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Database: PDB
Entry: 6G4Z
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Original site: 6G4Z 
HEADER    TRANSFERASE                             28-MAR-18   6G4Z              
TITLE     CRYSTAL STRUCTURE OF MURINE NF-KAPPAB INDUCING KINASE (NIK) IN COMPLEX
TITLE    2 WITH COMPOUND 2F                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 14;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NF-KAPPA-BETA-INDUCING KINASE,SERINE/THREONINE-PROTEIN      
COMPND   5 KINASE NIK;                                                          
COMPND   6 EC: 2.7.11.25;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: MAP3K14, NIK;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PROTEIN SERINE/THREONINE KINASE, NF-KAPPAB, MAP3K14, TRANSFERASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LEONARDO-SILVESTRE,P.A.MCEWAN,S.G.HYMOWITZ                          
REVDAT   3   22-AUG-18 6G4Z    1       TITLE  JRNL                              
REVDAT   2   01-AUG-18 6G4Z    1       JRNL                                     
REVDAT   1   04-JUL-18 6G4Z    0                                                
JRNL        AUTH   N.BLAQUIERE,G.M.CASTANEDO,J.D.BURCH,L.M.BEREZHKOVSKIY,       
JRNL        AUTH 2 H.BRIGHTBILL,S.BROWN,C.CHAN,P.C.CHIANG,J.J.CRAWFORD,T.DONG,  
JRNL        AUTH 3 P.FAN,J.FENG,N.GHILARDI,R.GODEMANN,E.GOGOL,A.GRABBE,         
JRNL        AUTH 4 A.J.HOLE,B.HU,S.G.HYMOWITZ,M.H.ALAOUI ISMAILI,H.LE,P.LEE,    
JRNL        AUTH 5 W.LEE,X.LIN,N.LIU,P.A.MCEWAN,B.MCKENZIE,H.L.SILVESTRE,       
JRNL        AUTH 6 E.SUTO,S.SUJATHA-BHASKAR,G.WU,L.C.WU,Y.ZHANG,Z.ZHONG,        
JRNL        AUTH 7 S.T.STABEN                                                   
JRNL        TITL   SCAFFOLD-HOPPING APPROACH TO DISCOVER POTENT, SELECTIVE, AND 
JRNL        TITL 2 EFFICACIOUS INHIBITORS OF NF-KAPPA B INDUCING KINASE.        
JRNL        REF    J. MED. CHEM.                 V.  61  6801 2018              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29940120                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B00678                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 21715                          
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) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1171                            
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) : 2.84                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.91                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1660                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.3930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5020                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 18                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 76.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : -0.04000                                             
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): 1.348         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.400         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.342         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 39.116        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.894                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.876                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5207 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4997 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7050 ; 1.052 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11540 ; 0.701 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   643 ; 5.477 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   215 ;33.017 ;23.442       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   900 ;15.319 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;14.664 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   755 ; 0.052 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5861 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1148 ; 0.001 ; 0.020       
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):  2584 ; 2.170 ; 6.387       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2583 ; 2.166 ; 6.386       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3220 ; 3.737 ; 9.572       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3221 ; 3.738 ; 9.573       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2623 ; 2.111 ; 6.682       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2623 ; 2.111 ; 6.682       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3830 ; 3.631 ; 9.916       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5780 ; 6.092 ;50.811       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5781 ; 6.092 ;50.816       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   334        A   472                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.4621  46.9095   1.5871              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0995 T22:   0.0666                                     
REMARK   3      T33:   0.0835 T12:   0.0139                                     
REMARK   3      T13:  -0.0285 T23:   0.0538                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8159 L22:   0.7609                                     
