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Database: PDB
Entry: 6F5E
LinkDB: 6F5E
Original site: 6F5E 
HEADER    DE NOVO PROTEIN                         01-DEC-17   6F5E              
TITLE     CRYSTAL STRUCTURE OF DARPIN-DARPIN RIGID FUSION, VARIANT DD_D12_10_47 
TITLE    2 IN COMPLEX JNK1A1 AND JIP1 PEPTIDE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DD_D12_10_47;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;                        
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: MAPK 8,JNK-46,STRESS-ACTIVATED PROTEIN KINASE 1C,SAPK1C,    
COMPND   9 STRESS-ACTIVATED PROTEIN KINASE JNK1,C-JUN N-TERMINAL KINASE 1;      
COMPND  10 EC: 2.7.11.24;                                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1;         
COMPND  14 CHAIN: C;                                                            
COMPND  15 SYNONYM: JNK-INTERACTING PROTEIN 1,ISLET-BRAIN-1,IB-1,JNK MAP KINASE 
COMPND  16 SCAFFOLD PROTEIN 1,MITOGEN-ACTIVATED PROTEIN KINASE 8-INTERACTING    
COMPND  17 PROTEIN 1;                                                           
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE   3 ORGANISM_TAXID: 32630;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   6 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE;                                 
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: MAPK8, JNK1, PRKM8, SAPK1, SAPK1C;                             
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE  14 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE;                                 
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  18 ORGANISM_COMMON: MOUSE;                                              
SOURCE  19 ORGANISM_TAXID: 10090                                                
KEYWDS    X-RAY CRYSTALLOGRAPHY; DESIGNED ANKYRIN REPEAT PROTEINS; PROTEIN      
KEYWDS   2 DESIGN; PROTEIN ENGINEERING; RIGID DOMAIN FUSIONS, TRANSFERASE, DE   
KEYWDS   3 NOVO PROTEIN                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.WU,P.R.MITTL,A.HONEGGER,A.BATYUK,A.PLUECKTHUN                       
REVDAT   1   13-DEC-17 6F5E    0                                                
SPRSDE     13-DEC-17 6F5E      5LEN                                             
JRNL        AUTH   Y.WU,P.R.MITTL,A.HONEGGER,A.BATYUK,A.PLUECKTHUN              
JRNL        TITL   CRYSTAL STRUCTURE OF DARPIN-DARPIN RIGID FUSION, VARIANT     
JRNL        TITL 2 DD_D12_10_47 IN COMPLEX JNK1A1 AND JIP1 PEPTIDE              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 30221                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1528                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.9665 -  6.0011    1.00     2608   157  0.1602 0.1728        
REMARK   3     2  6.0011 -  4.7647    1.00     2622   129  0.1917 0.2114        
REMARK   3     3  4.7647 -  4.1629    1.00     2629   136  0.1750 0.2056        
REMARK   3     4  4.1629 -  3.7824    1.00     2620   145  0.1968 0.2434        
REMARK   3     5  3.7824 -  3.5114    1.00     2569   128  0.2304 0.2590        
REMARK   3     6  3.5114 -  3.3044    1.00     2635   160  0.2436 0.3192        
REMARK   3     7  3.3044 -  3.1390    0.99     2601   133  0.2587 0.2672        
REMARK   3     8  3.1390 -  3.0024    0.99     2579   150  0.2976 0.3898        
REMARK   3     9  3.0024 -  2.8868    0.99     2624   123  0.3439 0.3496        
REMARK   3    10  2.8868 -  2.7872    1.00     2599   125  0.3525 0.4086        
REMARK   3    11  2.7872 -  2.7001    0.99     2607   142  0.3747 0.4116        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.480           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           5385                                  
REMARK   3   ANGLE     :  0.463           7298                                  
REMARK   3   CHIRALITY :  0.037            831                                  
REMARK   3   PLANARITY :  0.002            940                                  
REMARK   3   DIHEDRAL  : 11.973           3252                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 180 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  90.8249  54.8275  66.1711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8800 T22:   1.6965                                     
REMARK   3      T33:   1.2623 T12:   0.3135                                     
REMARK   3      T13:  -0.0646 T23:   0.0809                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2956 L22:   2.5084                                     
