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PDBsum entry 2waj

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Transferase PDB id
2waj
Jmol
Contents
Protein chain
348 a.a.
Ligands
SNB
Waters ×178
HEADER    TRANSFERASE                             08-FEB-09   2WAJ
TITLE     CRYSTAL STRUCTURE OF HUMAN JNK3 COMPLEXED WITH A 1-ARYL-3,4-
TITLE    2 DIHYDROISOQUINOLINE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 10;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES, 39-402;
COMPND   5 SYNONYM: STRESS-ACTIVATED PROTEIN KINASE JNK3, C-JUN N-TERMINAL
COMPND   6  KINASE 3, MAP KINASE P49 3F12;
COMPND   7 EC: 2.7.11.24;
COMPND   8 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
KEYWDS    KINASE, EPILEPSY, TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE,
KEYWDS   2 ATP-BINDING, PHOSPHOPROTEIN, PROTEIN KINASE, NUCLEOTIDE-BINDING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.D.BAX,J.A.CHRISTOPHER,E.J.JONES,J.E.MOSLEY
REVDAT   3   13-JUL-11 2WAJ    1       VERSN
REVDAT   2   14-APR-09 2WAJ    1       JRNL
REVDAT   1   31-MAR-09 2WAJ    0
JRNL        AUTH   J.A.CHRISTOPHER,F.L.ATKINSON,B.D.BAX,M.J.BROWN,
JRNL        AUTH 2 A.C.CHAMPIGNY,T.T.CHUANG,E.J.JONES,J.E.MOSLEY,J.R.MUSGRAVE
JRNL        TITL   1-ARYL-3,4-DIHYDROISOQUINOLINE INHIBITORS OF JNK3.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  19  2230 2009
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   19303774
JRNL        DOI    10.1016/J.BMCL.2009.02.098
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.3.0006
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) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8
REMARK   3   NUMBER OF REFLECTIONS             : 15099
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) : 0.187
REMARK   3   R VALUE            (WORKING SET) : 0.183
REMARK   3   FREE R VALUE                     : 0.264
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 799
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) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1101
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440
REMARK   3   BIN FREE R VALUE SET COUNT          : 60
REMARK   3   BIN FREE R VALUE                    : 0.3350
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2878
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 20
REMARK   3   SOLVENT ATOMS            : 178
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 5.77000
REMARK   3    B22 (A**2) : -2.52000
REMARK   3    B33 (A**2) : -3.25000
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): 0.472
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.292
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.241
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.721
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2970 ; 0.012 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4029 ; 1.405 ; 1.978
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   360 ; 6.218 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   135 ;36.501 ;24.222
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   541 ;18.402 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;16.735 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   441 ; 0.095 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2244 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1391 ; 0.217 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2032 ; 0.305 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   199 ; 0.176 ; 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):    33 ; 0.222 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.205 ; 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):  1839 ; 1.282 ; 2.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2924 ; 2.419 ; 5.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1284 ; 3.682 ; 6.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1105 ; 4.993 ; 8.000
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  : 2
REMARK   3   ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    46        A   149
REMARK   3    RESIDUE RANGE :   A   377        A   400
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5119  17.5176  41.3285
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1575 T22:  -0.0990
REMARK   3      T33:  -0.1411 T12:  -0.0125
REMARK   3      T13:   0.0517 T23:  -0.0086
REMARK   3    L TENSOR
REMARK   3      L11:   1.3679 L22:   5.8299
REMARK   3      L33:   4.1542 L12:   0.8915
REMARK   3      L13:   0.7005 L23:   0.4443
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0346 S12:   0.0090 S13:   0.2774
REMARK   3      S21:   0.1948 S22:  -0.0920 S23:   0.0336
REMARK   3      S31:  -0.2413 S32:  -0.0317 S33:   0.1266
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   150        A   206
REMARK   3    RESIDUE RANGE :   A   226        A   374
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2790  13.8694  11.4220
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1826 T22:  -0.1304
REMARK   3      T33:  -0.1546 T12:   0.0173
REMARK   3      T13:  -0.0235 T23:  -0.0109
REMARK   3    L TENSOR
REMARK   3      L11:   1.5152 L22:   3.9382
REMARK   3      L33:   3.1490 L12:   0.5908
REMARK   3      L13:   0.5043 L23:   0.3991
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0395 S12:   0.1065 S13:   0.0451
REMARK   3      S21:  -0.3126 S22:   0.0453 S23:   0.0226
REMARK   3      S31:  -0.1077 S32:  -0.0070 S33:  -0.0058
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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 2WAJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-FEB-09.
