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PDBsum entry 1wbt

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1wbt
Jmol
Contents
Protein chain
352 a.a.
Ligands
WBT
Waters ×254
HEADER    TRANSFERASE                             05-NOV-04   1WBT
TITLE     IDENTIFICATION OF NOVEL P38 ALPHA MAP KINASE INHIBITORS
TITLE    2 USING FRAGMENT-BASED LEAD GENERATION.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: P38 ALPHA MAP KINASE, MITOGEN-ACTIVATED PROTEIN
COMPND   5  KINASE P38 ALPHA, MAP KINASE P38ALPHA, CYTOKINE
COMPND   6  SUPPRESSIVE ANTI-INFLAMMATORY DRUG BINDING PROTEIN, CSAID
COMPND   7  BINDING PROTEIN, CSBP, MAX-INTERACTING PROTEIN 2, MAP
COMPND   8  KINASE MXI2, SAPK2A;
COMPND   9 EC: 2.7.1.37;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: BL21 DE3
KEYWDS    TRANSFERASE, ATP-BINDING, DIRECT PROTEIN SEQUENCING,
KEYWDS   2 NUCLEAR PROTEIN, PHOSPHORYLATION, SERINE/THREONINE-PROTEIN
KEYWDS   3 KINASE, P38 MAP KINASE, INHIBITOR STRUCTURE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.TICKLE,A.CLEASBY,L.A.DEVINE,H.JHOTI
REVDAT   2   24-FEB-09 1WBT    1       VERSN
REVDAT   1   03-NOV-05 1WBT    0
JRNL        AUTH   A.L.GILL,M.FREDERICKSON,A.CLEASBY,S.J.WOODHEAD,
JRNL        AUTH 2 M.G.CARR,A.J.WOODHEAD,M.T.WALKER,M.S.CONGREVE,
JRNL        AUTH 3 L.A.DEVINE,D.TISI,M.O'REILLY,L.C.SEAVERS,D.J.DAVIS,
JRNL        AUTH 4 J.CURRY,R.ANTHONY,A.PADOVA,C.W.MURRAY,R.A.CARR,
JRNL        AUTH 5 H.JHOTI
JRNL        TITL   IDENTIFICATION OF NOVEL P38ALPHA MAP KINASE
JRNL        TITL 2 INHIBITORS USING FRAGMENT-BASED LEAD GENERATION.
JRNL        REF    J.MED.CHEM.                   V.  48   414 2005
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   15658855
JRNL        DOI    10.1021/JM049575N
REMARK   2
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0003
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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.71
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5
REMARK   3   NUMBER OF REFLECTIONS             : 33834
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) : 0.229
REMARK   3   R VALUE            (WORKING SET) : 0.227
REMARK   3   FREE R VALUE                     : 0.276
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1662
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1840
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760
REMARK   3   BIN FREE R VALUE SET COUNT          : 100
REMARK   3   BIN FREE R VALUE                    : 0.3620
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          : 33
REMARK   3   SOLVENT ATOMS            : 254
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 32.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.18
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.06000
REMARK   3    B22 (A**2) : 1.14000
REMARK   3    B33 (A**2) : -1.09000
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): 0.190
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.179
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.563
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.926
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2937 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  2670 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3990 ; 1.479 ; 1.977
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6206 ; 0.857 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   350 ; 6.003 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   138 ;37.219 ;23.986
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   505 ;16.381 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;19.919 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   442 ; 0.083 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3229 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   596 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   612 ; 0.200 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2728 ; 0.177 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1411 ; 0.178 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1688 ; 0.085 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   174 ; 0.188 ; 0.200
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):     9 ; 0.120 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    36 ; 0.197 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.143 ; 0.200
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):  2302 ; 3.559 ;23.163
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2851 ; 4.215 ;23.436
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1393 ; 4.124 ;26.837
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1139 ; 5.719 ;28.479
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  : NULL
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
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 1WBT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  05-NOV-04.
