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Database: PDB
Entry: 4R3C
LinkDB: 4R3C
Original site: 4R3C 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       14-AUG-14   4R3C              
TITLE     CRYSTAL STRUCTURE OF P38 ALPHA MAP KINASE IN COMPLEX WITH A NOVEL     
TITLE    2 ISOFORM SELECTIVE DRUG CANDIDATE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAP KINASE 14, MAPK 14, CYTOKINE SUPPRESSIVE ANTI-          
COMPND   5 INFLAMMATORY DRUG-BINDING PROTEIN, CSAID-BINDING PROTEIN, CSBP, MAP  
COMPND   6 KINASE MXI2, MAX-INTERACTING PROTEIN 2, MITOGEN-ACTIVATED PROTEIN    
COMPND   7 KINASE P38 ALPHA, MAP KINASE P38 ALPHA, STRESS-ACTIVATED PROTEIN     
COMPND   8 KINASE 2A, SAPK2A;                                                   
COMPND   9 EC: 2.7.11.24;                                                       
COMPND  10 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, CSPB1, MXI2, SAPK2A;               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    SERINE/THREONINE-PROTEIN KINASE, PROTEIN KINASE DOMAIN, TRANSFERASE,  
KEYWDS   2 ATP BINDING, PHOSPHORYLATION, CYTOSOL, TRANSFERASE-TRANSFERASE       
KEYWDS   3 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.L.GRUM-TOKARS,G.MINASOV,S.M.ROY,W.F.ANDERSON,D.M.WATTERSON          
REVDAT   3   22-NOV-17 4R3C    1       REMARK                                   
REVDAT   2   01-JUL-15 4R3C    1       JRNL                                     
REVDAT   1   25-FEB-15 4R3C    0                                                
JRNL        AUTH   S.M.ROY,V.L.GRUM-TOKARS,J.P.SCHAVOCKY,F.SAEED,               
JRNL        AUTH 2 A.STANISZEWSKI,A.F.TEICH,O.ARANCIO,A.D.BACHSTETTER,          
JRNL        AUTH 3 S.J.WEBSTER,L.J.VAN ELDIK,G.MINASOV,W.F.ANDERSON,            
JRNL        AUTH 4 J.C.PELLETIER,D.M.WATTERSON                                  
JRNL        TITL   TARGETING HUMAN CENTRAL NERVOUS SYSTEM PROTEIN KINASES: AN   
JRNL        TITL 2 ISOFORM SELECTIVE P38 ALPHA MAPK INHIBITOR THAT ATTENUATES   
JRNL        TITL 3 DISEASE PROGRESSION IN ALZHEIMER'S DISEASE MOUSE MODELS.     
JRNL        REF    ACS CHEM NEUROSCI             V.   6   666 2015              
JRNL        REFN                   ESSN 1948-7193                               
JRNL        PMID   25676389                                                     
JRNL        DOI    10.1021/ACSCHEMNEURO.5B00002                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.06 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 23018                          
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 + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1241                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.06                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.11                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1541                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.67                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2720                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 77                                      
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.46000                                             
REMARK   3    B22 (A**2) : -1.49000                                             
REMARK   3    B33 (A**2) : 2.95000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.196         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.166         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.436         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2992 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2833 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4080 ; 1.397 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6512 ; 0.708 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   357 ; 2.618 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   141 ;30.021 ;24.184       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   507 ; 9.888 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;12.783 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   441 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3398 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   709 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1404 ; 2.301 ; 2.907       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1403 ; 2.302 ; 2.905       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1769 ; 3.437 ; 4.344       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1770 ; 3.436 ; 4.346       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1588 ; 2.953 ; 3.323       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1589 ; 2.952 ; 3.324       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2312 ; 4.674 ; 4.844       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3532 ; 7.046 ;24.661       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3498 ; 7.020 ;24.483       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A    53                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.2569  74.0330  21.2532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0919 T22:   0.0748                                     
REMARK   3      T33:   0.1413 T12:   0.0233                                     
REMARK   3      T13:   0.0729 T23:   0.0790                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6703 L22:   5.5228                                     
REMARK   3      L33:   3.4709 L12:   0.7596                                     