REMARK   3      L33:   5.4356 L12:   1.0924                                     
REMARK   3      L13:  -1.0847 L23:  -0.8069                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2432 S12:  -0.5249 S13:  -0.1532                       
REMARK   3      S21:   0.1041 S22:   0.1242 S23:   0.4673                       
REMARK   3      S31:   0.0421 S32:  -0.9025 S33:   0.0644                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 325 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  92.6240  53.8949  27.3860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7129 T22:   1.8993                                     
REMARK   3      T33:   1.1221 T12:  -0.1609                                     
REMARK   3      T13:   0.0017 T23:   0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5176 L22:   2.7825                                     
REMARK   3      L33:   6.9245 L12:   0.5530                                     
REMARK   3      L13:   2.5615 L23:   1.3758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3993 S12:   1.4144 S13:  -0.0976                       
REMARK   3      S21:  -0.2429 S22:   0.4756 S23:  -0.0435                       
REMARK   3      S31:   0.1623 S32:   0.2082 S33:  -0.0652                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 7 THROUGH 164 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  56.2847  65.6347   9.1709              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9015 T22:   1.3194                                     
REMARK   3      T33:   1.1171 T12:  -0.4961                                     
REMARK   3      T13:  -0.0430 T23:   0.1745                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4789 L22:   2.2937                                     
REMARK   3      L33:   5.2998 L12:  -0.3031                                     
REMARK   3      L13:   2.0693 L23:   0.7034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1313 S12:   0.6642 S13:   0.3635                       
REMARK   3      S21:  -0.8010 S22:   0.1381 S23:   0.0517                       
REMARK   3      S31:  -0.7628 S32:   1.0748 S33:  -0.0439                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 165 THROUGH 335 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  65.2545  65.3300  33.7727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8486 T22:   1.1844                                     
REMARK   3      T33:   0.9505 T12:  -0.3802                                     
REMARK   3      T13:  -0.0221 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9940 L22:   1.3733                                     
REMARK   3      L33:   3.0546 L12:  -1.1744                                     
REMARK   3      L13:   0.9244 L23:  -0.8861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3383 S12:  -0.2889 S13:   0.2854                       
REMARK   3      S21:   0.1655 S22:   0.2024 S23:  -0.1538                       
REMARK   3      S31:  -0.2691 S32:   0.4163 S33:   0.1309                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 336 THROUGH 362 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  62.2051  47.2164   3.8551              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1652 T22:   1.4724                                     
REMARK   3      T33:   1.3742 T12:  -0.2663                                     
REMARK   3      T13:  -0.0662 T23:  -0.0915                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4131 L22:   3.6822                                     
REMARK   3      L33:   6.6848 L12:  -2.4928                                     
REMARK   3      L13:  -3.9648 L23:   2.5503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4419 S12:   1.0992 S13:  -0.7465                       
REMARK   3      S21:  -0.7660 S22:  -0.1353 S23:  -0.3177                       
REMARK   3      S31:   1.3075 S32:   0.2595 S33:   0.3315                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 154 THROUGH 163 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  46.4013  78.6597  24.6974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0936 T22:   1.4169                                     
REMARK   3      T33:   1.4596 T12:  -0.0627                                     
REMARK   3      T13:  -0.2039 T23:  -0.0477                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3973 L22:   9.6878                                     
REMARK   3      L33:   9.9817 L12:  -1.9193                                     