REMARK 100 THE PDBE ID CODE IS EBI-21529.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33834
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.710
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4
REMARK 200  DATA REDUNDANCY                : 2.500
REMARK 200  R MERGE                    (I) : 0.11000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 4.1000
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   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: DENCOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
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       22.75950
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.28850
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.80100
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.28850
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.75950
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.80100
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 GENERATING THE BIOMOLECULE
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400  CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN.
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     1
REMARK 465     SER A     2
REMARK 465     GLN A     3
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 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     GLN A 355    CA   C    O    CB   CG   CD   OE1  NE2
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 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 149       -6.74     71.17
REMARK 500    ASP A 150       40.59   -144.46
REMARK 500    ASN A 196       73.02     40.52
REMARK 500    SER A 252       94.84    -63.20
REMARK 500    ASN A 278      120.48    -37.09
REMARK 500    PRO A 352      125.74    -33.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WBT A1355
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A9U   RELATED DB: PDB
REMARK 900  THE COMPLEX STRUCTURE OF THE MAP KINASE
REMARK 900  P38/SB203580
REMARK 900 RELATED ID: 1BL6   RELATED DB: PDB
REMARK 900  THE COMPLEX STRUCTURE OF THE MAP KINASE
REMARK 900  P38/SB216995
REMARK 900 RELATED ID: 1BL7   RELATED DB: PDB
REMARK 900  THE COMPLEX STRUCTURE OF THE MAP KINASE
REMARK 900  P38/SB220025
REMARK 900 RELATED ID: 1BMK   RELATED DB: PDB
REMARK 900  THE COMPLEX STRUCTURE OF THE MAP KINASE
REMARK 900  P38/SB218655
REMARK 900 RELATED ID: 1DI9   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF P38 MITOGEN-ACTIVATED
REMARK 900  PROTEIN KINASE INCOMPLEX WITH 4-[3-
REMARK 900  METHYLSULFANYLANILINO]-6,7-DIMETHOXYQUINAZOLINE
REMARK 900 RELATED ID: 1IAN   RELATED DB: PDB
REMARK 900  HUMAN P38 MAP KINASE INHIBITOR COMPLEX
REMARK 900 RELATED ID: 1KV1   RELATED DB: PDB
REMARK 900  P38 MAP KINASE IN COMPLEX WITH INHIBITOR 1
REMARK 900 RELATED ID: 1KV2   RELATED DB: PDB
REMARK 900  HUMAN P38 MAP KINASE IN COMPLEX WITH BIRB
REMARK 900   796
REMARK 900 RELATED ID: 1M7Q   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF P38 MAP KINASE IN
REMARK 900  COMPLEX WITH ADIHYDROQUINAZOLINONE 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: 1OUY   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF P38 ALPHA IN COMPLEX WITH
REMARK 900   A DIHYDROPYRIDO-PYRIMIDINE INHIBITOR
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: 1OZ1   RELATED DB: PDB
REMARK 900  P38 MITOGEN-ACTIVATED KINASE IN COMPLEX WITH
REMARK 900   4-AZAINDOLEINHIBITOR
REMARK 900 RELATED ID: 1R39   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF P38ALPHA
REMARK 900 RELATED ID: 1R3C   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF P38ALPHA C162S MUTANT
REMARK 900 RELATED ID: 1W7H   RELATED DB: PDB
REMARK 900  P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH
REMARK 900   SMALL MOLECULE INHIBITOR
REMARK 900 RELATED ID: 1W82   RELATED DB: PDB
REMARK 900  P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH
REMARK 900   SMALL MOLECULE INHIBITOR
REMARK 900 RELATED ID: 1W83   RELATED DB: PDB
REMARK 900  P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH
REMARK 900   SMALL MOLECULE INHIBITOR
REMARK 900 RELATED ID: 1W84   RELATED DB: PDB
REMARK 900  P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH
REMARK 900   SMALL MOLECULE INHIBITOR
REMARK 900 RELATED ID: 1WBN   RELATED DB: PDB
REMARK 900  FRAGMENT BASED P38 INHIBITORS
REMARK 900 RELATED ID: 1WBO   RELATED DB: PDB
REMARK 900  FRAGMENT BASED P38 INHIBITORS
REMARK 900 RELATED ID: 1WBS   RELATED DB: PDB
REMARK 900  IDENTIFICATION OF NOVEL P38 ALPHA MAP KINASE
REMARK 900   INHIBITORS USING FRAGMENT-BASED LEAD
REMARK 900  GENERATION.
