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Database: PDB
Entry: 4HYU
LinkDB: 4HYU
Original site: 4HYU 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       14-NOV-12   4HYU              
TITLE     CRYSTAL STRUCTURE OF JNK1 IN COMPLEX WITH JIP1 PEPTIDE AND 4-{4-[4-(3-
TITLE    2 METHANESULFONYL-PROPOXY)-INDAZOL-1-YL]-PYRIMIDIN-2-YLAMINO}-         
TITLE    3 CYCLOHEXAN                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-369;                                            
COMPND   5 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE 8 ISOFORM JNK1 BETA2,      
COMPND   6 MITOGEN-ACTIVATED PROTEIN KINASE 8, ISOFORM CRA_D, CDNA FLJ77387,    
COMPND   7 HIGHLY SIMILAR TO HOMO SAPIENS MITOGEN-ACTIVATED PROTEIN KINASE 8    
COMPND   8 (MAPK8), TRANSCRIPT VARIANT 4, MRNA;                                 
COMPND   9 EC: 2.7.1.37;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1;         
COMPND  13 CHAIN: B;                                                            
COMPND  14 FRAGMENT: RESIDUES 157-167;                                          
COMPND  15 SYNONYM: JIP-1, JNK-INTERACTING PROTEIN 1, ISLET-BRAIN 1, IB-1, JNK  
COMPND  16 MAP KINASE SCAFFOLD PROTEIN 1, MITOGEN-ACTIVATED PROTEIN KINASE 8-   
COMPND  17 INTERACTING PROTEIN 1;                                               
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAPK8, HCG_23734;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 OTHER_DETAILS: CHEMICAL SYNTHESIS                                    
KEYWDS    KINASE INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KUGLSTATTER,M.GHATE                                                 
REVDAT   1   30-OCT-13 4HYU    0                                                
JRNL        AUTH   W.S.PALMER,M.ALAM,H.B.ARZENO,K.C.CHANG,J.P.DUNN,             
JRNL        AUTH 2 D.M.GOLDSTEIN,L.GONG,B.GOYAL,J.C.HERMANN,J.H.HOGG,G.HSIEH,   
JRNL        AUTH 3 A.JAHANGIR,C.JANSON,S.JIN,R.URSULA KAMMLOTT,A.KUGLSTATTER,   
JRNL        AUTH 4 C.LUKACS,C.MICHOUD,L.NIU,D.C.REUTER,A.SHAO,T.SILVA,          
JRNL        AUTH 5 T.A.TREJO-MARTIN,K.STEIN,Y.C.TAN,P.TIVITMAHAISOON,P.TRAN,    
JRNL        AUTH 6 P.WAGNER,P.WELLER,S.Y.WU                                     
JRNL        TITL   DEVELOPMENT OF AMINO-PYRIMIDINE INHIBITORS OF C-JUN          
JRNL        TITL 2 N-TERMINAL KINASE (JNK): KINASE PROFILING GUIDED             
JRNL        TITL 3 OPTIMIZATION OF A 1,2,3-BENZOTRIAZOLE LEAD.                  
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  1486 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23352510                                                     
JRNL        DOI    10.1016/J.BMCL.2012.12.047                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 20592                          
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) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1109                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1046                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 57                           
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2674                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 76                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.02000                                             
REMARK   3    B22 (A**2) : 3.12000                                              
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): 0.277         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.220         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.167         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.368         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2766 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3738 ; 1.126 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   326 ; 5.834 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   123 ;37.633 ;24.309       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   504 ;16.151 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;14.178 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   412 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2047 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1201 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1878 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   105 ; 0.129 ; 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):    31 ; 0.269 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.196 ; 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):  1706 ; 0.592 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2682 ; 1.019 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1214 ; 1.322 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1056 ; 2.126 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER 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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB076090.                                      
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                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21746                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.44700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.740                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1UKH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M LISO4, 0.1 M BIS-    
REMARK 280  TRIS, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K       
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       30.21900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.25100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.88450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.25100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.21900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.88450            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     ARG A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     ALA A   173                                                      
REMARK 465     ARG A   174                                                      
REMARK 465     THR A   175                                                      
REMARK 465     ALA A   176                                                      
REMARK 465     GLY A   177                                                      
REMARK 465     THR A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     PHE A   180                                                      
REMARK 465     MET A   181                                                      
REMARK 465     MET A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     PRO A   184                                                      
REMARK 465     TYR A   185                                                      
REMARK 465     VAL A   186                                                      
REMARK 465     VAL A   187                                                      
REMARK 465     ALA A   282                                                      
REMARK 465     ASP A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     GLU A   285                                                      
REMARK 465     HIS A   286                                                      
REMARK 465     ASN A   287                                                      
REMARK 465     LYS A   288                                                      
REMARK 465     PRO A   335                                                      
REMARK 465     LYS A   336                                                      
REMARK 465     ILE A   337                                                      
REMARK 465     PRO A   338                                                      
REMARK 465     ASP A   339                                                      
REMARK 465     LYS A   340                                                      
REMARK 465     GLN A   341                                                      
