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PDBsum entry 2ghl

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2ghl
Jmol
Contents
Protein chain
334 a.a.
Ligands
LIB
Waters ×310
HEADER    TRANSFERASE                             27-MAR-06   2GHL
TITLE     MUTANT MUS MUSCULUS P38 KINASE DOMAIN IN COMPLEX WITH
TITLE    2 INHIBITOR PG-874743
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA, MAP
COMPND   5 KINASE P38 ALPHA, CRK1;
COMPND   6 EC: 2.7.1.37;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: MAPK14, CRK1, CSBP1, CSBP2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    MAP KINASE P38, P38, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.L.WALTER,M.J.MEKEL,A.G.EVDOKIMOV,M.E.POKROSS,T.A.BRUGEL
REVDAT   3   24-FEB-09 2GHL    1       VERSN
REVDAT   2   13-JUN-06 2GHL    1       JRNL
REVDAT   1   11-APR-06 2GHL    0
JRNL        AUTH   T.A.BRUGEL,J.A.MAIER,M.P.CLARK,M.SABAT,
JRNL        AUTH 2 A.GOLEBIOWSKI,R.G.BOOKLAND,M.J.LAUFERSWEILER,
JRNL        AUTH 3 S.K.LAUGHLIN,J.C.VANRENS,B.DE,L.C.HSIEH,M.J.MEKEL,
JRNL        AUTH 4 M.J.JANUSZ
JRNL        TITL   DEVELOPMENT OF N-2,4-PYRIMIDINE-N-PHENYL-N'-PHENYL
JRNL        TITL 2 UREAS AS INHIBITORS OF TUMOR NECROSIS FACTOR ALPHA
JRNL        TITL 3 (TNF-ALPHA) SYNTHESIS. PART 1.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16  3510 2006
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   16632356
JRNL        DOI    10.1016/J.BMCL.2006.03.095
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.45
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 20513
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : 5% RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.301
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1055
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2689
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 32
REMARK   3   SOLVENT ATOMS            : 310
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.05
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
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 : NULL
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : NULL
REMARK   3   ION PROBE RADIUS   : NULL
REMARK   3   SHRINKAGE RADIUS   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2GHL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB037127.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 22-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21666
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0
REMARK 200  DATA REDUNDANCY                : 6.500
REMARK 200  R MERGE                    (I) : 0.06300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.39100
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18%(W/V) PEG 1500  0.1M MES, PH
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 288K
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       32.63050
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.46900
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.21300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.46900
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.63050
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.21300
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 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     LYS A   118
REMARK 465     CYS A   119
REMARK 465     GLN A   120
REMARK 465     LYS A   121
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     ALA A   180
REMARK 465     GLY A   181
REMARK 465     PHE A   182
REMARK 465     VAL A   183
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     ARG A 173    CG   CD   NE   CZ   NH1  NH2
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   N    ARG A    57     O    HOH A   692              2.04
REMARK 500   OD1  ASP A   316     O    HOH A   661              2.18
REMARK 500   O    HOH A   464     O    HOH A   710              2.19
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    MET A 213   SD    MET A 213   CE     -0.341
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 296   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A 296   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ASP A 331   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 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    LYS A  15      -28.38     83.01
REMARK 500    ALA A  93      137.24    -37.65
REMARK 500    ASN A 100       10.92   -147.42
REMARK 500    ARG A 149      -16.10     75.63
REMARK 500    ASP A 150       45.40   -141.60
REMARK 500    ASP A 161       -2.22    -58.70
REMARK 500    ASP A 168       11.56     59.37
REMARK 500    PHE A 169      172.67    -48.09
REMARK 500    ALA A 172      156.51     96.85
REMARK 500    ASN A 196       50.11     71.76
REMARK 500    TRP A 197       77.09   -105.13
REMARK 500    MET A 198        5.03    -66.57
REMARK 500    HIS A 199       63.41   -105.75
REMARK 500    TYR A 200     -165.25    -74.59
REMARK 500    ALA A 244      -38.71    -35.55
REMARK 500    LEU A 289       52.47    -96.84