REMARK 900 RELATED ID: 1WBV   RELATED DB: PDB
REMARK 900  IDENTIFICATION OF NOVEL P38 ALPHA MAP KINASE
REMARK 900   INHIBITORS USING FRAGMENT-BASED LEAD
REMARK 900  GENERATION.
REMARK 900 RELATED ID: 1WBW   RELATED DB: PDB
REMARK 900  IDENTIFICATION OF NOVEL P38 ALPHA MAP KINASE
REMARK 900   INHIBITORS USING FRAGMENT-BASED LEAD
REMARK 900  GENERATION.
REMARK 900 RELATED ID: 1WFC   RELATED DB: PDB
REMARK 900  STRUCTURE OF APO, UNPHOSPHORYLATED, P38
REMARK 900  MITOGEN ACTIVATEDPROTEIN KINASE P38 (P38 MAP
REMARK 900  KINASE) THE MAMMALIAN HOMOLOGUEOF THE YEAST
REMARK 900  HOG1 PROTEIN
REMARK 900 RELATED ID: 1YQJ   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF P38 ALPHA IN COMPLEX
REMARK 900  WITH A SELECTIVEPYRIDAZINE INHIBITOR
REMARK 900 RELATED ID: 1ZZ2   RELATED DB: PDB
REMARK 900  TWO CLASSES OF P38ALPHA MAP KINASE
REMARK 900  INHIBITORS HAVING ACOMMON DIPHENYLETHER CORE
REMARK 900  BUT EXHIBITING DIVERGENT BINDINGMODES
REMARK 900 RELATED ID: 1ZZL   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF P38 WITH TRIAZOLOPYRIDINE
DBREF  1WBT A    1     1  PDB    1WBT     1WBT             1      1
DBREF  1WBT A    2   360  UNP    Q16539   MK14_HUMAN       1    359
SEQRES   1 A  360  MET SER GLN GLU ARG PRO THR PHE TYR ARG GLN GLU LEU
SEQRES   2 A  360  ASN LYS THR ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN
SEQRES   3 A  360  LEU SER PRO VAL GLY SER GLY ALA TYR GLY SER VAL CYS
SEQRES   4 A  360  ALA ALA PHE ASP THR LYS THR GLY LEU ARG VAL ALA VAL
SEQRES   5 A  360  LYS LYS LEU SER ARG PRO PHE GLN SER ILE ILE HIS ALA
SEQRES   6 A  360  LYS ARG THR TYR ARG GLU LEU ARG LEU LEU LYS HIS MET
SEQRES   7 A  360  LYS HIS GLU ASN VAL ILE GLY LEU LEU ASP VAL PHE THR
SEQRES   8 A  360  PRO ALA ARG SER LEU GLU GLU PHE ASN ASP VAL TYR LEU
SEQRES   9 A  360  VAL THR HIS LEU MET GLY ALA ASP LEU ASN ASN ILE VAL
SEQRES  10 A  360  LYS CYS GLN LYS LEU THR ASP ASP HIS VAL GLN PHE LEU
SEQRES  11 A  360  ILE TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER
SEQRES  12 A  360  ALA ASP ILE ILE HIS ARG ASP LEU LYS PRO SER ASN LEU
SEQRES  13 A  360  ALA VAL ASN GLU ASP CYS GLU LEU LYS ILE LEU ASP PHE
SEQRES  14 A  360  GLY LEU ALA ARG HIS THR ASP ASP GLU MET THR GLY TYR
SEQRES  15 A  360  VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU
SEQRES  16 A  360  ASN TRP MET HIS TYR ASN GLN THR VAL ASP ILE TRP SER
SEQRES  17 A  360  VAL GLY CYS ILE MET ALA GLU LEU LEU THR GLY ARG THR
SEQRES  18 A  360  LEU PHE PRO GLY THR ASP HIS ILE ASP GLN LEU LYS LEU
SEQRES  19 A  360  ILE LEU ARG LEU VAL GLY THR PRO GLY ALA GLU LEU LEU
SEQRES  20 A  360  LYS LYS ILE SER SER GLU SER ALA ARG ASN TYR ILE GLN
