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Database: PDB
Entry: 6G4Y
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Original site: 6G4Y 
HEADER    TRANSFERASE                             28-MAR-18   6G4Y              
TITLE     CRYSTAL STRUCTURE OF MURINE NF-KAPPAB INDUCING KINASE (NIK) IN COMPLEX
TITLE    2 WITH COMPOUND 1A                                                     
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: HOUSE 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    A.J.HOLE,S.G.HYMOWITZ,P.A.MCEWAN                                      
REVDAT   3   22-AUG-18 6G4Y    1       TITLE  JRNL                              
REVDAT   2   01-AUG-18 6G4Y    1       JRNL                                     
REVDAT   1   04-JUL-18 6G4Y    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.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
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) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 143.80                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 26274                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1408                            
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) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1894                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 124                          
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5054                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 83                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.64000                                             
REMARK   3    B22 (A**2) : -2.64000                                             
REMARK   3    B33 (A**2) : 5.27000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.526         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.300         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.240         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.843        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5287 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4932 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7163 ; 1.309 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11472 ; 0.915 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   649 ; 5.785 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   219 ;35.279 ;23.379       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   908 ;14.821 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;15.527 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   763 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5857 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1033 ; 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):  2602 ; 1.020 ; 3.410       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2601 ; 1.020 ; 3.409       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3246 ; 1.880 ; 5.106       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3247 ; 1.879 ; 5.108       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2685 ; 0.823 ; 3.632       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2685 ; 0.822 ; 3.632       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3917 ; 1.522 ; 5.413       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5690 ; 3.903 ;40.105       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5681 ; 3.872 ;40.087       
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  : 2                                          
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   675                          
REMARK   3    ORIGIN FOR THE GROUP (A): 192.3391  20.8781   3.3872              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0630 T22:   0.0870                                     
REMARK   3      T33:   0.0171 T12:  -0.0103                                     
REMARK   3      T13:   0.0209 T23:   0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9980 L22:   1.2810                                     
REMARK   3      L33:   0.5096 L12:  -0.6657                                     
REMARK   3      L13:   0.1656 L23:  -0.1568                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0339 S12:  -0.2126 S13:  -0.0786                       
REMARK   3      S21:   0.0309 S22:  -0.0245 S23:   0.0808                       
REMARK   3      S31:  -0.0872 S32:   0.1137 S33:  -0.0094                       
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 :   B   334        B   675                          
REMARK   3    ORIGIN FOR THE GROUP (A): 163.6649  49.0317  -2.2381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1495 T22:   0.0495                                     
REMARK   3      T33:   0.0640 T12:   0.0340                                     
REMARK   3      T13:   0.0399 T23:  -0.0193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3861 L22:   2.0845                                     
REMARK   3      L33:   1.1181 L12:   1.0317                                     
REMARK   3      L13:   0.4253 L23:   0.4367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0859 S12:   0.1144 S13:  -0.1111                       
REMARK   3      S21:  -0.1431 S22:   0.1895 S23:  -0.1450                       
REMARK   3      S31:  -0.0904 S32:   0.1406 S33:  -0.1036                       
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 6G4Y 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_1200008448.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-AUG-12                          
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                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27695                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 143.800                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
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       22.80700            
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       34.21050            
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       11.40350            
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 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    TRP A 362       42.08    -93.54                                   
REMARK 500    TYR A 395       86.52   -156.90                                   
REMARK 500    VAL A 399      -59.50   -130.00                                   
REMARK 500    GLN A 405      -77.30    -29.55                                   
REMARK 500    ARG A 407       82.55    -69.26                                   
REMARK 500    ASP A 517       59.41   -163.69                                   
REMARK 500    ASP A 536       86.21     62.40                                   
REMARK 500    ASP A 576     -163.29   -129.64                                   
REMARK 500    TRP A 598      -29.59     74.12                                   
REMARK 500    PRO A 674     -173.78    -61.75                                   