REMARK   3      L33:   0.4499 L12:  -0.8187                                     
REMARK   3      L13:  -0.3371 L23:   0.0608                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0022 S12:   0.0182 S13:   0.0122                       
REMARK   3      S21:   0.0659 S22:   0.0238 S23:  -0.0307                       
REMARK   3      S31:   0.0217 S32:  -0.0065 S33:  -0.0260                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   473        A   675                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7639  54.6184   3.5200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0173 T22:   0.1553                                     
REMARK   3      T33:   0.0709 T12:  -0.0242                                     
REMARK   3      T13:  -0.0163 T23:   0.0476                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6994 L22:   1.1040                                     
REMARK   3      L33:   1.5185 L12:   0.4106                                     
REMARK   3      L13:   0.5132 L23:   0.2722                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1118 S12:  -0.1477 S13:   0.0719                       
REMARK   3      S21:  -0.0124 S22:  -0.2053 S23:   0.1443                       
REMARK   3      S31:   0.0061 S32:  -0.0613 S33:   0.0935                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   334        B   472                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.9112  31.6399  -4.2589              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0887 T22:   0.0559                                     
REMARK   3      T33:   0.1142 T12:   0.0062                                     
REMARK   3      T13:  -0.0544 T23:   0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7456 L22:   0.5679                                     
REMARK   3      L33:   0.8188 L12:   0.5196                                     
REMARK   3      L13:  -0.4588 L23:   0.1090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0400 S12:  -0.0213 S13:   0.0947                       
REMARK   3      S21:   0.0051 S22:   0.1180 S23:   0.0306                       
REMARK   3      S31:   0.0797 S32:   0.0622 S33:  -0.0780                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   473        B   675                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.5769  17.6391  -1.8957              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0800 T22:   0.0791                                     
REMARK   3      T33:   0.1243 T12:  -0.0497                                     
REMARK   3      T13:  -0.0418 T23:   0.0667                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4174 L22:   2.3276                                     
REMARK   3      L33:   1.6156 L12:   0.1304                                     
REMARK   3      L13:   0.0797 L23:  -0.4385                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0978 S12:   0.0962 S13:  -0.0462                       
REMARK   3      S21:   0.0668 S22:   0.1719 S23:   0.2046                       
REMARK   3      S31:   0.0197 S32:  -0.0806 S33:  -0.0741                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 ADDED IN THE RIDING   
REMARK   3   POSITIONS                                                          
REMARK   4                                                                      
REMARK   4 6G4Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008316.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21715                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.840                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.210                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.84                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74500                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 4G3E                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3-0.9M AMMONIUM SULPHATE, 0.05-0.1M    
REMARK 280  SODIUM CITRATE, 0.7-1.0M LITHIUM SULPHATE, PH 6.2, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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       23.26500            
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       34.89750            
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       11.63250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   327                                                      
REMARK 465     SER A   328                                                      
REMARK 465     ALA A   329                                                      
REMARK 465     LEU A   330                                                      
REMARK 465     GLU A   331                                                      
REMARK 465     LYS A   332                                                      
REMARK 465     VAL A   333                                                      
REMARK 465     SER A   364                                                      
REMARK 465     GLY A   365                                                      
REMARK 465     SER A   366                                                      
