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Database: PDB
Entry: 3VUL
LinkDB: 3VUL
Original site: 3VUL 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       02-JUL-12   3VUL              
TITLE     CRYSTAL STRUCTURE OF A CYSTEINE-DEFICIENT MUTANT M1 IN MAP KINASE JNK1
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 1-364;                         
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: 2.7.11.24;                                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES;                                                       
COMPND  12 MOL_ID: 2;                                                           
COMPND  13 MOLECULE: PEPTIDE FROM C-JUN-AMINO-TERMINAL KINASE-INTERACTING       
COMPND  14 PROTEIN 1;                                                           
COMPND  15 CHAIN: F;                                                            
COMPND  16 SYNONYM: JIP-1, JNK-INTERACTING PROTEIN 1, ISLET-BRAIN 1, IB-1, JNK  
COMPND  17 MAP KINASE SCAFFOLD PROTEIN 1, MITOGEN-ACTIVATED PROTEIN KINASE 8-   
COMPND  18 INTERACTING PROTEIN 1;                                               
COMPND  19 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;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET24A;                                   
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    TRANSCRIPTION, PHOSPHORYLATION, ATP BINDING, TRANSFERASE-TRANSFERASE  
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.NAKANIWA,T.KINOSHITA,T.INOUE                                        
REVDAT   1   13-FEB-13 3VUL    0                                                
JRNL        AUTH   T.NAKANIWA,H.FUKADA,T.INOUE,M.GOUDA,R.NAKAI,Y.KIRII,         
JRNL        AUTH 2 M.ADACHI,T.TAMADA,S.SEGAWA,R.KUROKI,T.TADA,T.KINOSHITA       
JRNL        TITL   SEVEN CYSTEINE-DEFICIENT MUTANTS DEPICT THE INTERPLAY        
JRNL        TITL 2 BETWEEN THERMAL AND CHEMICAL STABILITIES OF INDIVIDUAL       
JRNL        TITL 3 CYSTEINE RESIDUES IN MITOGEN-ACTIVATED PROTEIN KINASE C-JUN  
JRNL        TITL 4 N-TERMINAL KINASE 1                                          
JRNL        REF    BIOCHEMISTRY                  V.  51  8410 2012              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   23020677                                                     
JRNL        DOI    10.1021/BI300918W                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
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) : 2.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 15954                          
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) : 0.252                           
REMARK   3   R VALUE            (WORKING SET) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.315                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 853                             
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) : 2.81                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.88                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1124                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 64                           
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2859                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 37                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.03000                                              
REMARK   3    B12 (A**2) : -0.01000                                             
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): 0.582         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.385         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.312         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.437        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.907                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.858                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2922 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3953 ; 1.858 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   351 ; 8.296 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   135 ;39.824 ;24.519       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   534 ;23.852 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;20.582 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   438 ; 0.133 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2184 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1771 ; 1.019 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2876 ; 1.934 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1151 ; 2.217 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1077 ; 3.857 ; 4.500       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3VUL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB095518.                                      
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                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NE3A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16976                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2M AMMONIUM SULFATE, 0.2M SODIUM       
REMARK 280  CHLORIDE, 0.1M SODIUM CACODYLATE PH 6.5 , VAPOR DIFFUSION,          
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       43.86250            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       43.86250            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       43.86250            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       43.86250            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       43.86250            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       43.86250            
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: 1220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 426  LIES ON A SPECIAL POSITION.                          
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     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     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     HIS A   370                                                      
REMARK 465     ARG F   553                                                      
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     GLU A 346    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 358    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A  41   CB    CYS A  41   SG     -0.101                       
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    ASN A   9      -31.38     86.14                                   
REMARK 500    TYR A  11      171.32    179.72                                   
REMARK 500    ALA A  36      -78.15     38.47                                   
REMARK 500    GLN A  37       51.03   -109.42                                   
REMARK 500    ARG A  59       72.00     13.41                                   
REMARK 500    GLN A  62      -52.07    -28.89                                   
REMARK 500    THR A  65      -77.54    -49.48                                   
REMARK 500    LYS A  78      -70.43    -65.14                                   
REMARK 500    HIS A  82      147.16   -171.94                                   
REMARK 500    ILE A  86      128.89    -38.24                                   
REMARK 500    ASN A  90      141.66   -174.23                                   
REMARK 500    GLN A 102      -31.82   -138.36                                   
REMARK 500    GLN A 117      -59.45    146.44                                   
REMARK 500    GLU A 122       79.72   -109.00                                   
REMARK 500    ARG A 150      -14.75     61.80                                   
REMARK 500    ASP A 169      126.64     85.46                                   
REMARK 500    PHE A 170        1.53   -150.76                                   
REMARK 500    LEU A 172      -31.35   -156.52                                   
REMARK 500    PRO A 226       73.44    -52.23                                   