REMARK   3      L13:  -1.2196 L23:  -6.2570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3018 S12:   0.1873 S13:   0.7039                       
REMARK   3      S21:  -0.0393 S22:   0.1108 S23:   0.8142                       
REMARK   3      S31:  -0.7991 S32:   0.8124 S33:  -0.4271                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6F5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007772.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30294                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.959                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 41.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.9900                            
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     (%) : 100.0                              
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         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10000 3% W/V HEPES 0.1 M, PH 6.8     
REMARK 280  ADDITIVES (0.033% W/V) 1,5-NAPHTHALENE- DISULFONIC ACID DISODIUM    
REMARK 280  SALT 2,5-PYRIDINEDICARBOXYLIC ACID 3,5-DINITROSALICYLIC ACID,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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      220.48333            
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      110.24167            
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      165.36250            
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       55.12083            
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      275.60417            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     ARG A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     MET B    -9                                                      
REMARK 465     ARG B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     SER B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     GLY B    33                                                      
REMARK 465     SER B    34                                                      
REMARK 465     GLY B    35                                                      
REMARK 465     ALA B    36                                                      
REMARK 465     GLN B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     MET B   182                                                      
REMARK 465     THR B   183                                                      
REMARK 465     PRO B   184                                                      
REMARK 465     TYR B   185                                                      
REMARK 465     LEU B   363                                                      
REMARK 465     ARG C   153                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    PHE B   225    HE22  GLN B   233              1.60            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  77     -166.88   -123.19                                   
REMARK 500    ALA A 180       34.46   -158.13                                   
REMARK 500    ASN A 230       41.60   -108.60                                   
REMARK 500    ASN B   9       32.23    -87.52                                   
REMARK 500    ASN B  28       71.15     59.20                                   
REMARK 500    GLN B 102      -64.83   -141.20                                   
REMARK 500    ASP B 151       42.37   -157.58                                   
REMARK 500    SER B 179      -71.56    -72.34                                   
REMARK 500    LYS B 203     -169.89   -116.75                                   
REMARK 500    ASP B 283       57.94   -150.51                                   
REMARK 500    SER B 284      161.03    176.89                                   
REMARK 500    GLU B 344       38.35    -83.50                                   
REMARK 500    LEU C 160      106.01   -161.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6F5E A    1   325  PDB    6F5E     6F5E             1    325             
DBREF  6F5E B    2   363  UNP    P45983   MK08_HUMAN       2    363             
DBREF  6F5E C  153   163  UNP    Q9WVI9   JIP1_MOUSE     153    163             
SEQADV 6F5E MET B   -9  UNP  P45983              INITIATING METHIONINE          
SEQADV 6F5E ARG B   -8  UNP  P45983              EXPRESSION TAG                 
SEQADV 6F5E GLY B   -7  UNP  P45983              EXPRESSION TAG                 
SEQADV 6F5E SER B   -6  UNP  P45983              EXPRESSION TAG                 
SEQADV 6F5E HIS B   -5  UNP  P45983              EXPRESSION TAG                 
SEQADV 6F5E HIS B   -4  UNP  P45983              EXPRESSION TAG                 