REMARK 500    GLN B 405      -99.54      4.69                                   
REMARK 500    ARG B 407       96.17    -65.76                                   
REMARK 500    CYS B 428     -157.81   -149.60                                   
REMARK 500    ASP B 517       61.50   -159.93                                   
REMARK 500    ASP B 536       89.83     62.43                                   
REMARK 500    GLN B 544      171.29    -58.30                                   
REMARK 500    ASP B 576     -163.95   -123.79                                   
REMARK 500    TRP B 598      -25.97     75.07                                   
REMARK 500    PRO B 605      109.22    -39.94                                   
REMARK 500    PRO B 616       44.50    -74.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ELZ A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ELZ B 703                 
DBREF  6G4Y A  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
DBREF  6G4Y B  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
SEQADV 6G4Y GLY A  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 6G4Y SER A  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 6G4Y GLY B  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 6G4Y 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    SO4  A 701       5                                                       
HET    SO4  A 702       5                                                       
HET    ELZ  A 703      36                                                       
HET    SO4  B 701       5                                                       
HET    SO4  B 702       5                                                       
HET    ELZ  B 703      36                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ELZ 10-[2-[(3~{R})-1-METHYL-3-OXIDANYL-2-OXIDANYLIDENE-              
HETNAM   2 ELZ  PYRROLIDIN-3-YL]ETHYNYL]-~{N}3-(OXAN-4-YL)-5,6-                 
HETNAM   3 ELZ  DIHYDROIMIDAZO[1,2-D][1,4]BENZOXAZEPINE-2,3-                    
HETNAM   4 ELZ  DICARBOXAMIDE                                                   
FORMUL   3  SO4    4(O4 S 2-)                                                   
FORMUL   5  ELZ    2(C25 H27 N5 O6)                                             
FORMUL   9  HOH   *83(H2 O)                                                     
HELIX    1 AA1 PRO A  334  GLN A  344  1                                  11    
HELIX    2 AA2 GLN A  351  LYS A  360  1                                  10    
HELIX    3 AA3 GLU A  436  ARG A  439  5                                   4    
HELIX    4 AA4 VAL A  440  ALA A  447  1                                   8    
HELIX    5 AA5 LEU A  479  GLY A  487  1                                   9    
HELIX    6 AA6 PRO A  490  ARG A  511  1                                  22    
HELIX    7 AA7 LYS A  519  ASP A  521  5                                   3    
HELIX    8 AA8 ALA A  566  MET A  571  1                                   6    
HELIX    9 AA9 ALA A  577  GLY A  594  1                                  18    
HELIX   10 AB1 PRO A  605  GLU A  613  1                                   9    
HELIX   11 AB2 PRO A  616  ILE A  620  5                                   5    
HELIX   12 AB3 ALA A  625  LEU A  636  1                                  12    
HELIX   13 AB4 GLU A  639  ARG A  643  5                                   5    
HELIX   14 AB5 SER A  645  VAL A  660  1                                  16    
HELIX   15 AB6 VAL B  335  GLN B  344  1                                  10    
HELIX   16 AB7 GLN B  351  LYS B  360  1                                  10    
HELIX   17 AB8 THR B  361  SER B  363  5                                   3    
HELIX   18 AB9 GLU B  436  ARG B  439  5                                   4    
HELIX   19 AC1 VAL B  440  ALA B  447  1                                   8    
HELIX   20 AC2 SER B  478  GLY B  487  1                                  10    
HELIX   21 AC3 PRO B  490  ARG B  511  1                                  22    
HELIX   22 AC4 LYS B  519  ASP B  521  5                                   3    
HELIX   23 AC5 THR B  561  MET B  565  5                                   5    
HELIX   24 AC6 ALA B  566  MET B  571  1                                   6    
HELIX   25 AC7 ALA B  577  GLY B  594  1                                  18    
HELIX   26 AC8 PRO B  605  GLU B  613  1                                   9    
HELIX   27 AC9 PRO B  616  ILE B  620  5                                   5    
HELIX   28 AD1 ALA B  625  LEU B  636  1                                  12    
HELIX   29 AD2 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  ALA A 429   O  MET A 471           
SHEET    6 AA1 7 VAL A 416  ASP A 421 -1  N  HIS A 417   O  VAL A 430           
SHEET    7 AA1 7 TRP A 401  THR A 403 -1  N  MET A 402   O  LYS A 420           
SHEET    1 AA2 3 GLY A 477  SER A 478  0                                        
SHEET    2 AA2 3 VAL A 523  LEU A 525 -1  O  LEU A 525   N  GLY A 477           
SHEET    3 AA2 3 ALA A 532  LEU A 534 -1  O  ALA A 533   N  LEU A 524           
SHEET    1 AA3 2 ILE A 513  LEU A 514  0                                        
SHEET    2 AA3 2 LEU A 541  CYS A 542 -1  O  LEU A 541   N  LEU A 514           
SHEET    1 AA4 7 VAL B 347  SER B 349  0                                        
SHEET    2 AA4 7 ASN B 379  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  MET B 419   O  CYS B 428           
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  4 ARG A 637  LYS A 638  GLU A 639  HIS A 642                    
SITE     1 AC2  2 ARG A 650  ARG A 651                                          
SITE     1 AC3 17 ARG A 410  GLY A 411  VAL A 416  ARG A 418                    
SITE     2 AC3 17 ALA A 429  GLU A 442  VAL A 455  ILE A 469                    
SITE     3 AC3 17 MET A 471  GLU A 472  LEU A 473  LEU A 474                    
SITE     4 AC3 17 GLY A 477  LEU A 524  CYS A 535  ASP A 536                    
SITE     5 AC3 17 PHE A 537                                                     
SITE     1 AC4  4 ARG B 637  LYS B 638  GLU B 639  HIS B 642                    
SITE     1 AC5  4 LYS A 519  THR A 561  HIS A 596  GLN B 351                    
SITE     1 AC6 19 ARG B 410  GLY B 411  VAL B 416  ARG B 418                    
SITE     2 AC6 19 GLU B 442  VAL B 455  ILE B 469  MET B 471                    
SITE     3 AC6 19 GLU B 472  LEU B 474  GLU B 475  GLY B 477                    
SITE     4 AC6 19 SER B 478  GLN B 481  ASP B 521  LEU B 524                    
SITE     5 AC6 19 CYS B 535  ASP B 536  PHE B 537                               
CRYST1  143.829  143.829   45.614  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      0.006953  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006953  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021923        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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