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Database: PDB
Entry: 3VUH
LinkDB: 3VUH
Original site: 3VUH 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       28-JUN-12   3VUH              
TITLE     CRYSTAL STRUCTURE OF A CYSTEINE-DEFICIENT MUTANT M3 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   2   04-DEC-19 3VUH    1       REMARK SEQADV                            
REVDAT   1   13-FEB-13 3VUH    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.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 16849                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 908                             
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1118                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.4240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2932                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 45                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.03000                                             
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): 0.424         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.298         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.223         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.952        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
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):  3022 ; 0.014 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4092 ; 2.493 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   362 ; 8.648 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   136 ;38.619 ;24.485       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   542 ;20.505 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;23.890 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   457 ; 0.281 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2240 ; 0.009 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 3VUH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000095514.                                   
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   : 17780                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
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     (%) : 99.6                               
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) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
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   (%): 65.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58                     
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: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       84.96450            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       84.96450            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       43.65750            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       84.96450            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       84.96450            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       43.65750            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       84.96450            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       84.96450            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       43.65750            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       84.96450            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       84.96450            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       43.65750            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       84.96450            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       84.96450            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       43.65750            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       84.96450            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       84.96450            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       43.65750            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       84.96450            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       84.96450            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       43.65750            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       84.96450            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       84.96450            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       43.65750            
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: 2230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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 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     PHE A   180                                                      
REMARK 465     MET A   181                                                      
REMARK 465     MET A   182                                                      
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: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O2   SO4 A   402     O3   SO4 A   402     6555     1.82            
REMARK 500   O4   SO4 A   402     O4   SO4 A   402     6555     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLN A 117   N   -  CA  -  C   ANGL. DEV. = -23.1 DEGREES          
REMARK 500    ASP A 151   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    MET A 301   CG  -  SD  -  CE  ANGL. DEV. = -13.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  59       68.37     18.88                                   
REMARK 500    GLN A  62       -6.86    -54.59                                   
REMARK 500    ASN A  63      144.49   -173.89                                   
REMARK 500    GLN A 102      -37.63   -141.84                                   
REMARK 500    GLN A 117      -42.56   -174.05                                   
REMARK 500    ARG A 150      -28.42     77.42                                   
REMARK 500    LYS A 153      156.49    173.92                                   
REMARK 500    ALA A 163        3.55     88.47                                   
REMARK 500    ASP A 169      107.19     44.38                                   
REMARK 500    ALA A 176      157.48    -45.45                                   
REMARK 500    THR A 178     -146.68    106.99                                   
REMARK 500    PRO A 226      -95.46    -49.28                                   
REMARK 500    GLU A 285      -72.24    -54.54                                   
REMARK 500    ASN A 287      -99.55     52.51                                   
REMARK 500    GLU A 331       42.25   -142.96                                   
REMARK 500    PRO A 338      107.89    -46.84                                   
REMARK 500    LYS A 340      -76.46    -43.37                                   
REMARK 500    ASP A 343       58.88    -61.37                                   
REMARK 500    GLU A 344      -45.92   -162.16                                   
REMARK 500    HIS A 347     -154.90   -141.75                                   
REMARK 500    ILE A 349      -50.06    -14.67                                   
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                  -60.68                    
REMARK 500 GLY A  177     THR A  178                 -148.00                    
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 SO4 A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
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: 3VUI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VUK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VUL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VUM   RELATED DB: PDB                                   
DBREF  3VUH A    1   364  UNP    A1L4K2   A1L4K2_HUMAN     1    364             
DBREF  3VUH F  553   563  UNP    Q9UQF2   JIP1_HUMAN     157    167             
SEQADV 3VUH SER A  116  UNP  A1L4K2    CYS   116 ENGINEERED MUTATION            
SEQADV 3VUH ALA A  163  UNP  A1L4K2    CYS   163 ENGINEERED MUTATION            
SEQADV 3VUH SER A  245  UNP  A1L4K2    CYS   245 ENGINEERED MUTATION            
SEQADV 3VUH HIS A  365  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 3VUH HIS A  366  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 3VUH HIS A  367  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 3VUH HIS A  368  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 3VUH HIS A  369  UNP  A1L4K2              EXPRESSION TAG                 
SEQADV 3VUH 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  CYS 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 CYS 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 CYS 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                  
HET    SO4  A 400       5                                                       
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    GOL  A 405       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   8  GOL    C3 H8 O3                                                     
FORMUL   9  HOH   *45(H2 O)                                                     
HELIX    1   1 PRO A   60  GLN A   62  5                                   3    
HELIX    2   2 ASN A   63  VAL A   80  1                                  18    
HELIX    3   3 SER A  116  VAL A  118  5                                   3    
HELIX    4   4 ASP A  124  ALA A  145  1                                  22    
HELIX    5   5 LYS A  153  SER A  155  5                                   3    
HELIX    6   6 THR A  188  ARG A  192  5                                   5    
HELIX    7   7 ALA A  193  LEU A  198  1                                   6    
HELIX    8   8 GLU A  204  GLY A  221  1                                  18    
HELIX    9   9 ILE A  231  GLY A  242  1                                  12    
HELIX   10  10 SER A  245  LYS A  250  1                                   6    
HELIX   11  11 GLN A  253  ARG A  263  1                                  11    
HELIX   12  12 SER A  270  PHE A  275  1                                   6    
HELIX   13  13 PRO A  276  PHE A  280  5                                   5    
HELIX   14  14 LYS A  290  LEU A  302  1                                  13    
HELIX   15  15 ASP A  305  ARG A  309  5                                   5    
HELIX   16  16 SER A  311  HIS A  318  1                                   8    
HELIX   17  17 HIS A  318  VAL A  323  1                                   6    
HELIX   18  18 ASP A  326  GLU A  331  1                                   6    
HELIX   19  19 THR A  348  GLU A  364  1                                  17    
SHEET    1   A 2 SER A  12  ILE A  15  0                                        
SHEET    2   A 2 SER A  18  THR A  21 -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  TYR A  44   N  GLN A  27           
SHEET    3   B 5 ARG A  50  SER A  58 -1  O  ILE A  54   N  CYS A  41           
SHEET    4   B 5 ASP A 103  MET A 108 -1  O  ILE A 106   N  LYS A  55           
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  5 ARG A 189  ARG A 192  HIS A 230  THR A 255                    
SITE     2 AC1  5 HOH A 533                                                     
SITE     1 AC2  3 LYS A 153  SER A 155  HOH A 508                               
SITE     1 AC3  1 ARG A 263                                                     
SITE     1 AC4  5 ARG A  69  ARG A  72  ARG A 150  ARG A 174                    
SITE     2 AC4  5 THR A 183                                                     
SITE     1 AC5  5 GLY A  38  LYS A  56  LEU A  57  SER A  58                    
SITE     2 AC5  5 HIS A  66                                                     
SITE     1 AC6  3 GLU A 109  LEU A 110  MET A 111                               
SITE     1 AC7 15 ILE A  15  ASP A  17  PRO A  31  GLY A  33                    
SITE     2 AC7 15 SER A  34  ILE A  39  VAL A  40  MET A 121                    
SITE     3 AC7 15 ARG A 127  TYR A 130  SER A 161  ASP A 162                    
SITE     4 AC7 15 ALA A 163  TRP A 324  GLU A 329                               
CRYST1  169.929  169.929   87.315  90.00  90.00  90.00 I 4 2 2      16          
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      0.005885  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005885  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011453        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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