SEQADV 6F5E HIS B   -3  UNP  P45983              EXPRESSION TAG                 
SEQADV 6F5E HIS B   -2  UNP  P45983              EXPRESSION TAG                 
SEQADV 6F5E HIS B   -1  UNP  P45983              EXPRESSION TAG                 
SEQADV 6F5E HIS B    0  UNP  P45983              EXPRESSION TAG                 
SEQADV 6F5E GLY B    1  UNP  P45983              EXPRESSION TAG                 
SEQRES   1 A  325  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 A  325  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 A  325  ASP ASP GLU VAL ARG ILE LEU LEU ALA ASN GLY ALA ASP          
SEQRES   4 A  325  VAL ASN THR ALA ASP GLU THR GLY PHE THR PRO LEU HIS          
SEQRES   5 A  325  LEU ALA ALA TRP GLU GLY HIS LEU GLY ILE VAL GLU VAL          
SEQRES   6 A  325  LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA ASN ASP GLU          
SEQRES   7 A  325  ARG GLY HIS THR PRO LEU HIS LEU ALA ALA TYR THR GLY          
SEQRES   8 A  325  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS ASN GLY ALA          
SEQRES   9 A  325  GLY VAL ASN ALA THR ASP VAL ILE GLY THR ALA PRO LEU          
SEQRES  10 A  325  HIS LEU ALA ALA MET TRP GLY HIS LEU GLU ILE VAL GLU          
SEQRES  11 A  325  VAL LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA GLN ASP          
SEQRES  12 A  325  LYS PHE GLY LYS THR PRO TYR ASP LEU ALA THR ASP ASN          
SEQRES  13 A  325  GLY ASN GLN TRP ILE ALA GLU LEU LEU LYS ARG ALA ALA          
SEQRES  14 A  325  LEU ARG ARG LYS LEU LEU GLU ALA ALA ARG ALA GLY HIS          
SEQRES  15 A  325  ARG ASP GLU VAL GLU ASP LEU ILE LYS ASN GLY ALA ASP          
SEQRES  16 A  325  VAL ASN ALA ILE ASP ALA MET GLY LEU THR PRO LEU HIS          
SEQRES  17 A  325  LEU ALA ALA MET ARG GLY HIS LEU GLU ILE VAL GLU VAL          
SEQRES  18 A  325  LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLU ASP TYR          
SEQRES  19 A  325  TYR GLY THR THR PRO LEU ARG LEU ALA ALA TYR ILE GLY          
SEQRES  20 A  325  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA          
SEQRES  21 A  325  ASP VAL ASN ALA TYR ASP ILE SER GLY THR THR PRO LEU          
SEQRES  22 A  325  HIS LEU ALA ALA VAL LEU GLY HIS LEU GLU ILE VAL GLU          
SEQRES  23 A  325  VAL LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLN ASP          
SEQRES  24 A  325  LYS PHE GLY LYS THR ALA PHE ASP ILE SER ILE ASP ASN          
SEQRES  25 A  325  GLY ASN GLU ASP LEU ALA GLU ILE LEU GLN LYS LEU ASN          
SEQRES   1 B  373  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ARG          
SEQRES   2 B  373  SER LYS ARG ASP ASN ASN PHE TYR SER VAL GLU ILE GLY          
SEQRES   3 B  373  ASP SER THR PHE THR VAL LEU LYS ARG TYR GLN ASN LEU          
SEQRES   4 B  373  LYS PRO ILE GLY SER GLY ALA GLN GLY ILE VAL CYS ALA          
SEQRES   5 B  373  ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL ALA ILE LYS          
SEQRES   6 B  373  LYS LEU SER ARG PRO PHE GLN ASN GLN THR HIS ALA LYS          
SEQRES   7 B  373  ARG ALA TYR ARG GLU LEU VAL LEU MET LYS CYS VAL ASN          
SEQRES   8 B  373  HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL PHE THR PRO          
SEQRES   9 B  373  GLN LYS SER LEU GLU GLU PHE GLN ASP VAL TYR ILE VAL          
SEQRES  10 B  373  MET GLU LEU MET ASP ALA ASN LEU CYS GLN VAL ILE GLN          
SEQRES  11 B  373  MET GLU LEU ASP HIS GLU ARG MET SER TYR LEU LEU TYR          
SEQRES  12 B  373  GLN MET LEU CYS GLY ILE LYS HIS LEU HIS SER ALA GLY          
SEQRES  13 B  373  ILE ILE HIS ARG ASP LEU LYS PRO SER ASN ILE VAL VAL          
SEQRES  14 B  373  LYS SER ASP CYS THR LEU LYS ILE LEU ASP PHE GLY LEU          
SEQRES  15 B  373  ALA ARG THR ALA GLY THR SER PHE MET MET THR PRO TYR          
SEQRES  16 B  373  VAL VAL THR ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU          
SEQRES  17 B  373  GLY MET GLY TYR LYS GLU ASN VAL ASP LEU TRP SER VAL          
SEQRES  18 B  373  GLY CYS ILE MET GLY GLU MET VAL CYS HIS LYS ILE LEU          
SEQRES  19 B  373  PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL          
SEQRES  20 B  373  ILE GLU GLN LEU GLY THR PRO CYS PRO GLU PHE MET LYS          
SEQRES  21 B  373  LYS LEU GLN PRO THR VAL ARG THR TYR VAL GLU ASN ARG          
SEQRES  22 B  373  PRO LYS TYR ALA GLY TYR SER PHE GLU LYS LEU PHE PRO          
SEQRES  23 B  373  ASP VAL LEU PHE PRO ALA ASP SER GLU HIS ASN LYS LEU          
SEQRES  24 B  373  LYS ALA SER GLN ALA ARG ASP LEU LEU SER LYS MET LEU          
SEQRES  25 B  373  VAL ILE ASP ALA SER LYS ARG ILE SER VAL ASP GLU ALA          