REMARK   3      L13:  -0.3208 L23:  -1.5839                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0078 S12:  -0.2331 S13:   0.1784                       
REMARK   3      S21:   0.3770 S22:   0.2717 S23:   0.6783                       
REMARK   3      S31:  -0.3523 S32:  -0.1161 S33:  -0.2639                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    54        A    92                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.2244  80.3533  10.4699              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1041 T22:   0.0267                                     
REMARK   3      T33:   0.0427 T12:   0.0050                                     
REMARK   3      T13:  -0.0020 T23:  -0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4153 L22:   4.4999                                     
REMARK   3      L33:   2.5495 L12:  -1.3789                                     
REMARK   3      L13:  -0.2359 L23:  -2.2938                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2000 S12:   0.0404 S13:   0.0762                       
REMARK   3      S21:   0.1333 S22:  -0.0293 S23:   0.1294                       
REMARK   3      S31:  -0.2613 S32:  -0.0920 S33:  -0.1708                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    93        A   150                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.9484  73.0541  17.6559              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1294 T22:   0.0596                                     
REMARK   3      T33:   0.0172 T12:   0.0025                                     
REMARK   3      T13:   0.0035 T23:   0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2955 L22:   1.4059                                     
REMARK   3      L33:   1.0113 L12:   0.4487                                     
REMARK   3      L13:   0.1235 L23:  -0.6418                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0892 S12:  -0.1273 S13:  -0.0667                       
REMARK   3      S21:   0.0347 S22:  -0.0835 S23:   0.0811                       
REMARK   3      S31:   0.0595 S32:  -0.0111 S33:  -0.0057                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   151        A   189                          
REMARK   3    ORIGIN FOR THE GROUP (A):  73.9125  76.0438  21.9393              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1093 T22:   0.1275                                     
REMARK   3      T33:   0.0310 T12:  -0.0105                                     
REMARK   3      T13:   0.0268 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1066 L22:   7.4795                                     
REMARK   3      L33:   0.9907 L12:   2.9830                                     
REMARK   3      L13:   0.5595 L23:   1.2590                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0611 S12:  -0.3149 S13:   0.1605                       
REMARK   3      S21:   0.2906 S22:  -0.1964 S23:   0.3300                       
REMARK   3      S31:   0.1431 S32:   0.0014 S33:   0.1353                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   190        A   309                          
REMARK   3    ORIGIN FOR THE GROUP (A):  90.9184  82.3477  17.9495              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0473 T22:   0.1209                                     
REMARK   3      T33:   0.0762 T12:  -0.0103                                     
REMARK   3      T13:  -0.0218 T23:   0.0423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5377 L22:   3.1416                                     
REMARK   3      L33:   0.5229 L12:   0.5734                                     
REMARK   3      L13:  -0.2011 L23:   0.0633                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0566 S12:  -0.2080 S13:   0.0671                       
REMARK   3      S21:   0.1966 S22:  -0.0777 S23:  -0.3815                       
REMARK   3      S31:  -0.0142 S32:   0.1817 S33:   0.0211                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   310        A   352                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.9048  77.0799   3.7274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1518 T22:   0.0945                                     
REMARK   3      T33:   0.0174 T12:   0.0167                                     
REMARK   3      T13:  -0.0420 T23:  -0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9623 L22:   5.7101                                     
REMARK   3      L33:   1.6634 L12:  -2.6402                                     
REMARK   3      L13:   0.7886 L23:  -2.0790                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1265 S12:   0.4536 S13:  -0.0414                       
REMARK   3      S21:  -0.4061 S22:  -0.0530 S23:   0.1673                       
REMARK   3      S31:   0.1060 S32:  -0.1356 S33:  -0.0734                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4R3C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000086846.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : BERYLLIUM LENSES                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24314                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.1700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.59900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.370                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PDB ENTRY 4F9W               