REMARK 465     ALA A   367                                                      
REMARK 465     LYS A   368                                                      
REMARK 465     LEU A   369                                                      
REMARK 465     GLN A   370                                                      
REMARK 465     ARG A   371                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     GLY A   373                                                      
REMARK 465     PRO A   374                                                      
REMARK 465     GLU A   375                                                      
REMARK 465     THR A   376                                                      
REMARK 465     GLU A   377                                                      
REMARK 465     PRO A   545                                                      
REMARK 465     ASP A   546                                                      
REMARK 465     GLY A   547                                                      
REMARK 465     LEU A   548                                                      
REMARK 465     GLY A   549                                                      
REMARK 465     LYS A   550                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     SER B   328                                                      
REMARK 465     ALA B   329                                                      
REMARK 465     LEU B   330                                                      
REMARK 465     GLU B   331                                                      
REMARK 465     LYS B   332                                                      
REMARK 465     VAL B   333                                                      
REMARK 465     SER B   364                                                      
REMARK 465     GLY B   365                                                      
REMARK 465     SER B   366                                                      
REMARK 465     ALA B   367                                                      
REMARK 465     LYS B   368                                                      
REMARK 465     LEU B   369                                                      
REMARK 465     GLN B   370                                                      
REMARK 465     ARG B   371                                                      
REMARK 465     LEU B   372                                                      
REMARK 465     GLY B   373                                                      
REMARK 465     PRO B   374                                                      
REMARK 465     GLU B   375                                                      
REMARK 465     THR B   376                                                      
REMARK 465     GLU B   377                                                      
REMARK 465     TYR B   601                                                      
REMARK 465     PHE B   602                                                      
REMARK 465     ARG B   603                                                      
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    PRO A 605   C   -  N   -  CA  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    PRO A 605   C   -  N   -  CD  ANGL. DEV. = -18.5 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    GLU A 386      -35.85    -39.25                                   
REMARK 500    ASP A 392       59.79     38.12                                   
REMARK 500    VAL A 399      -52.67   -129.85                                   
REMARK 500    ARG A 407       98.38     61.31                                   
REMARK 500    ASP A 517       58.73   -168.25                                   
REMARK 500    LYS A 519      141.43   -178.21                                   
REMARK 500    ASP A 536       77.99     63.46                                   
REMARK 500    PHE A 537       34.68    -92.65                                   
REMARK 500    LEU A 552      -58.83     75.61                                   
REMARK 500    TRP A 598      -44.26     73.74                                   
REMARK 500    ARG A 603      -87.85   -106.88                                   
REMARK 500    PRO A 605       97.10     17.95                                   
REMARK 500    PRO A 640      -38.98    -39.61                                   
REMARK 500    ASN B 379       93.86     66.72                                   
REMARK 500    ASP B 392       59.82     33.91                                   
REMARK 500    GLU B 398       26.68     49.79                                   
REMARK 500    VAL B 399      -57.92   -126.79                                   
REMARK 500    GLN B 405      -92.97     12.95                                   
REMARK 500    ALA B 445      -70.79    -60.59                                   
REMARK 500    ASP B 536       83.46     56.58                                   
REMARK 500    PRO B 545       67.01    -54.46                                   
REMARK 500    ASP B 546      -33.41   -179.02                                   
REMARK 500    LEU B 553       53.52    102.94                                   