SEQRES  26 B  373  LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR ASP PRO SER          
SEQRES  27 B  373  GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO ASP LYS GLN          
SEQRES  28 B  373  LEU ASP GLU ARG GLU HIS THR ILE GLU GLU TRP LYS GLU          
SEQRES  29 B  373  LEU ILE TYR LYS GLU VAL MET ASP LEU                          
SEQRES   1 C   11  ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE                  
HELIX    1 AA1 SER A   12  GLY A   25  1                                  14    
HELIX    2 AA2 GLN A   26  GLY A   37  1                                  12    
HELIX    3 AA3 THR A   49  GLY A   58  1                                  10    
HELIX    4 AA4 HIS A   59  ASN A   69  1                                  11    
HELIX    5 AA5 THR A   82  GLY A   91  1                                  10    
HELIX    6 AA6 HIS A   92  ASN A  102  1                                  11    
HELIX    7 AA7 ALA A  115  TRP A  123  1                                   9    
HELIX    8 AA8 HIS A  125  ASN A  135  1                                  11    
HELIX    9 AA9 THR A  148  ASN A  156  1                                   9    
HELIX   10 AB1 ASN A  158  GLY A  181  1                                  24    
HELIX   11 AB2 HIS A  182  ASN A  192  1                                  11    
HELIX   12 AB3 THR A  205  GLY A  214  1                                  10    
HELIX   13 AB4 HIS A  215  TYR A  225  1                                  11    
HELIX   14 AB5 THR A  238  GLY A  247  1                                  10    
HELIX   15 AB6 HIS A  248  TYR A  258  1                                  11    
HELIX   16 AB7 THR A  271  GLY A  280  1                                  10    
HELIX   17 AB8 HIS A  281  TYR A  291  1                                  11    
HELIX   18 AB9 THR A  304  ASN A  312  1                                   9    
HELIX   19 AC1 ASN A  314  ASN A  325  1                                  12    
HELIX   20 AC2 PRO B   60  GLN B   62  5                                   3    
HELIX   21 AC3 ASN B   63  VAL B   80  1                                  18    
HELIX   22 AC4 LEU B  115  ILE B  119  1                                   5    
HELIX   23 AC5 ASP B  124  ALA B  145  1                                  22    
HELIX   24 AC6 LYS B  153  SER B  155  5                                   3    
HELIX   25 AC7 THR B  188  ARG B  192  5                                   5    
HELIX   26 AC8 ALA B  193  LEU B  198  1                                   6    
HELIX   27 AC9 ASN B  205  HIS B  221  1                                  17    
HELIX   28 AD1 ASP B  229  GLY B  242  1                                  14    
HELIX   29 AD2 CYS B  245  LYS B  250  1                                   6    
HELIX   30 AD3 GLN B  253  GLU B  261  1                                   9    
HELIX   31 AD4 SER B  270  PHE B  275  1                                   6    
HELIX   32 AD5 SER B  284  LEU B  302  1                                  19    
HELIX   33 AD6 SER B  311  GLN B  317  1                                   7    
HELIX   34 AD7 ILE B  321  TYR B  325  5                                   5    
HELIX   35 AD8 ASP B  326  GLU B  331  1                                   6    
HELIX   36 AD9 THR B  348  MET B  361  1                                  14    
SHEET    1 AA1 2 PHE B  10  ILE B  15  0                                        
SHEET    2 AA1 2 SER B  18  LEU B  23 -1  O  PHE B  20   N  VAL B  13           
SHEET    1 AA2 5 TYR B  26  PRO B  31  0                                        
SHEET    2 AA2 5 VAL B  40  ASP B  45 -1  O  ALA B  42   N  LYS B  30           
SHEET    3 AA2 5 ARG B  50  SER B  58 -1  O  VAL B  52   N  ALA B  43           
SHEET    4 AA2 5 ASP B 103  GLU B 109 -1  O  MET B 108   N  ALA B  53           
SHEET    5 AA2 5 LEU B  88  PHE B  92 -1  N  LEU B  89   O  VAL B 107           
SHEET    1 AA3 3 ALA B 113  ASN B 114  0                                        
SHEET    2 AA3 3 ILE B 157  VAL B 159 -1  O  VAL B 159   N  ALA B 113           
SHEET    3 AA3 3 LEU B 165  ILE B 167 -1  O  LYS B 166   N  VAL B 158           
CRYST1   76.995   76.995  330.725  90.00  90.00 120.00 P 65          6          
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      0.012988  0.007499  0.000000        0.00000                         
SCALE2      0.000000  0.014997  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003024        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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