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Database: PDB
Entry: 2YIX
LinkDB: 2YIX
Original site: 2YIX 
HEADER    TRANSFERASE                             17-MAY-11   2YIX              
TITLE     TRIAZOLOPYRIDINE INHIBITORS OF P38                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 4-354;                                            
COMPND   5 SYNONYM: P38 KINASE, MAP KINASE 14, MAPK 14, CYTOKINE SUPPRESSIVE    
COMPND   6  ANTI-INFLAMMATORY DRUG-BINDING PROTEIN, CSAID-BINDING PROTEIN,      
COMPND   7  CSBP, MAP KINASE MXI2, MAX-INTERACTING PROTEIN 2,                   
COMPND   8  MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA, MAP KINASE P38 ALPHA,   
COMPND   9  SAPK2A;                                                             
COMPND  10 EC: 2.7.11.24;                                                       
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PHOSPHORYLATION, SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.S.MILLAN,M.ANDERSON,M.E.BUNNAGE,J.L.BURROWS,K.J.BUTCHER,P.G.DODD,   
AUTHOR   2 T.J.EVANS,D.A.FAIRMAN,S.HAN,S.J.HUGHES,S.L.IRVING,I.C.KILTY,         
AUTHOR   3 A.LEMAITRE,R.A.LEWTHAWAITE,A.MAHKE,E.MARR,J.P.MATHIAS,J.PHILIP,      
AUTHOR   4 C.PHILLIPS,R.T.SMITH,M.H.STEFANIAK,M.YEADON                          
REVDAT   1   30-NOV-11 2YIX    0                                                
JRNL        AUTH   D.S.MILLAN,M.E.BUNNAGE,J.L.BURROWS,K.J.BUTCHER,P.G.DODD,     
JRNL        AUTH 2 T.J.EVANS,D.A.FAIRMAN,S.J.HUGHES,I.C.KILTY,A.LEMAITRE,       
JRNL        AUTH 3 R.A.LEWTHWAITE,A.MAHNKE,J.P.MATHIAS,J.PHILIP,R.T.SMITH,      
JRNL        AUTH 4 M.H.STEFANIAK,M.YEADON,C.PHILLIPS                            
JRNL        TITL   DESIGN AND SYNTHESIS OF INHALED P38 INHIBITORS FOR THE       
JRNL        TITL 2 TREATMENT OF CHRONIC OBSTRUCTIVE PULMONARY DISEASE.          
JRNL        REF    J.MED.CHEM.                   V.  54  7797 2011              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   21888439                                                     
JRNL        DOI    10.1021/JM200677B                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.6                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.75                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.40                          
REMARK   3   NUMBER OF REFLECTIONS             : 21609                          
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)  : 0.1959                         
REMARK   3   R VALUE            (WORKING SET)  : 0.1932                         
REMARK   3   FREE R VALUE                      : 0.2472                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.12                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 1106                           
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               : 11                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.41                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.40                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2671                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2474                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2527                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2450                   
REMARK   3   BIN FREE R VALUE                        : 0.2899                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.39                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 144                      
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            : 2834                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 273                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.05                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.8458                                               
REMARK   3    B22 (A**2) : 3.3912                                               
REMARK   3    B33 (A**2) : -8.2370                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.284               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.295               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.226               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.264               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.219               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.9332                        
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.9018                        
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2926   ; 2.00   ; HARMONIC            
REMARK   3    BOND ANGLES               : 3974   ; 2.00   ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1012   ; 2.00   ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 81     ; 2.00   ; HARMONIC            
REMARK   3    GENERAL PLANES            : 421    ; 5.00   ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2926   ; 20.00  ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.00   ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 377    ; 5.00   ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3414   ; 4.00   ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.13                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.97                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.56                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2YIX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAY-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-48323.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21609                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.30                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 2.8                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       22.97200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.29000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.26150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.29000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.97200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.26150            
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN A   201     OG1  THR A   203              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP A 354   C     ASP A 354   O       2.274                       
