GenomeNet

Database: PDB
Entry: 6NFZ
LinkDB: 6NFZ
Original site: 6NFZ 
HEADER    SIGNALING PROTEIN                       21-DEC-18   6NFZ              
TITLE     CRYSTAL STRUCTURE OF DIPHOSPHORYLATED HPK1 KINASE DOMAIN IN COMPLEX   
TITLE    2 WITH SUNITINIB IN THE ACTIVE STATE.                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 1;   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HEMATOPOIETIC PROGENITOR KINASE,MAPK/ERK KINASE KINASE      
COMPND   5 KINASE 1,MEKKK 1;                                                    
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAP4K1, HPK1;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    KINASE, ACTIVE STATE, DIMER, SIGNALING PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.JOHNSON,M.MCTIGUE,C.N.CRONIN                                        
REVDAT   4   26-JUN-19 6NFZ    1       JRNL                                     
REVDAT   3   19-JUN-19 6NFZ    1       JRNL                                     
REVDAT   2   08-MAY-19 6NFZ    1       JRNL                                     
REVDAT   1   01-MAY-19 6NFZ    0                                                
JRNL        AUTH   E.JOHNSON,M.MCTIGUE,R.A.GALLEGO,T.W.JOHNSON,S.TIMOFEEVSKI,   
JRNL        AUTH 2 M.MAESTRE,T.S.FISHER,R.KANIA,S.SAWASDIKOSOL,S.BURAKOFF,      
JRNL        AUTH 3 C.N.CRONIN                                                   
JRNL        TITL   MULTIPLE CONFORMATIONAL STATES OF THE HPK1 KINASE DOMAIN IN  
JRNL        TITL 2 COMPLEX WITH SUNITINIB REVEAL THE STRUCTURAL CHANGES         
JRNL        TITL 3 ACCOMPANYING HPK1 TRANS-REGULATION.                          
JRNL        REF    J.BIOL.CHEM.                  V. 294  9029 2019              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   31018963                                                     
JRNL        DOI    10.1074/JBC.AC119.007466                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 14215                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 707                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.5200 -  5.0678    1.00     2788   137  0.1838 0.2225        
REMARK   3     2  5.0678 -  4.0240    1.00     2699   151  0.1776 0.2048        
REMARK   3     3  4.0240 -  3.5158    1.00     2701   132  0.2112 0.2620        
REMARK   3     4  3.5158 -  3.1945    1.00     2685   133  0.2533 0.3088        
REMARK   3     5  3.1945 -  2.9656    1.00     2635   154  0.2791 0.3449        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.410           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 76.61                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           4525                                  
REMARK   3   ANGLE     :  0.958           6116                                  
REMARK   3   CHIRALITY :  0.035            674                                  
REMARK   3   PLANARITY :  0.003            762                                  
REMARK   3   DIHEDRAL  : 18.818           1705                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6NFZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000236778.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-NOV-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 180                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14226                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.966                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.995                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.00                              
REMARK 200  R MERGE                    (I) : 0.19600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.00                              
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   (%): 49.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM FLUORIDE, 20% PEG 3350,    
REMARK 280  100NL WELL + 100NL PROTEIN @ 22MG/ML, PH 7.5, VAPOR DIFFUSION,      
REMARK 280  SITTING DROP, TEMPERATURE 286.15K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       74.96600            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       43.28164            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       52.25133            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       74.96600            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       43.28164            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       52.25133            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       74.96600            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       43.28164            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       52.25133            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       74.96600            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       43.28164            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       52.25133            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       74.96600            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       43.28164            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       52.25133            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       74.96600            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       43.28164            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       52.25133            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       86.56328            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      104.50267            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       86.56328            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      104.50267            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       86.56328            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      104.50267            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       86.56328            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      104.50267            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       86.56328            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      104.50267            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       86.56328            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      104.50267            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     LYS A    49                                                      