REMARK 465     LEU A   342                                                      
REMARK 465     ASP A   343                                                      
REMARK 465     GLU A   344                                                      
REMARK 465     ASP A   362                                                      
REMARK 465     LEU A   363                                                      
REMARK 465     HIS A   364                                                      
REMARK 465     HIS A   365                                                      
REMARK 465     HIS A   366                                                      
REMARK 465     HIS A   367                                                      
REMARK 465     HIS A   368                                                      
REMARK 465     HIS A   369                                                      
REMARK 465     ARG B   153                                                      
REMARK 465     PHE B   163                                                      
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    GLN A 102      -42.63   -137.54                                   
REMARK 500    ARG A 150       -3.04     77.82                                   
REMARK 500    ASP A 151       33.81   -145.84                                   
REMARK 500    VAL A 278      -37.92    -39.76                                   
REMARK 500    GLU A 331       40.82   -140.16                                   
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 1BK A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4HYS   RELATED DB: PDB                                   
DBREF  4HYU A    1   363  UNP    A1L4K2   A1L4K2_HUMAN     1    363             
DBREF  4HYU B  153   163  UNP    Q9UQF2   JIP1_HUMAN     157    167             
SEQADV 4HYU HIS A  364  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 4HYU HIS A  365  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 4HYU HIS A  366  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 4HYU HIS A  367  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 4HYU HIS A  368  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 4HYU HIS A  369  UNP  A1L4K2              EXPRESSION TAG                 
SEQRES   1 A  369  MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL          
SEQRES   2 A  369  GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR          
SEQRES   3 A  369  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE          
SEQRES   4 A  369  VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL          
SEQRES   5 A  369  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR          
SEQRES   6 A  369  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS          
SEQRES   7 A  369  CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL          
SEQRES   8 A  369  PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL          
SEQRES   9 A  369  TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN          
SEQRES  10 A  369  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR          
SEQRES  11 A  369  LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS          
SEQRES  12 A  369  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN          
SEQRES  13 A  369  ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP          
SEQRES  14 A  369  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET          
SEQRES  15 A  369  THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU          
SEQRES  16 A  369  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE          
SEQRES  17 A  369  TRP SER VAL GLY CYS ILE MET GLY GLU MET ILE LYS GLY          
SEQRES  18 A  369  GLY VAL LEU PHE PRO GLY THR ASP HIS ILE ASP GLN TRP          
SEQRES  19 A  369  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU          
SEQRES  20 A  369  PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR VAL          
SEQRES  21 A  369  GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS          
SEQRES  22 A  369  LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS          
SEQRES  23 A  369  ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER          
SEQRES  24 A  369  LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL          
SEQRES  25 A  369  ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR          
SEQRES  26 A  369  ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO          
SEQRES  27 A  369  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU          
SEQRES  28 A  369  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU HIS          
SEQRES  29 A  369  HIS HIS HIS HIS HIS                                          
SEQRES   1 B   11  ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE                  
HET    1BK  A 401      31                                                       
HETNAM     1BK TRANS-4-[(4-{4-[3-(METHYLSULFONYL)PROPOXY]-1H-INDAZOL-           
HETNAM   2 1BK  1-YL}PYRIMIDIN-2-YL)AMINO]CYCLOHEXANOL                          
FORMUL   3  1BK    C21 H27 N5 O4 S                                              
FORMUL   4  HOH   *76(H2 O)                                                     
HELIX    1   1 ASN A   63  VAL A   80  1                                  18    
HELIX    2   2 LEU A  115  ILE A  119  1                                   5    
HELIX    3   3 ASP A  124  ALA A  145  1                                  22    
HELIX    4   4 LYS A  153  SER A  155  5                                   3    
HELIX    5   5 ALA A  193  LEU A  198  1                                   6    
HELIX    6   6 ASN A  205  GLY A  221  1                                  17    
HELIX    7   7 ASP A  229  GLY A  242  1                                  14    
HELIX    8   8 CYS A  245  LYS A  251  1                                   7    
HELIX    9   9 GLN A  253  GLU A  261  1                                   9    
HELIX   10  10 SER A  270  PHE A  275  1                                   6    
HELIX   11  11 PRO A  276  PHE A  280  5                                   5    
HELIX   12  12 LYS A  290  LEU A  302  1                                  13    
HELIX   13  13 ASP A  305  ARG A  309  5                                   5    
HELIX   14  14 SER A  311  HIS A  318  1                                   8    
HELIX   15  15 HIS A  318  VAL A  323  1                                   6    
HELIX   16  16 ASP A  326  GLU A  331  1                                   6    
HELIX   17  17 THR A  348  MET A  361  1                                  14    
SHEET    1   A 2 PHE A  10  ILE A  15  0                                        
SHEET    2   A 2 SER A  18  LEU A  23 -1  O  SER A  18   N  ILE A  15           
SHEET    1   B 5 TYR A  26  GLY A  35  0                                        
SHEET    2   B 5 GLY A  38  ASP A  45 -1  O  TYR A  44   N  GLN A  27           
SHEET    3   B 5 ARG A  50  LEU A  57 -1  O  ILE A  54   N  CYS A  41           
SHEET    4   B 5 TYR A 105  GLU A 109 -1  O  ILE A 106   N  LYS A  55           
SHEET    5   B 5 ASN A  90  PHE A  92 -1  N  ASN A  90   O  VAL A 107           
SHEET    1   C 3 ALA A 113  ASN A 114  0                                        
SHEET    2   C 3 ILE A 157  VAL A 159 -1  O  VAL A 159   N  ALA A 113           
SHEET    3   C 3 LEU A 165  ILE A 167 -1  O  LYS A 166   N  VAL A 158           
SITE     1 AC1 15 ILE A  32  SER A  34  GLY A  35  ALA A  36                    
SITE     2 AC1 15 GLN A  37  GLY A  38  VAL A  40  ALA A  53                    
SITE     3 AC1 15 LYS A  55  GLU A 109  MET A 111  LEU A 168                    
SITE     4 AC1 15 THR A 258  ASN A 262  HOH A 504                               
CRYST1   60.438   81.769   82.502  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      0.016546  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012230  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012121        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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