REMARK 500    ASP A 354   C     ASP A 354   OXT     1.571                       
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    ASP A 354   CA  -  C   -  O   ANGL. DEV. = -19.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  57       55.24     39.49                                   
REMARK 500    ASN A 100      -42.18   -140.61                                   
REMARK 500    ASN A 115       14.36    -66.69                                   
REMARK 500    ILE A 116      -54.88   -129.02                                   
REMARK 500    VAL A 117       75.97   -115.39                                   
REMARK 500    CYS A 119       -2.69     57.86                                   
REMARK 500    ARG A 149      -12.91     74.29                                   
REMARK 500    LEU A 289       56.42    -91.72                                   
REMARK 500    PRO A 314        0.63    -65.45                                   
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 YIX A1355                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2BAJ   RELATED DB: PDB                                   
REMARK 900  P38ALPHA BOUND TO PYRAZOLOUREA                                      
REMARK 900 RELATED ID: 1WFC   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF APO, UNPHOSPHORYLATED, P38 MITOGEN                     
REMARK 900  ACTIVATEDPROTEIN KINASE P38 (P38 MAP KINASE) THE                    
REMARK 900  MAMMALIAN HOMOLOGUEOF THE YEAST HOG1 PROTEIN                        
REMARK 900 RELATED ID: 1W7H   RELATED DB: PDB                                   
REMARK 900  P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH SMALL                  
REMARK 900  MOLECULE INHIBITOR                                                  
REMARK 900 RELATED ID: 1WBO   RELATED DB: PDB                                   
REMARK 900  FRAGMENT BASED P38 INHIBITORS                                       
REMARK 900 RELATED ID: 1KV2   RELATED DB: PDB                                   
REMARK 900  HUMAN P38 MAP KINASE IN COMPLEX WITH BIRB 796                       
REMARK 900 RELATED ID: 1BMK   RELATED DB: PDB                                   
REMARK 900  THE COMPLEX STRUCTURE OF THE MAP KINASE P38/SB218655                
REMARK 900 RELATED ID: 1YQJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF P38 ALPHA IN COMPLEX WITH A                    
REMARK 900  SELECTIVEPYRIDAZINE INHIBITOR                                       
REMARK 900 RELATED ID: 1BL7   RELATED DB: PDB                                   
REMARK 900  THE COMPLEX STRUCTURE OF THE MAP KINASE P38/SB220025                
REMARK 900 RELATED ID: 1ZYJ   RELATED DB: PDB                                   
REMARK 900  HUMAN P38 MAP KINASE IN COMPLEX WITH INHIBITOR 1A                   
REMARK 900 RELATED ID: 1A9U   RELATED DB: PDB                                   
REMARK 900  THE COMPLEX STRUCTURE OF THE MAP KINASE P38/SB203580                
REMARK 900 RELATED ID: 1WBT   RELATED DB: PDB                                   
REMARK 900  IDENTIFICATION OF NOVEL P38 ALPHA MAP KINASE INHIBITORS             
REMARK 900   USING FRAGMENT-BASED LEAD GENERATION.                              
REMARK 900 RELATED ID: 2I0H   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF P38ALPHA IN COMPLEX WITH                           
REMARK 900  ANARYLPYRIDAZINONE                                                  
REMARK 900 RELATED ID: 2BAQ   RELATED DB: PDB                                   
REMARK 900  P38ALPHA BOUND TO RO3201195                                         
REMARK 900 RELATED ID: 1WBV   RELATED DB: PDB                                   
REMARK 900  IDENTIFICATION OF NOVEL P38 ALPHA MAP KINASE INHIBITORS             
REMARK 900   USING FRAGMENT-BASED LEAD GENERATION.                              
REMARK 900 RELATED ID: 1ZZ2   RELATED DB: PDB                                   
REMARK 900  TWO CLASSES OF P38ALPHA MAP KINASE INHIBITORS HAVING                
REMARK 900  ACOMMON DIPHENYLETHER CORE BUT EXHIBITING DIVERGENT                 
REMARK 900  BINDINGMODES                                                        
REMARK 900 RELATED ID: 1DI9   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF P38 MITOGEN-ACTIVATED PROTEIN KINASE               
REMARK 900  INCOMPLEX WITH 4-[3-METHYLSULFANYLANILINO]-6,7-                     
REMARK 900  DIMETHOXYQUINAZOLINE                                                
REMARK 900 RELATED ID: 1W83   RELATED DB: PDB                                   
REMARK 900  P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH SMALL                  
REMARK 900  MOLECULE INHIBITOR                                                  
REMARK 900 RELATED ID: 1BL6   RELATED DB: PDB                                   
REMARK 900  THE COMPLEX STRUCTURE OF THE MAP KINASE P38/SB216995                
REMARK 900 RELATED ID: 1M7Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF P38 MAP KINASE IN COMPLEX WITH                 
REMARK 900  ADIHYDROQUINAZOLINONE INHIBITOR                                     
REMARK 900 RELATED ID: 1IAN   RELATED DB: PDB                                   
REMARK 900  HUMAN P38 MAP KINASE INHIBITOR COMPLEX                              
REMARK 900 RELATED ID: 1OZ1   RELATED DB: PDB                                   
REMARK 900  P38 MITOGEN-ACTIVATED KINASE IN COMPLEX WITH 4-                     
REMARK 900  AZAINDOLEINHIBITOR                                                  
REMARK 900 RELATED ID: 1WBN   RELATED DB: PDB                                   
REMARK 900  FRAGMENT BASED P38 INHIBITORS                                       
REMARK 900 RELATED ID: 2BAK   RELATED DB: PDB                                   
REMARK 900  P38ALPHA MAP KINASE BOUND TO MPAQ                                   
REMARK 900 RELATED ID: 2BAL   RELATED DB: PDB                                   
REMARK 900  P38ALPHA MAP KINASE BOUND TO PYRAZOLOAMINE                          
REMARK 900 RELATED ID: 1WBS   RELATED DB: PDB                                   
REMARK 900  IDENTIFICATION OF NOVEL P38 ALPHA MAP KINASE INHIBITORS             
REMARK 900   USING FRAGMENT-BASED LEAD GENERATION.                              