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.075M AMMONIUM ACETATE, 0.1M BISTRIS    
REMARK 280  (PH 5.5), 16% PEG 10000, VAPOR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.92500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.90400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.25600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.90400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.92500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.25600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     GLY A   -13                                                      
REMARK 465     VAL A   -12                                                      
REMARK 465     ASP A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     ASN A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     GLY A   170                                                      
REMARK 465     LEU A   171                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     ARG A   173                                                      
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     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 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    LYS A  15       19.78     56.39                                   
REMARK 500    ARG A  57       55.25     37.33                                   
REMARK 500    ARG A 149      -14.57     81.10                                   
REMARK 500    LEU A 289       55.30    -93.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GG5 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3GF A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3GF A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 404                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4F9W   RELATED DB: PDB                                   
REMARK 900 P38 ALPHA MAPK IN COMPLEX WITH N,N-DIMETHYL-6-(NAPHTHALEN-2-YL)-5-   
REMARK 900 (PYRIDIN- 4-YL)PYRIDAZIN-3-AMINE                                     
REMARK 900 RELATED ID: 4F9Y   RELATED DB: PDB                                   
REMARK 900 P38 ALPHA MAPK IN COMPLEX WITH N,N-DIMETHYL-6-(NAPHTHALEN-1-YL)-5-   
REMARK 900 (PYRIDIN- 4-YL)PYRIDAZIN-3-AMINE                                     
REMARK 900 RELATED ID: 4EWQ   RELATED DB: PDB                                   
REMARK 900 P38 ALPHA MAPK IN COMPLEX WITH 3-PHENYL-4-(PYRIDIN-4-YL)-6-[4-       
REMARK 900 (PYRIMIDIN- 2-YL)PIPERAZIN-1-YL]PYRIDAZINE                           
DBREF  4R3C A    2   360  UNP    Q16539   MK14_HUMAN       2    360             
SEQADV 4R3C MET A  -22  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C HIS A  -21  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C HIS A  -20  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C HIS A  -19  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C HIS A  -18  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C HIS A  -17  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C HIS A  -16  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C SER A  -15  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C SER A  -14  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C GLY A  -13  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C VAL A  -12  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C ASP A  -11  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C LEU A  -10  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C GLY A   -9  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C THR A   -8  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C GLU A   -7  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C ASN A   -6  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C LEU A   -5  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C TYR A   -4  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C PHE A   -3  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C GLN A   -2  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C SER A   -1  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C ASN A    0  UNP  Q16539              EXPRESSION TAG                 
SEQADV 4R3C ALA A    1  UNP  Q16539              EXPRESSION TAG                 
SEQRES   1 A  383  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  383  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA SER GLN          
SEQRES   3 A  383  GLU ARG PRO THR PHE TYR ARG GLN GLU LEU ASN LYS THR          
SEQRES   4 A  383  ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN LEU SER PRO          
SEQRES   5 A  383  VAL GLY SER GLY ALA TYR GLY SER VAL CYS ALA ALA PHE          
SEQRES   6 A  383  ASP THR LYS THR GLY LEU ARG VAL ALA VAL LYS LYS LEU          
SEQRES   7 A  383  SER ARG PRO PHE GLN SER ILE ILE HIS ALA LYS ARG THR          
SEQRES   8 A  383  TYR ARG GLU LEU ARG LEU LEU LYS HIS MET LYS HIS GLU          
SEQRES   9 A  383  ASN VAL ILE GLY LEU LEU ASP VAL PHE THR PRO ALA ARG          
SEQRES  10 A  383  SER LEU GLU GLU PHE ASN ASP VAL TYR LEU VAL THR HIS          
SEQRES  11 A  383  LEU MET GLY ALA ASP LEU ASN ASN ILE VAL LYS CYS GLN          
SEQRES  12 A  383  LYS LEU THR ASP ASP HIS VAL GLN PHE LEU ILE TYR GLN          
SEQRES  13 A  383  ILE LEU ARG GLY LEU LYS TYR ILE HIS SER ALA ASP ILE          
SEQRES  14 A  383  ILE HIS ARG ASP LEU LYS PRO SER ASN LEU ALA VAL ASN          
SEQRES  15 A  383  GLU ASP CME GLU LEU LYS ILE LEU ASP PHE GLY LEU ALA          
SEQRES  16 A  383  ARG HIS THR ASP ASP GLU MET THR GLY TYR VAL ALA THR          