SEQRES  21 A  360  SER LEU THR GLN MET PRO LYS MET ASN PHE ALA ASN VAL
SEQRES  22 A  360  PHE ILE GLY ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU
SEQRES  23 A  360  LYS MET LEU VAL LEU ASP SER ASP LYS ARG ILE THR ALA
SEQRES  24 A  360  ALA GLN ALA LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS
SEQRES  25 A  360  ASP PRO ASP ASP GLU PRO VAL ALA ASP PRO TYR ASP GLN
SEQRES  26 A  360  SER PHE GLU SER ARG ASP LEU LEU ILE ASP GLU TRP LYS
SEQRES  27 A  360  SER LEU THR TYR ASP GLU VAL ILE SER PHE VAL PRO PRO
SEQRES  28 A  360  PRO LEU ASP GLN GLU GLU MET GLU SER
HET    WBT  A1355      33
HETNAM     WBT 3-FLUORO-5-MORPHOLIN-4-YL-N-[1-(2-PYRIDIN-4-
HETNAM   2 WBT  YLETHYL)-1H-INDOL-6-YL]BENZAMIDE
FORMUL   2  WBT    C26 H25 F N4 O2
FORMUL   3  HOH   *254(H2 O1)
HELIX    1   1 SER A   61  MET A   78  1                                  18
HELIX    2   2 ASP A  112  CYS A  119  1                                   8
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 ASP A  176  THR A  180  5                                   5
HELIX    6   6 ALA A  190  LEU A  195  1                                   6
HELIX    7   7 THR A  203  GLY A  219  1                                  17
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  VAL A  273  5                                   5
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 ASP A  313  GLU A  317  5                                   5
HELIX   17  17 GLN A  325  ARG A  330  5                                   6
HELIX   18  18 LEU A  333  PHE A  348  1                                  16
SHEET    1  AA 2 PHE A   8  GLU A  12  0
SHEET    2  AA 2 ILE A  17  PRO A  21 -1  O  TRP A  18   N  GLN A  11
SHEET    1  AB 5 TYR A  24  GLY A  33  0
SHEET    2  AB 5 GLY A  36  ASP A  43 -1  O  GLY A  36   N  GLY A  33
SHEET    3  AB 5 LEU A  48  LEU A  55 -1  O  LEU A  48   N  ASP A  43
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 2 LEU A 156  VAL A 158  0
SHEET    2  AC 2 LEU A 164  ILE A 166 -1  O  LYS A 165   N  ALA A 157
CISPEP   1 LEU A  353    ASP A  354          0       -13.95
SITE     1 AC1 15 ALA A  51  LYS A  53  GLU A  71  LEU A  75
SITE     2 AC1 15 ILE A  84  THR A 106  HIS A 107  LEU A 108
SITE     3 AC1 15 MET A 109  ILE A 141  HIS A 148  ILE A 166
SITE     4 AC1 15 LEU A 167  ASP A 168  PHE A 169
CRYST1   45.519   85.602  126.577  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      0.021969  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011682  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007900        0.00000
      
PROCHECK
Go to PROCHECK summary
 References