REMARK 900 RELATED ID: 1OUY   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF P38 ALPHA IN COMPLEX WITH A                        
REMARK 900  DIHYDROPYRIDO-PYRIMIDINE INHIBITOR                                  
REMARK 900 RELATED ID: 1OUK   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF P38 ALPHA IN COMPLEX WITH                          
REMARK 900  APYRIDINYLIMIDAZOLE INHIBITOR                                       
REMARK 900 RELATED ID: 2Y8O   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN P38ALPHA COMPLEXED WITH A                
REMARK 900  MAPK DOCKING PEPTIDE                                                
REMARK 900 RELATED ID: 2YIS   RELATED DB: PDB                                   
REMARK 900  TRIAZOLOPYRIDINE INHIBITORS OF P38 KINASE.                          
REMARK 900 RELATED ID: 1R39   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF P38ALPHA                                           
REMARK 900 RELATED ID: 1KV1   RELATED DB: PDB                                   
REMARK 900  P38 MAP KINASE IN COMPLEX WITH INHIBITOR 1                          
REMARK 900 RELATED ID: 1WBW   RELATED DB: PDB                                   
REMARK 900  IDENTIFICATION OF NOVEL P38 ALPHA MAP KINASE INHIBITORS             
REMARK 900   USING FRAGMENT-BASED LEAD GENERATION.                              
REMARK 900 RELATED ID: 1W82   RELATED DB: PDB                                   
REMARK 900  P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH SMALL                  
REMARK 900  MOLECULE INHIBITOR                                                  
REMARK 900 RELATED ID: 1R3C   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF P38ALPHA C162S MUTANT                              
REMARK 900 RELATED ID: 1OVE   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF P38 ALPHA IN COMPLEX WITH                          
REMARK 900  ADIHYDROQUINOLINONE                                                 
REMARK 900 RELATED ID: 1ZZL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF P38 WITH TRIAZOLOPYRIDINE                      
REMARK 900 RELATED ID: 1W84   RELATED DB: PDB                                   
REMARK 900  P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH SMALL                  
REMARK 900  MOLECULE INHIBITOR                                                  
REMARK 900 RELATED ID: 2YIW   RELATED DB: PDB                                   
REMARK 900  TRIAZOLOPYRIDINE INHIBITORS OF P38 KINASE                           
DBREF  2YIX A    4   354  UNP    Q16539   MK14_HUMAN       4    354             
SEQRES   1 A  351  GLU ARG PRO THR PHE TYR ARG GLN GLU LEU ASN LYS THR          
SEQRES   2 A  351  ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN LEU SER PRO          
SEQRES   3 A  351  VAL GLY SER GLY ALA TYR GLY SER VAL CYS ALA ALA PHE          
SEQRES   4 A  351  ASP THR LYS THR GLY LEU ARG VAL ALA VAL LYS LYS LEU          
SEQRES   5 A  351  SER ARG PRO PHE GLN SER ILE ILE HIS ALA LYS ARG THR          
SEQRES   6 A  351  TYR ARG GLU LEU ARG LEU LEU LYS HIS MET LYS HIS GLU          
SEQRES   7 A  351  ASN VAL ILE GLY LEU LEU ASP VAL PHE THR PRO ALA ARG          
SEQRES   8 A  351  SER LEU GLU GLU PHE ASN ASP VAL TYR LEU VAL THR HIS          
SEQRES   9 A  351  LEU MET GLY ALA ASP LEU ASN ASN ILE VAL LYS CYS GLN          
SEQRES  10 A  351  LYS LEU THR ASP ASP HIS VAL GLN PHE LEU ILE TYR GLN          
SEQRES  11 A  351  ILE LEU ARG GLY LEU LYS TYR ILE HIS SER ALA ASP ILE          
SEQRES  12 A  351  ILE HIS ARG ASP LEU LYS PRO SER ASN LEU ALA VAL ASN          
SEQRES  13 A  351  GLU ASP CYS GLU LEU LYS ILE LEU ASP PHE GLY LEU ALA          
SEQRES  14 A  351  ARG HIS THR ASP ASP GLU MET THR GLY TYR VAL ALA THR          
SEQRES  15 A  351  ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN TRP MET          
SEQRES  16 A  351  HIS TYR ASN GLN THR VAL ASP ILE TRP SER VAL GLY CYS          
SEQRES  17 A  351  ILE MET ALA GLU LEU LEU THR GLY ARG THR LEU PHE PRO          
SEQRES  18 A  351  GLY THR ASP HIS ILE ASP GLN LEU LYS LEU ILE LEU ARG          
SEQRES  19 A  351  LEU VAL GLY THR PRO GLY ALA GLU LEU LEU LYS LYS ILE          
