HEADER KINASE/INHIBITOR 16-SEP-04 1W83
TITLE P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH SMALL MOLECULE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: P38 MAP KINASE;
COMPND 5 EC: 2.7.1.37;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: KINASE DOMAIN
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 KINASE/INHIBITOR, KINASE/INHIBITOR COMPLEX, P38, KINASE,
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.TICKLE,H.JHOTI,A.CLEASBY,L.DEVINE
REVDAT 2 24-FEB-09 1W83 1 VERSN
REVDAT 1 08-FEB-05 1W83 0
JRNL AUTH A.GILL,M.FREDERICKSON,A.CLEASBY,S.WOODHEAD,M.CARR,
JRNL AUTH 2 A.WOODHEAD,M.WALKER,M.CONGREVE,L.DEVINE,D.TISI,
JRNL AUTH 3 M.O'REILLY,L.SEAVERS,D.DAVIS,J.CURRY,R.ANTHONY,
JRNL AUTH 4 A.PADOVA,C.MURRAY,R.CARR,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. 2.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003A
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 16512
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.322
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 880
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1127
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.4060
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 : 31
REMARK 3 SOLVENT ATOMS : 369
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.79000
REMARK 3 B22 (A**2) : -0.30000
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): 0.552
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.362
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.271
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.081
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.834
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2934 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3985 ; 1.710 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 350 ; 6.759 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 138 ;38.034 ;23.986
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 505 ;20.084 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;18.367 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 442 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2225 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1424 ; 0.157 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1949 ; 0.301 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 102 ; 0.124 ; 0.500
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): 39 ; 0.117 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.111 ; 0.500
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): 1807 ; 3.773 ;21.126
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2851 ; 5.646 ;21.593
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1284 ; 7.486 ;26.919
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1134 ; 7.536 ;26.888
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 1W83 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-SEP-04.
REMARK 100 THE PDBE ID CODE IS EBI-21058.
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 : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
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 : 17439
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.6000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL
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 22.84050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.03950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.05050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.03950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.84050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.05050
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 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2073 - O HOH A 2205 2.18
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 LEU A 167 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 PRO A 350 C - N - CA ANGL. DEV. = 9.7 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 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 40.51 38.98
REMARK 500 ALA A 111 116.50 93.83
REMARK 500 ARG A 149 -14.60 77.55
REMARK 500 ASP A 150 46.49 -142.68
REMARK 500 HIS A 174 81.99 56.59
REMARK 500 THR A 175 -167.77 -101.85
REMARK 500 PRO A 350 139.91 -35.13
REMARK 500 PRO A 352 20.14 -60.47
REMARK 500 LEU A 353 62.93 63.12
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 L11 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: 1W84 RELATED DB: PDB
REMARK 900 P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH
REMARK 900 SMALL MOLECULE INHIBITOR
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
DBREF 1W83 A 1 1 PDB 1W83 1W83 1 1
DBREF 1W83 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 L11 A1355 31
HETNAM L11 N-[4-CHLORO-3-(PYRIDIN-3-YLOXYMETHYL)-PHENYL]
HETNAM 2 L11 -3-FLUORO-
FORMUL 2 L11 C23 H25 CL F N3 O3
FORMUL 3 HOH *369(H2 O1)
HELIX 1 1 SER A 61 MET A 78 1 18
HELIX 2 2 ASP A 112 GLN A 120 1 9
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 VAL A 183 TYR A 188 1 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 GLN A 260 1 9
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 THR A 298 LEU A 303 1 6
HELIX 15 15 ALA A 304 ALA A 309 5 6
HELIX 16 16 GLN A 325 ARG A 330 5 6
HELIX 17 17 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 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 ARG A 49 LEU A 55 -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 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
SITE 1 AC1 13 VAL A 38 ALA A 51 GLU A 71 LEU A 75
SITE 2 AC1 13 ILE A 84 THR A 106 MET A 109 ILE A 141
SITE 3 AC1 13 HIS A 148 ILE A 166 LEU A 167 ASP A 168
SITE 4 AC1 13 PHE A 169
CRYST1 45.681 86.101 126.079 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 0.021891 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011614 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007932 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