REMARK 465     MET A    50                                                      
REMARK 465     GLU A    51                                                      
REMARK 465     PRO A    52                                                      
REMARK 465     ASP A    53                                                      
REMARK 465     ASP A    54                                                      
REMARK 465     ASP A    55                                                      
REMARK 465     VAL A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     LEU A    82                                                      
REMARK 465     TRP A    83                                                      
REMARK 465     LEU A    84                                                      
REMARK 465     GLN A    85                                                      
REMARK 465     LYS A    86                                                      
REMARK 465     ASN A   293                                                      
REMARK 465     PRO A   294                                                      
REMARK 465     GLY A   295                                                      
REMARK 465     LYS A   296                                                      
REMARK 465     GLY A   297                                                      
REMARK 465     PRO A   298                                                      
REMARK 465     SER A   299                                                      
REMARK 465     ILE A   300                                                      
REMARK 465     GLY A   301                                                      
REMARK 465     ASP A   302                                                      
REMARK 465     ILE A   303                                                      
REMARK 465     GLU A   304                                                      
REMARK 465     ASP A   305                                                      
REMARK 465     GLU A   306                                                      
REMARK 465     GLU A   307                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     THR B    27                                                      
REMARK 465     TYR B    28                                                      
REMARK 465     ASP B    54                                                      
REMARK 465     ASP B    55                                                      
REMARK 465     VAL B    56                                                      
REMARK 465     SER B    57                                                      
REMARK 465     THR B    58                                                      
REMARK 465     ALA B   164                                                      
REMARK 465     TPO B   165                                                      
REMARK 465     LEU B   166                                                      
REMARK 465     ASN B   293                                                      
REMARK 465     PRO B   294                                                      
REMARK 465     GLY B   295                                                      
REMARK 465     LYS B   296                                                      
REMARK 465     GLY B   297                                                      
REMARK 465     PRO B   298                                                      
REMARK 465     SER B   299                                                      
REMARK 465     ILE B   300                                                      
REMARK 465     GLY B   301                                                      
REMARK 465     ASP B   302                                                      
REMARK 465     ILE B   303                                                      
REMARK 465     GLU B   304                                                      
REMARK 465     ASP B   305                                                      
REMARK 465     GLU B   306                                                      
REMARK 465     GLU B   307                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  22    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A  28    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A  37    CG   CD   CE   NZ                                   
REMARK 470     LYS A  46    CG   CD   CE   NZ                                   
REMARK 470     MET A  47    CG   SD   CE                                        
REMARK 470     THR A  58    OG1  CG2                                            
REMARK 470     LYS A  61    CG   CD   CE   NZ                                   
REMARK 470     LEU A  87    CG   CD1  CD2                                       
REMARK 470     ASP B  53    CG   OD1  OD2                                       
REMARK 470     LEU B  59    CG   CD1  CD2                                       
REMARK 470     GLN B  60    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  61    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HB3  ASP A   101     H21  B49 A   401              1.31            