SEQRES  20 A  351  SER SER GLU SER ALA ARG ASN TYR ILE GLN SER LEU THR          
SEQRES  21 A  351  GLN MET PRO LYS MET ASN PHE ALA ASN VAL PHE ILE GLY          
SEQRES  22 A  351  ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU LYS MET LEU          
SEQRES  23 A  351  VAL LEU ASP SER ASP LYS ARG ILE THR ALA ALA GLN ALA          
SEQRES  24 A  351  LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS ASP PRO ASP          
SEQRES  25 A  351  ASP GLU PRO VAL ALA ASP PRO TYR ASP GLN SER PHE GLU          
SEQRES  26 A  351  SER ARG ASP LEU LEU ILE ASP GLU TRP LYS SER LEU THR          
SEQRES  27 A  351  TYR ASP GLU VAL ILE SER PHE VAL PRO PRO PRO LEU ASP          
HET    YIX  A1355      26                                                       
HETNAM     YIX 1-ETHYL-3-(2-{[3-(1-METHYLETHYL)[1,2,4]                          
HETNAM   2 YIX  TRIAZOLO[4,3-A]PYRIDIN-6-YL]SULFANYL}BENZYL)                    
HETNAM   3 YIX  UREA                                                            
HETSYN     YIX CE-159167                                                        
FORMUL   2  YIX    C19 H23 N5 O S                                               
FORMUL   3  HOH   *273(H2 O)                                                    
HELIX    1   1 GLY A   31  ALA A   34  5                                   4    
HELIX    2   2 SER A   61  MET A   78  1                                  18    
HELIX    3   3 SER A   95  PHE A   99  5                                   5    
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  172  ASP A  177  5                                   6    
HELIX    7   7 VAL A  183  TYR A  188  1                                   6    
HELIX    8   8 ALA A  190  LEU A  195  1                                   6    
HELIX    9   9 THR A  203  GLY A  219  1                                  17    
HELIX   10  10 ASP A  227  GLY A  240  1                                  14    
HELIX   11  11 GLY A  243  ILE A  250  1                                   8    
HELIX   12  12 SER A  252  SER A  261  1                                  10    
HELIX   13  13 ASN A  269  PHE A  274  1                                   6    
HELIX   14  14 ASN A  278  LEU A  289  1                                  12    
HELIX   15  15 ASP A  292  ARG A  296  5                                   5    
HELIX   16  16 THR A  298  ALA A  304  1                                   7    
HELIX   17  17 HIS A  305  ALA A  309  5                                   5    
HELIX   18  18 GLN A  325  ARG A  330  5                                   6    
HELIX   19  19 LEU A  333  SER A  347  1                                  15    
SHEET    1  AA 2 PHE A   8  LEU A  13  0                                        
SHEET    2  AA 2 THR A  16  PRO A  21 -1  O  THR A  16   N  LEU A  13           
SHEET    1  AB 5 TYR A  24  PRO A  29  0                                        
SHEET    2  AB 5 VAL A  38  ASP A  43 -1  O  ALA A  40   N  SER A  28           
SHEET    3  AB 5 ARG A  49  LYS A  54 -1  O  VAL A  50   N  ALA A  41           
SHEET    4  AB 5 TYR A 103  HIS A 107 -1  O  LEU A 104   N  LYS A  53           
SHEET    5  AB 5 ASP A  88  PHE A  90 -1  O  ASP A  88   N  VAL A 105           
SHEET    1  AC 3 ALA A 111  ASP A 112  0                                        
SHEET    2  AC 3 LEU A 156  VAL A 158 -1  O  VAL A 158   N  ALA A 111           
SHEET    3  AC 3 LEU A 164  ILE A 166 -1  O  LYS A 165   N  ALA A 157           
SITE     1 AC1 14 LYS A  53  GLU A  71  LEU A  74  LEU A  75                    
SITE     2 AC1 14 ILE A  84  THR A 106  HIS A 107  LEU A 108                    
SITE     3 AC1 14 MET A 109  GLY A 110  ALA A 111  LEU A 167                    
SITE     4 AC1 14 ASP A 168  PHE A 169                                          
CRYST1   45.944   86.523  122.580  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      0.021766  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011558  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008158        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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