REMARK 100 THE PDBE ID CODE IS EBI-38736.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 287
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          : RIGAKU MICROMAX007HF
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : L
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15942
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.71
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : 4.5
REMARK 200  R MERGE                    (I) : 0.10
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.5
REMARK 200  R MERGE FOR SHELL          (I) : 0.45
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 2O0U
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 0.1M SODIUM HEPES
REMARK 280  PH7.5
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       25.82950
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.77050
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.66950
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.77050
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.82950
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.66950
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: 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    39
REMARK 465     SER A    40
REMARK 465     LYS A    41
REMARK 465     SER A    42
REMARK 465     LYS A    43
REMARK 465     VAL A    44
REMARK 465     ASP A    45
REMARK 465     ALA A    74
REMARK 465     GLN A    75
REMARK 465     THR A   213
REMARK 465     ALA A   214
REMARK 465     GLY A   215
REMARK 465     ILE A   375
REMARK 465     TYR A   376
REMARK 465     SER A   401
REMARK 465     GLU A   402
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     MET A 219    CG   SD   CE
REMARK 470     TYR A 223    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLN A 374    CG   CD   OE1  NE2
REMARK 470     GLU A 382    CG   CD   OE1  OE2
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  2023     O    HOH A  2085              2.17
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    ASP A  55       42.33   -102.23
REMARK 500    ARG A  97       58.06     34.81
REMARK 500    GLN A 140      -48.14   -140.26
REMARK 500    ARG A 188       -9.70     76.83
REMARK 500    ALA A 211     -115.84   -106.16
REMARK 500    SER A 217       82.14    133.35
REMARK 500    PRO A 284      -48.98    -26.73
REMARK 500    ALA A 320       51.76   -157.28
REMARK 500    GLU A 369       42.83    -93.68
REMARK 500    LYS A 378      -81.73    123.59
REMARK 500    GLN A 379        1.56    -68.78
REMARK 500    ASP A 381      -32.44     91.54
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 SNB A1401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PMV   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF JNK3 IN COMPLEX WITH
REMARK 900  ADIHYDROANTHRAPYRAZOLE INHIBITOR
REMARK 900 RELATED ID: 1PMQ   RELATED DB: PDB
REMARK 900  THE STRUCTURE OF JNK3 IN COMPLEX WITH AN
REMARK 900  IMIDAZOLE-PYRIMIDINE INHIBITOR
REMARK 900 RELATED ID: 1JNK   RELATED DB: PDB
REMARK 900  THE C-JUN N-TERMINAL KINASE (JNK3S)
REMARK 900  COMPLEXED WITH MGAMP-PNP
REMARK 900 RELATED ID: 1PMU   RELATED DB: PDB
REMARK 900  THE CRYSTAL STRUCTURE OF JNK3 IN COMPLEX
REMARK 900  WITH APHENANTROLINE INHIBITOR
REMARK 900 RELATED ID: 1PMN   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF JNK3 IN COMPLEX WITH
REMARK 900  AN IMIDAZOLE-PYRIMIDINE INHIBITOR
DBREF  2WAJ A   39   402  UNP    P53779   MK10_HUMAN      39    402
SEQRES   1 A  364  MET SER LYS SER LYS VAL ASP ASN GLN PHE TYR SER VAL
SEQRES   2 A  364  GLU VAL GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR
SEQRES   3 A  364  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE
SEQRES   4 A  364  VAL CYS ALA ALA TYR ASP ALA VAL LEU ASP ARG ASN VAL
SEQRES   5 A  364  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR
SEQRES   6 A  364  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS
SEQRES   7 A  364  CYS VAL ASN HIS LYS ASN ILE ILE SER LEU LEU ASN VAL
SEQRES   8 A  364  PHE THR PRO GLN LYS THR LEU GLU GLU PHE GLN ASP VAL