REMARK 500    ASP B 556       19.81     56.70                                   
REMARK 500    TRP B 598       88.62     64.06                                   
REMARK 500    THR B 599       44.62   -108.43                                   
REMARK 500    PRO B 616       44.95    -78.30                                   
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 ELW A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ELW B 701                 
DBREF  6G4Z A  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
DBREF  6G4Z B  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
SEQADV 6G4Z GLY A  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 6G4Z SER A  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 6G4Z GLY B  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 6G4Z SER B  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQRES   1 A  349  GLY SER ALA LEU GLU LYS VAL PRO VAL GLU GLU TYR LEU          
SEQRES   2 A  349  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 A  349  HIS SER LEU ALA SER LEU ALA LYS THR TRP SER SER GLY          
SEQRES   4 A  349  SER ALA LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP          
SEQRES   5 A  349  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 A  349  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS          
SEQRES   7 A  349  GLN PRO ARG VAL GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 A  349  ARG MET LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 A  349  LYS LYS VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU          
SEQRES  10 A  349  VAL ALA CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO          
SEQRES  11 A  349  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 A  349  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 A  349  ILE LYS GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 A  349  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 A  349  HIS THR ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 A  349  ASN VAL LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU          
SEQRES  17 A  349  CYS ASP PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY          
SEQRES  18 A  349  LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 A  349  THR GLU THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS          
SEQRES  20 A  349  PRO CYS ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS          
SEQRES  21 A  349  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 A  349  GLN TYR PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 A  349  GLU PRO PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 A  349  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 A  349  GLU PRO VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG          
SEQRES  26 A  349  LYS VAL GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS          
SEQRES  27 A  349  SER PRO TRP LYS GLY GLU TYR LYS GLU PRO ARG                  
SEQRES   1 B  349  GLY SER ALA LEU GLU LYS VAL PRO VAL GLU GLU TYR LEU          
SEQRES   2 B  349  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 B  349  HIS SER LEU ALA SER LEU ALA LYS THR TRP SER SER GLY          
SEQRES   4 B  349  SER ALA LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP          
SEQRES   5 B  349  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 B  349  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS          
SEQRES   7 B  349  GLN PRO ARG VAL GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 B  349  ARG MET LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 B  349  LYS LYS VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU          
SEQRES  10 B  349  VAL ALA CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO          
SEQRES  11 B  349  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 B  349  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 B  349  ILE LYS GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 B  349  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 B  349  HIS THR ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 B  349  ASN VAL LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU          
SEQRES  17 B  349  CYS ASP PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY          
SEQRES  18 B  349  LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 B  349  THR GLU THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS          
SEQRES  20 B  349  PRO CYS ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS          
SEQRES  21 B  349  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 B  349  GLN TYR PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 B  349  GLU PRO PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 B  349  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 B  349  GLU PRO VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG          
SEQRES  26 B  349  LYS VAL GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS          
SEQRES  27 B  349  SER PRO TRP LYS GLY GLU TYR LYS GLU PRO ARG                  
HET    ELW  A 701      29                                                       
HET    ELW  B 701      29                                                       
HETNAM     ELW 5-FLUORANYL-1-[4-[2-[(3~{R})-1-METHYL-3-OXIDANYL-2-              