REMARK 500    HIS A 230       23.04    -78.06                                   
REMARK 500    ILE A 231       -1.47   -145.32                                   
REMARK 500    GLU A 247       29.46    -75.94                                   
REMARK 500    LYS A 251      -17.09    -41.62                                   
REMARK 500    ARG A 263      148.81    -37.18                                   
REMARK 500    ASP A 277      -54.21    -27.20                                   
REMARK 500    ASN A 287      -59.32    -22.98                                   
REMARK 500    LEU A 302       38.40    -75.66                                   
REMARK 500    ILE A 310      144.94    -38.51                                   
REMARK 500    ASP A 339      -13.57     40.53                                   
REMARK 500    LEU A 342       54.49   -173.61                                   
REMARK 500    ASP A 343       72.28      4.59                                   
REMARK 500    LEU F 562       79.81   -100.76                                   
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 SER A  116     GLN A  117                  -33.95                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER A 116        21.0      L          L   OUTSIDE RANGE           
REMARK 500    LYS F 555        23.9      L          L   OUTSIDE RANGE           
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 CHAIN F OF PEPTIDE FROM C-JUN-    
REMARK 800  AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VUD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VUG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VUH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VUI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VUK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VUM   RELATED DB: PDB                                   
DBREF  3VUL A    1   364  UNP    A1L4K2   A1L4K2_HUMAN     1    364             
DBREF  3VUL F  553   563  UNP    Q9UQF2   JIP1_HUMAN     157    167             
SEQADV 3VUL VAL A   79  UNP  A1L4K2    CYS    79 ENGINEERED MUTATION            
SEQADV 3VUL SER A  116  UNP  A1L4K2    CYS   116 ENGINEERED MUTATION            
SEQADV 3VUL VAL A  137  UNP  A1L4K2    CYS   137 ENGINEERED MUTATION            
SEQADV 3VUL ALA A  163  UNP  A1L4K2    CYS   163 ENGINEERED MUTATION            
SEQADV 3VUL VAL A  213  UNP  A1L4K2    CYS   213 ENGINEERED MUTATION            
SEQADV 3VUL SER A  245  UNP  A1L4K2    CYS   245 ENGINEERED MUTATION            
SEQADV 3VUL HIS A  365  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 3VUL HIS A  366  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 3VUL HIS A  367  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 3VUL HIS A  368  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 3VUL HIS A  369  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 3VUL HIS A  370  UNP  A1L4K2              EXPRESSION TAG                 
SEQRES   1 A  370  MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL          
SEQRES   2 A  370  GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR          
SEQRES   3 A  370  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE          
SEQRES   4 A  370  VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL          
SEQRES   5 A  370  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR          
SEQRES   6 A  370  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS          
SEQRES   7 A  370  VAL VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL          
SEQRES   8 A  370  PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL          
SEQRES   9 A  370  TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU SER GLN          
SEQRES  10 A  370  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR          
SEQRES  11 A  370  LEU LEU TYR GLN MET LEU VAL GLY ILE LYS HIS LEU HIS          
SEQRES  12 A  370  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN          
SEQRES  13 A  370  ILE VAL VAL LYS SER ASP ALA THR LEU LYS ILE LEU ASP          
SEQRES  14 A  370  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET          
SEQRES  15 A  370  THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU          
SEQRES  16 A  370  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE          
SEQRES  17 A  370  TRP SER VAL GLY VAL ILE MET GLY GLU MET ILE LYS GLY          
SEQRES  18 A  370  GLY VAL LEU PHE PRO GLY THR ASP HIS ILE ASP GLN TRP          
SEQRES  19 A  370  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO SER PRO GLU          
SEQRES  20 A  370  PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR VAL          
SEQRES  21 A  370  GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS          
SEQRES  22 A  370  LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS          
SEQRES  23 A  370  ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER          
SEQRES  24 A  370  LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL          
SEQRES  25 A  370  ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR          
SEQRES  26 A  370  ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO          
SEQRES  27 A  370  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU          
SEQRES  28 A  370  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU GLU          
SEQRES  29 A  370  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 F   11  ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE                  
FORMUL   3  HOH   *37(H2 O)                                                     
HELIX    1   1 ASN A   63  VAL A   80  1                                  18    
HELIX    2   2 ASP A  124  ALA A  145  1                                  22    
HELIX    3   3 LYS A  153  SER A  155  5                                   3    
HELIX    4   4 ALA A  193  LEU A  198  1                                   6    
HELIX    5   5 ASN A  205  GLY A  221  1                                  17    
HELIX    6   6 ILE A  231  GLY A  242  1                                  12    
HELIX    7   7 SER A  245  LYS A  250  1                                   6    
HELIX    8   8 GLN A  253  ARG A  263  1                                  11    
HELIX    9   9 SER A  270  PHE A  275  1                                   6    
HELIX   10  10 PRO A  276  PHE A  280  5                                   5    
HELIX   11  11 LYS A  290  LEU A  302  1                                  13    
HELIX   12  12 ASP A  305  ARG A  309  5                                   5    
HELIX   13  13 SER A  311  HIS A  318  1                                   8    
HELIX   14  14 ILE A  321  TYR A  325  5                                   5    
HELIX   15  15 ASP A  326  GLU A  331  1                                   6    
HELIX   16  16 THR A  348  LEU A  363  1                                  16    
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  SER A  34  0                                        
SHEET    2   B 5 ILE A  39  ASP A  45 -1  O  ALA A  42   N  LYS A  30           
SHEET    3   B 5 ARG A  50  LEU A  57 -1  O  ILE A  54   N  CYS A  41           
SHEET    4   B 5 VAL A 104  GLU A 109 -1  O  ILE A 106   N  LYS A  55           
SHEET    5   B 5 LEU A  88  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 16 GLY A  16  ASP A  17  GLY A  33  SER A  34                    
SITE     2 AC1 16 ASP A 112  MET A 121  ARG A 127  TYR A 130                    
SITE     3 AC1 16 TYR A 133  LYS A 160  SER A 161  ASP A 162                    
SITE     4 AC1 16 HIS A 286  TRP A 324  GLU A 329  HOH F 601                    
CRYST1  161.781  161.781   87.725  90.00  90.00 120.00 P 63 2 2     12          
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      0.006181  0.003569  0.000000        0.00000                         
SCALE2      0.000000  0.007137  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011399        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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