REMARK 500    ASP A 316       51.19   -143.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 LEU A  171     ALA A  172                 -130.46
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 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 514        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH A 523        DISTANCE =  7.31 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LIB A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YW2   RELATED DB: PDB
REMARK 900 RELATED ID: 1YWR   RELATED DB: PDB
DBREF  2GHL A    5   352  UNP    P47811   MK14_MOUSE       4    351
SEQADV 2GHL ALA A  180  UNP  P47811    THR   179 ENGINEERED
SEQADV 2GHL PHE A  182  UNP  P47811    TYR   181 ENGINEERED
SEQRES   1 A  348  ARG PRO THR PHE TYR ARG GLN GLU LEU ASN LYS THR ILE
SEQRES   2 A  348  TRP GLU VAL PRO GLU ARG TYR GLN ASN LEU SER PRO VAL
SEQRES   3 A  348  GLY SER GLY ALA TYR GLY SER VAL CYS ALA ALA PHE ASP
SEQRES   4 A  348  THR LYS THR GLY HIS ARG VAL ALA VAL LYS LYS LEU SER
SEQRES   5 A  348  ARG PRO PHE GLN SER ILE ILE HIS ALA LYS ARG THR TYR
SEQRES   6 A  348  ARG GLU LEU ARG LEU LEU LYS HIS MET LYS HIS GLU ASN
SEQRES   7 A  348  VAL ILE GLY LEU LEU ASP VAL PHE THR PRO ALA ARG SER
SEQRES   8 A  348  LEU GLU GLU PHE ASN ASP VAL TYR LEU VAL THR HIS LEU
SEQRES   9 A  348  MET GLY ALA ASP LEU ASN ASN ILE VAL LYS CYS GLN LYS
SEQRES  10 A  348  LEU THR ASP ASP HIS VAL GLN PHE LEU ILE TYR GLN ILE
SEQRES  11 A  348  LEU ARG GLY LEU LYS TYR ILE HIS SER ALA ASP ILE ILE
SEQRES  12 A  348  HIS ARG ASP LEU LYS PRO SER ASN LEU ALA VAL ASN GLU
SEQRES  13 A  348  ASP CYS GLU LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG
SEQRES  14 A  348  HIS THR ASP ASP GLU MET ALA GLY PHE VAL ALA THR ARG
SEQRES  15 A  348  TRP TYR ARG ALA PRO GLU ILE MET LEU ASN TRP MET HIS
SEQRES  16 A  348  TYR ASN GLN THR VAL ASP ILE TRP SER VAL GLY CYS ILE
SEQRES  17 A  348  MET ALA GLU LEU LEU THR GLY ARG THR LEU PHE PRO GLY
SEQRES  18 A  348  THR ASP HIS ILE ASP GLN LEU LYS LEU ILE LEU ARG LEU
SEQRES  19 A  348  VAL GLY THR PRO GLY ALA GLU LEU LEU LYS LYS ILE SER
SEQRES  20 A  348  SER GLU SER ALA ARG ASN TYR ILE GLN SER LEU ALA GLN
SEQRES  21 A  348  MET PRO LYS MET ASN PHE ALA ASN VAL PHE ILE GLY ALA
SEQRES  22 A  348  ASN PRO LEU ALA VAL ASP LEU LEU GLU LYS MET LEU VAL
SEQRES  23 A  348  LEU ASP SER ASP LYS ARG ILE THR ALA ALA GLN ALA LEU
SEQRES  24 A  348  ALA HIS ALA TYR PHE ALA GLN TYR HIS ASP PRO ASP ASP
SEQRES  25 A  348  GLU PRO VAL ALA ASP PRO TYR ASP GLN SER PHE GLU SER
SEQRES  26 A  348  ARG ASP LEU LEU ILE ASP GLU TRP LYS SER LEU THR TYR
SEQRES  27 A  348  ASP GLU VAL ILE SER PHE VAL PRO PRO PRO
HET    LIB  A 401      32
HETNAM     LIB 3-(2-CHLOROPHENYL)-1-(2-{[(1S)-2-HYDROXY-1,2-
HETNAM   2 LIB  DIMETHYLPROPYL]AMINO}PYRIMIDIN-4-YL)-1-(4-
HETNAM   3 LIB  METHOXYPHENYL)UREA
HETSYN     LIB 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.]PYRAZOLE
FORMUL   2  LIB    C23 H26 CL N5 O3
FORMUL   3  HOH   *310(H2 O)
HELIX    1   1 SER A   61  MET A   78  1                                  18
HELIX    2   2 THR A  123  ALA A  144  1                                  22
HELIX    3   3 LYS A  152  SER A  154  5                                   3
HELIX    4   4 ALA A  184  ARG A  189  5                                   6
HELIX    5   5 ALA A  190  LEU A  195  1                                   6
HELIX    6   6 THR A  203  GLY A  219  1                                  17
HELIX    7   7 ASP A  227  GLY A  240  1                                  14
HELIX    8   8 GLY A  243  LYS A  248  1                                   6
HELIX    9   9 SER A  252  GLN A  260  1                                   9
HELIX   10  10 ASN A  269  PHE A  274  1                                   6
HELIX   11  11 ASN A  278  LEU A  289  1                                  12
HELIX   12  12 THR A  298  HIS A  305  1                                   8
HELIX   13  13 ALA A  306  ALA A  309  5                                   4
HELIX   14  14 GLN A  325  ARG A  330  5                                   6
HELIX   15  15 LEU A  333  SER A  347  1                                  15
SHEET    1   A 2 PHE A   8  LEU A  13  0
SHEET    2   A 2 THR A  16  PRO A  21 -1  O  TRP A  18   N  GLN A  11
SHEET    1   B 5 TYR A  24  SER A  32  0
SHEET    2   B 5 GLY A  36  ASP A  43 -1  O  PHE A  42   N  GLN A  25
SHEET    3   B 5 ARG A  49  LEU A  55 -1  O  VAL A  50   N  ALA A  41
SHEET    4   B 5 TYR A 103  HIS A 107 -1  O  LEU A 104   N  LYS A  53
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
CISPEP   1 GLY A  170    LEU A  171          0       -23.57
SITE     1 AC1 14 VAL A  30  TYR A  35  ALA A  51  LYS A  53
SITE     2 AC1 14 LEU A 104  VAL A 105  THR A 106  HIS A 107
SITE     3 AC1 14 MET A 109  ALA A 111  ASP A 112  HOH A 402
SITE     4 AC1 14 HOH A 598  HOH A 635
CRYST1   65.261   74.426   76.938  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      0.015320  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013440  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013000        0.00000
      
PROCHECK
Go to PROCHECK summary
 References