HETNAM   2 ELW  OXIDANYLIDENE-PYRROL-3-YL]ETHYNYL]PYRIDIN-2-                    
HETNAM   3 ELW  YL]INDAZOLE-3-CARBOXAMIDE                                       
FORMUL   3  ELW    2(C20 H14 F N5 O3)                                           
FORMUL   5  HOH   *18(H2 O)                                                     
HELIX    1 AA1 VAL A  335  GLN A  344  1                                  10    
HELIX    2 AA2 GLN A  351  THR A  361  1                                  11    
HELIX    3 AA3 VAL A  440  ALA A  447  1                                   8    
HELIX    4 AA4 SER A  478  GLY A  487  1                                  10    
HELIX    5 AA5 PRO A  490  ARG A  511  1                                  22    
HELIX    6 AA6 LYS A  519  ASP A  521  5                                   3    
HELIX    7 AA7 ALA A  566  GLY A  572  1                                   7    
HELIX    8 AA8 ALA A  577  GLY A  594  1                                  18    
HELIX    9 AA9 PRO A  605  GLU A  613  1                                   9    
HELIX   10 AB1 PRO A  616  ILE A  620  5                                   5    
HELIX   11 AB2 ALA A  625  LEU A  636  1                                  12    
HELIX   12 AB3 SER A  645  VAL A  660  1                                  16    
HELIX   13 AB4 VAL B  335  GLN B  344  1                                  10    
HELIX   14 AB5 GLN B  351  LYS B  360  1                                  10    
HELIX   15 AB6 GLU B  436  ARG B  439  5                                   4    
HELIX   16 AB7 VAL B  440  ALA B  447  1                                   8    
HELIX   17 AB8 SER B  478  GLY B  487  1                                  10    
HELIX   18 AB9 PRO B  490  ARG B  511  1                                  22    
HELIX   19 AC1 LYS B  519  ASP B  521  5                                   3    
HELIX   20 AC2 ALA B  566  MET B  571  1                                   6    
HELIX   21 AC3 ALA B  577  GLY B  594  1                                  18    
HELIX   22 AC4 PRO B  605  GLU B  613  1                                   9    
HELIX   23 AC5 PRO B  615  ILE B  620  5                                   6    
HELIX   24 AC6 ALA B  625  GLY B  635  1                                  11    
HELIX   25 AC7 SER B  645  VAL B  660  1                                  16    
SHEET    1 AA1 7 VAL A 347  SER A 349  0                                        
SHEET    2 AA1 7 ASN A 379  LEU A 383  1  O  LEU A 383   N  SER A 348           
SHEET    3 AA1 7 LEU A 457  GLU A 463 -1  O  ARG A 462   N  GLU A 380           
SHEET    4 AA1 7 TRP A 466  MET A 471 -1  O  ASN A 468   N  VAL A 461           
SHEET    5 AA1 7 GLN A 427  ARG A 434 -1  N  LYS A 431   O  ILE A 469           
SHEET    6 AA1 7 VAL A 416  ASP A 421 -1  N  MET A 419   O  CYS A 428           
SHEET    7 AA1 7 TRP A 401  THR A 403 -1  N  MET A 402   O  LYS A 420           
SHEET    1 AA2 2 ILE A 513  LEU A 514  0                                        
SHEET    2 AA2 2 LEU A 541  CYS A 542 -1  O  LEU A 541   N  LEU A 514           
SHEET    1 AA3 2 VAL A 523  LEU A 525  0                                        
SHEET    2 AA3 2 ALA A 532  LEU A 534 -1  O  ALA A 533   N  LEU A 524           
SHEET    1 AA4 7 VAL B 347  SER B 349  0                                        
SHEET    2 AA4 7 GLU B 380  LEU B 383  1  O  LEU B 383   N  SER B 348           
SHEET    3 AA4 7 LEU B 457  GLU B 463 -1  O  ARG B 462   N  GLU B 380           
SHEET    4 AA4 7 TRP B 466  MET B 471 -1  O  PHE B 470   N  TYR B 458           
SHEET    5 AA4 7 GLN B 427  ARG B 434 -1  N  LYS B 431   O  ILE B 469           
SHEET    6 AA4 7 VAL B 416  ASP B 421 -1  N  HIS B 417   O  VAL B 430           
SHEET    7 AA4 7 TRP B 401  THR B 403 -1  N  MET B 402   O  LYS B 420           
SHEET    1 AA5 2 ILE B 513  LEU B 514  0                                        
SHEET    2 AA5 2 LEU B 541  CYS B 542 -1  O  LEU B 541   N  LEU B 514           
SHEET    1 AA6 2 VAL B 523  LEU B 525  0                                        
SHEET    2 AA6 2 ALA B 532  LEU B 534 -1  O  ALA B 533   N  LEU B 524           
SITE     1 AC1 18 ARG A 410  VAL A 416  ALA A 429  GLU A 442                    
SITE     2 AC1 18 CYS A 446  VAL A 455  ILE A 469  MET A 471                    
SITE     3 AC1 18 GLU A 472  LEU A 473  LEU A 474  GLY A 477                    
SITE     4 AC1 18 SER A 478  GLN A 481  LEU A 524  CYS A 535                    
SITE     5 AC1 18 ASP A 536  PHE A 537                                          
SITE     1 AC2 17 ARG B 410  VAL B 416  ALA B 429  LYS B 431                    
SITE     2 AC2 17 GLU B 442  VAL B 455  ILE B 469  MET B 471                    
SITE     3 AC2 17 GLU B 472  LEU B 474  GLY B 477  SER B 478                    
SITE     4 AC2 17 GLN B 481  LEU B 524  CYS B 535  ASP B 536                    
SITE     5 AC2 17 PHE B 537                                                     
CRYST1  144.830  144.830   46.530  90.00  90.00  90.00 P 43          8          
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      0.006905  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006905  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021492        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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