SEQRES  17 A  383  ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN TRP MET          
SEQRES  18 A  383  HIS TYR ASN GLN THR VAL ASP ILE TRP SER VAL GLY CYS          
SEQRES  19 A  383  ILE MET ALA GLU LEU LEU THR GLY ARG THR LEU PHE PRO          
SEQRES  20 A  383  GLY THR ASP HIS ILE ASP GLN LEU LYS LEU ILE LEU ARG          
SEQRES  21 A  383  LEU VAL GLY THR PRO GLY ALA GLU LEU LEU LYS LYS ILE          
SEQRES  22 A  383  SER SER GLU SER ALA ARG ASN TYR ILE GLN SER LEU THR          
SEQRES  23 A  383  GLN MET PRO LYS MET ASN PHE ALA ASN VAL PHE ILE GLY          
SEQRES  24 A  383  ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU LYS MET LEU          
SEQRES  25 A  383  VAL LEU ASP SER ASP LYS ARG ILE THR ALA ALA GLN ALA          
SEQRES  26 A  383  LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS ASP PRO ASP          
SEQRES  27 A  383  ASP GLU PRO VAL ALA ASP PRO TYR ASP GLN SER PHE GLU          
SEQRES  28 A  383  SER ARG ASP LEU LEU ILE ASP GLU TRP LYS SER LEU THR          
SEQRES  29 A  383  TYR ASP GLU VAL ILE SER PHE VAL PRO PRO PRO LEU ASP          
SEQRES  30 A  383  GLN GLU GLU MET GLU SER                                      
MODRES 4R3C CME A  162  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
HET    CME  A 162      10                                                       
HET    GG5  A 401      18                                                       
HET    3GF  A 402      29                                                       
HET    3GF  A 403      29                                                       
HET     CL  A 404       2                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     GG5 4-[3-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL]PYRIDINE                   
HETNAM     3GF 6-(4-METHYLPIPERAZIN-1-YL)-3-(NAPHTHALEN-2-YL)-4-                
HETNAM   2 3GF  (PYRIDIN-4-YL)PYRIDAZINE                                        
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  GG5    C14 H10 F N3                                                 
FORMUL   3  3GF    2(C24 H23 N5)                                                
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  HOH   *146(H2 O)                                                    
HELIX    1   1 SER A   61  MET A   78  1                                  18    
HELIX    2   2 SER A   95  PHE A   99  5                                   5    
HELIX    3   3 LEU A  113  GLN A  120  1                                   8    
HELIX    4   4 THR A  123  ALA A  144  1                                  22    
HELIX    5   5 LYS A  152  SER A  154  5                                   3    
HELIX    6   6 ALA A  184  ARG A  189  5                                   6    
HELIX    7   7 ALA A  190  LEU A  195  1                                   6    
HELIX    8   8 THR A  203  GLY A  219  1                                  17    
HELIX    9   9 ASP A  227  GLY A  240  1                                  14    
HELIX   10  10 GLY A  243  LYS A  248  1                                   6    
HELIX   11  11 SER A  252  LEU A  262  1                                  11    
HELIX   12  12 ASN A  269  PHE A  274  1                                   6    
HELIX   13  13 ASN A  278  LEU A  289  1                                  12    
HELIX   14  14 ASP A  292  ARG A  296  5                                   5    
HELIX   15  15 THR A  298  ALA A  304  1                                   7    
HELIX   16  16 HIS A  305  ALA A  309  5                                   5    
HELIX   17  17 ASP A  313  GLU A  317  5                                   5    
HELIX   18  18 GLN A  325  ARG A  330  5                                   6    
HELIX   19  19 LEU A  333  PHE A  348  1                                  16    
SHEET    1   A 2 PHE A   8  GLU A  12  0                                        
SHEET    2   A 2 ILE A  17  PRO A  21 -1  O  TRP A  18   N  GLN A  11           
SHEET    1   B 5 TYR A  24  SER A  32  0                                        
SHEET    2   B 5 GLY A  36  ASP A  43 -1  O  ALA A  40   N  SER A  28           
SHEET    3   B 5 LEU A  48  LEU A  55 -1  O  VAL A  52   N  CYS A  39           
SHEET    4   B 5 TYR A 103  HIS A 107 -1  O  THR A 106   N  ALA A  51           
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           
LINK         C   ASP A 161                 N   CME A 162     1555   1555  1.34  
LINK         C   CME A 162                 N   GLU A 163     1555   1555  1.33  
SITE     1 AC1 11 PRO A 191  GLU A 192  LEU A 195  TRP A 197                    
SITE     2 AC1 11 PRO A 242  LEU A 246  LYS A 249  ILE A 250                    
SITE     3 AC1 11 ILE A 259  LEU A 291  SER A 293                               
SITE     1 AC2 11 ALA A  51  LYS A  53  LEU A 104  VAL A 105                    
SITE     2 AC2 11 THR A 106  HIS A 107  MET A 109  SER A 154                    
SITE     3 AC2 11 LEU A 167  ASP A 168  HOH A 599                               
SITE     1 AC3  8 GLU A  22  ARG A  23  THR A  44  ILE A 229                    
SITE     2 AC3  8 SER A 254  TYR A 258  ASP A 283  HOH A 571                    
SITE     1 AC4  3 GLY A  31  SER A  32  GLY A  33                               
CRYST1   65.850   74.512   77.808  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015186  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013421  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012852        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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