SEQRES   9 A  364  TYR LEU VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN
SEQRES  10 A  364  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR
SEQRES  11 A  364  LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS
SEQRES  12 A  364  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN
SEQRES  13 A  364  ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP
SEQRES  14 A  364  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET
SEQRES  15 A  364  THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU
SEQRES  16 A  364  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE
SEQRES  17 A  364  TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL ARG HIS
SEQRES  18 A  364  LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP
SEQRES  19 A  364  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU
SEQRES  20 A  364  PHE MET LYS LYS LEU GLN PRO THR VAL ARG ASN TYR VAL
SEQRES  21 A  364  GLU ASN ARG PRO LYS TYR ALA GLY LEU THR PHE PRO LYS
SEQRES  22 A  364  LEU PHE PRO ASP SER LEU PHE PRO ALA ASP SER GLU HIS
SEQRES  23 A  364  ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER
SEQRES  24 A  364  LYS MET LEU VAL ILE ASP PRO ALA LYS ARG ILE SER VAL
SEQRES  25 A  364  ASP ASP ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR
SEQRES  26 A  364  ASP PRO ALA GLU VAL GLU ALA PRO PRO PRO GLN ILE TYR
SEQRES  27 A  364  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU
SEQRES  28 A  364  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASN SER GLU
HET    SNB  A1401      20
HETNAM     SNB 1-(3-BROMOPHENYL)-7-CHLORO-6-METHOXY-3,4-
HETNAM   2 SNB  DIHYDROISOQUINOLINE
FORMUL   2  SNB    C16 H13 N1 O1 BR1 CL1
FORMUL   3  HOH   *178(H2 O)
HELIX    1   1 ASN A  101  CYS A  117  1                                  17
HELIX    2   2 LEU A  153  GLN A  158  1                                   6
HELIX    3   3 ASP A  162  ALA A  183  1                                  22
HELIX    4   4 LYS A  191  SER A  193  5                                   3
HELIX    5   5 ALA A  231  LEU A  236  1                                   6
HELIX    6   6 ASN A  243  HIS A  259  1                                  17
HELIX    7   7 ASP A  267  GLY A  280  1                                  14
HELIX    8   8 CYS A  283  LYS A  288  1                                   6
HELIX    9   9 GLN A  291  ASN A  300  1                                  10
HELIX   10  10 THR A  308  PHE A  313  1                                   6
HELIX   11  11 PRO A  314  PHE A  318  5                                   5
HELIX   12  12 SER A  322  LEU A  340  1                                  19
HELIX   13  13 SER A  349  GLN A  355  1                                   7
HELIX   14  14 ILE A  359  TYR A  363  5                                   5
HELIX   15  15 ASP A  364  GLU A  369  1                                   6
HELIX   16  16 THR A  386  ASN A  400  1                                  15
SHEET    1  AA 2 PHE A  48  GLU A  52  0
SHEET    2  AA 2 THR A  57  LEU A  61 -1  O  PHE A  58   N  VAL A  51
SHEET    1  AB 5 TYR A  64  GLY A  71  0
SHEET    2  AB 5 ILE A  77  ASP A  83 -1  O  VAL A  78   N  ILE A  70
SHEET    3  AB 5 ARG A  88  SER A  96 -1  O  ARG A  88   N  ASP A  83
SHEET    4  AB 5 ASP A 141  GLU A 147 -1  O  VAL A 142   N  LEU A  95
SHEET    5  AB 5 ASN A 128  PHE A 130 -1  O  ASN A 128   N  VAL A 145
SHEET    1  AC 3 ALA A 151  ASN A 152  0
SHEET    2  AC 3 ILE A 195  VAL A 197 -1  O  VAL A 197   N  ALA A 151
SHEET    3  AC 3 LEU A 203  ILE A 205 -1  O  LYS A 204   N  VAL A 196
CISPEP   1 THR A  216    SER A  217          0       -10.96
CISPEP   2 PRO A  373    GLN A  374          0        -6.89
SITE     1 AC1  8 ALA A  91  ILE A 124  LEU A 144  MET A 146
SITE     2 AC1  8 GLU A 147  MET A 149  LEU A 206  HOH A2028
CRYST1   51.659   71.339  107.541  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      0.019358  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014018  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009299        0.00000
      
PROCHECK
Go to PROCHECK summary
 References