   N  SER D  37           
SHEET    4   E 5 VAL D 102  HIS D 107 -1  O  THR D 106   N  ALA D  51           
SHEET    5   E 5 ASP D  88  PHE D  90 -1  N  ASP D  88   O  VAL D 105           
SHEET    1   F 3 ALA D 111  ASP D 112  0                                        
SHEET    2   F 3 LEU D 156  VAL D 158 -1  O  VAL D 158   N  ALA D 111           
SHEET    3   F 3 LEU D 164  ILE D 166 -1  O  LYS D 165   N  ALA D 157           
CRYST1   81.550   81.550  121.360  90.00  90.00 120.00 P 31          6          
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      0.012262  0.007080  0.000000        0.00000                         
SCALE2      0.000000  0.014159  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008240        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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