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Database: PDB
Entry: 4E73
LinkDB: 4E73
Original site: 4E73 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       16-MAR-12   4E73              
TITLE     CRYSTAL STRUCTURE OF JNK1BETA-JIP IN COMPLEX WITH AN AZAQUINOLONE     
TITLE    2 INHBITOR                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAP KINASE 8, MAPK 8, JNK-46, STRESS-ACTIVATED PROTEIN      
COMPND   5 KINASE 1C, SAPK1C, STRESS-ACTIVATED PROTEIN KINASE JNK1, C-JUN N-    
COMPND   6 TERMINAL KINASE 1;                                                   
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1;         
COMPND  11 CHAIN: B;                                                            
COMPND  12 SYNONYM: JIP-1, JNK-INTERACTING PROTEIN 1, ISLET-BRAIN 1, IB-1, JNK  
COMPND  13 MAP KINASE SCAFFOLD PROTEIN 1, MITOGEN-ACTIVATED PROTEIN KINASE 8-   
COMPND  14 INTERACTING PROTEIN 1;                                               
COMPND  15 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, JNK1, PRKM8, SAPK1, SAPK1C;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.LUKACS,C.A.JANSON                                                 
REVDAT   2   24-SEP-14 4E73    1       JRNL                                     
REVDAT   1   29-MAY-13 4E73    0                                                
JRNL        AUTH   N.E.HAYNES,N.R.SCOTT,L.C.CHEN,C.A.JANSON,J.K.LI,C.M.LUKACS,  
JRNL        AUTH 2 A.RAILKAR,E.TOZZO,T.WHITTARD,N.F.BROWN,A.W.CHEUNG            
JRNL        TITL   IDENTIFICATION OF AN ADAMANTYL AZAQUINOLONE JNK SELECTIVE    
JRNL        TITL 2 INHIBITOR.                                                   
JRNL        REF    ACS MED CHEM LETT             V.   3   764 2012              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   24900545                                                     
JRNL        DOI    10.1021/ML300175C                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2005                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1131880.990                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 20301                          
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) : 0.249                           
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1035                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : 0.2510               
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : 0.2490               
REMARK   3   FREE R VALUE                    (NO CUTOFF) : 0.283                
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : 5.100                
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : 1035                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0090               
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 20301                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.27                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3180                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3040                       
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 175                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2645                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.25                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.28000                                              
REMARK   3    B22 (A**2) : -4.23000                                             
REMARK   3    B33 (A**2) : 3.95000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.29                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.35                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.900                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.650                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.650 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.790 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.110 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.110 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 64.55                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARA                               
REMARK   3  PARAMETER FILE  2  : LIG.PAR                                        
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : LIG.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4E73 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071251.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20514                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.04200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1UKH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13-16% PEG 3350, 0.1M ADA PH 6.0, 10     
REMARK 280  MM DTT, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K             
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       31.45050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.76200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.92000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.76200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.45050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.92000            
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: 1180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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     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     THR A   188                                                      
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     LEU A   289                                                      
REMARK 465     ALA A   332                                                      
REMARK 465     PRO A   333                                                      
REMARK 465     PRO A   334                                                      
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     LYS 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    ARG A  59       69.00     35.26                                   
REMARK 500    HIS A  82      144.12   -171.15                                   
REMARK 500    PHE A 101      116.20    -37.29                                   
REMARK 500    GLN A 102      -55.63   -124.35                                   
REMARK 500    MET A 111     -159.20   -104.55                                   
REMARK 500    ARG A 150       -5.48     71.21                                   
REMARK 500    ILE A 219      -60.91    -97.78                                   
REMARK 500    PRO A 246      -83.30    -46.44                                   
REMARK 500    GLU A 247       37.89     34.87                                   
REMARK 500    PHE A 248      -51.05    158.41                                   
REMARK 500    ARG A 263      151.18    -45.54                                   
REMARK 500    ALA A 291      -74.54     42.71                                   
REMARK 500    LYS B 155       97.82     47.35                                   
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 PRO A  246     GLU A  247                  102.42                    
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 584        DISTANCE =  5.35 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0NR A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UKH   RELATED DB: PDB                                   
DBREF  4E73 A    1   363  UNP    P45983   MK08_HUMAN       1    363             
DBREF  4E73 B  153   163  UNP    Q9UQF2   JIP1_HUMAN     157    167             
SEQADV 4E73 HIS A  364  UNP  P45983              EXPRESSION TAG                 
SEQADV 4E73 HIS A  365  UNP  P45983              EXPRESSION TAG                 
SEQADV 4E73 HIS A  366  UNP  P45983              EXPRESSION TAG                 
SEQADV 4E73 HIS A  367  UNP  P45983              EXPRESSION TAG                 
SEQADV 4E73 HIS A  368  UNP  P45983              EXPRESSION TAG                 
SEQADV 4E73 HIS A  369  UNP  P45983              EXPRESSION TAG                 
SEQADV 4E73 LYS B  153  UNP  Q9UQF2    ARG   157 CONFLICT                       
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  LYS PRO LYS ARG PRO THR THR LEU ASN LEU PHE                  
HET    0NR  A 401      42                                                       
HETNAM     0NR METHYL 3-(4-{[(1R,2S,3S,5S,7S)-5-                                
HETNAM   2 0NR  AMINOTRICYCLO[3.3.1.1~3,7~]DEC-2-YL]CARBAMOYL}BENZYL)-          
HETNAM   3 0NR  4-OXO-1-PHENYL-1,4-DIHYDRO-1,8-NAPHTHYRIDINE-2-                 
HETNAM   4 0NR  CARBOXYLATE                                                     
FORMUL   3  0NR    C34 H34 N4 O4                                                
FORMUL   4  HOH   *89(H2 O)                                                     
HELIX    1   1 ASN A   63  VAL A   80  1                                  18    
HELIX    2   2 LEU A  115  GLN A  120  1                                   6    
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  250  1                                   6    
HELIX    9   9 GLN A  253  ARG A  263  1                                  11    
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 ALA A  291  LEU A  302  1                                  12    
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 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  ALA A  42   N  LYS A  30           
SHEET    3   B 5 ARG A  50  LEU A  57 -1  O  VAL A  52   N  ALA A  43           
SHEET    4   B 5 TYR A 105  GLU A 109 -1  O  MET A 108   N  ALA A  53           
SHEET    5   B 5 LEU A  88  PHE A  92 -1  N  LEU A  89   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 17 ILE A  32  GLY A  33  VAL A  40  ALA A  42                    
SITE     2 AC1 17 ALA A  53  MET A 108  GLU A 109  MET A 111                    
SITE     3 AC1 17 ASP A 112  ALA A 113  ASN A 114  VAL A 158                    
SITE     4 AC1 17 LEU A 168  ASN A 262  HOH A 518  HOH A 573                    
SITE     5 AC1 17 HOH A 577                                                     
CRYST1   62.901   79.840   85.524  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      0.015898  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012525  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011693        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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