REMARK 500   HA3  GLY A    29     O    MET A    47              1.43            
REMARK 500   H    LEU B    20     O    LYS B    33              1.47            
REMARK 500   O    ASP A   137    HD22  ASN A   142              1.55            
REMARK 500   OD1  ASP B    18     HZ3  LYS B    37              1.55            
REMARK 500  HD21  ASN B   146     OE1  GLU B   150              1.58            
REMARK 500   O    PHE B   156     HG   SER B   159              1.58            
REMARK 500   O    HIS A   271     HG   SER A   275              1.59            
REMARK 500   CA   GLY A    29     O    MET A    47              2.13            
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    TYR A  17     -159.29   -131.06                                   
REMARK 500    TYR A  28     -124.11     63.11                                   
REMARK 500    ARG A 136       -9.45     72.34                                   
REMARK 500    ASP A 155       80.12     58.53                                   
REMARK 500    PHE A 156       31.70    -96.32                                   
REMARK 500    LEU A 211       -3.86     66.35                                   
REMARK 500    LEU A 255       51.10   -101.00                                   
REMARK 500    ARG B  70       72.38   -160.05                                   
REMARK 500    ASP B 137       35.62   -144.70                                   
REMARK 500    ASN B 193     -159.87   -143.26                                   
REMARK 500    LEU B 211       -5.29     67.46                                   
REMARK 500    LYS B 238      -73.15    -71.29                                   
REMARK 500    LEU B 291       21.35    -79.77                                   
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 B49 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue B49 B 9001                
DBREF  6NFZ A    1   307  UNP    Q92918   M4K1_HUMAN       1    307             
DBREF  6NFZ B    1   307  UNP    Q92918   M4K1_HUMAN       1    307             
SEQADV 6NFZ GLY A   -1  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6NFZ SER A    0  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6NFZ GLY B   -1  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6NFZ SER B    0  UNP  Q92918              EXPRESSION TAG                 
SEQRES   1 A  309  GLY SER MET ASP VAL VAL ASP PRO ASP ILE PHE ASN ARG          
SEQRES   2 A  309  ASP PRO ARG ASP HIS TYR ASP LEU LEU GLN ARG LEU GLY          
SEQRES   3 A  309  GLY GLY THR TYR GLY GLU VAL PHE LYS ALA ARG ASP LYS          
SEQRES   4 A  309  VAL SER GLY ASP LEU VAL ALA LEU LYS MET VAL LYS MET          
SEQRES   5 A  309  GLU PRO ASP ASP ASP VAL SER THR LEU GLN LYS GLU ILE          
SEQRES   6 A  309  LEU ILE LEU LYS THR CYS ARG HIS ALA ASN ILE VAL ALA          
SEQRES   7 A  309  TYR HIS GLY SER TYR LEU TRP LEU GLN LYS LEU TRP ILE          
SEQRES   8 A  309  CYS MET GLU PHE CYS GLY ALA GLY SER LEU GLN ASP ILE          
SEQRES   9 A  309  TYR GLN VAL THR GLY SER LEU SER GLU LEU GLN ILE SER          
SEQRES  10 A  309  TYR VAL CYS ARG GLU VAL LEU GLN GLY LEU ALA TYR LEU          
SEQRES  11 A  309  HIS SER GLN LYS LYS ILE HIS ARG ASP ILE LYS GLY ALA          
SEQRES  12 A  309  ASN ILE LEU ILE ASN ASP ALA GLY GLU VAL ARG LEU ALA          
SEQRES  13 A  309  ASP PHE GLY ILE SER ALA GLN ILE GLY ALA TPO LEU ALA          
SEQRES  14 A  309  ARG ARG LEU SEP PHE ILE GLY THR PRO TYR TRP MET ALA          
SEQRES  15 A  309  PRO GLU VAL ALA ALA VAL ALA LEU LYS GLY GLY TYR ASN          
SEQRES  16 A  309  GLU LEU CYS ASP ILE TRP SER LEU GLY ILE THR ALA ILE          
SEQRES  17 A  309  GLU LEU ALA GLU LEU GLN PRO PRO LEU PHE ASP VAL HIS          
SEQRES  18 A  309  PRO LEU ARG VAL LEU PHE LEU MET THR LYS SER GLY TYR          
SEQRES  19 A  309  GLN PRO PRO ARG LEU LYS GLU LYS GLY LYS TRP SER ALA          
SEQRES  20 A  309  ALA PHE HIS ASN PHE ILE LYS VAL THR LEU THR LYS SER          
SEQRES  21 A  309  PRO LYS LYS ARG PRO SER ALA THR LYS MET LEU SER HIS          
SEQRES  22 A  309  GLN LEU VAL SER GLN PRO GLY LEU ASN ARG GLY LEU ILE          
SEQRES  23 A  309  LEU ASP LEU LEU ASP LYS LEU LYS ASN PRO GLY LYS GLY          
SEQRES  24 A  309  PRO SER ILE GLY ASP ILE GLU ASP GLU GLU                      
SEQRES   1 B  309  GLY SER MET ASP VAL VAL ASP PRO ASP ILE PHE ASN ARG          
SEQRES   2 B  309  ASP PRO ARG ASP HIS TYR ASP LEU LEU GLN ARG LEU GLY          
SEQRES   3 B  309  GLY GLY THR TYR GLY GLU VAL PHE LYS ALA ARG ASP LYS          
SEQRES   4 B  309  VAL SER GLY ASP LEU VAL ALA LEU LYS MET VAL LYS MET          
SEQRES   5 B  309  GLU PRO ASP ASP ASP VAL SER THR LEU GLN LYS GLU ILE          
SEQRES   6 B  309  LEU ILE LEU LYS THR CYS ARG HIS ALA ASN ILE VAL ALA          
SEQRES   7 B  309  TYR HIS GLY SER TYR LEU TRP LEU GLN LYS LEU TRP ILE          
SEQRES   8 B  309  CYS MET GLU PHE CYS GLY ALA GLY SER LEU GLN ASP ILE          
SEQRES   9 B  309  TYR GLN VAL THR GLY SER LEU SER GLU LEU GLN ILE SER          
SEQRES  10 B  309  TYR VAL CYS ARG GLU VAL LEU GLN GLY LEU ALA TYR LEU          
SEQRES  11 B  309  HIS SER GLN LYS LYS ILE HIS ARG ASP ILE LYS GLY ALA          
SEQRES  12 B  309  ASN ILE LEU ILE ASN ASP ALA GLY GLU VAL ARG LEU ALA          
SEQRES  13 B  309  ASP PHE GLY ILE SER ALA GLN ILE GLY ALA TPO LEU ALA          
SEQRES  14 B  309  ARG ARG LEU SEP PHE ILE GLY THR PRO TYR TRP MET ALA          
SEQRES  15 B  309  PRO GLU VAL ALA ALA VAL ALA LEU LYS GLY GLY TYR ASN          
SEQRES  16 B  309  GLU LEU CYS ASP ILE TRP SER LEU GLY ILE THR ALA ILE          
SEQRES  17 B  309  GLU LEU ALA GLU LEU GLN PRO PRO LEU PHE ASP VAL HIS          
SEQRES  18 B  309  PRO LEU ARG VAL LEU PHE LEU MET THR LYS SER GLY TYR          
SEQRES  19 B  309  GLN PRO PRO ARG LEU LYS GLU LYS GLY LYS TRP SER ALA          
SEQRES  20 B  309  ALA PHE HIS ASN PHE ILE LYS VAL THR LEU THR LYS SER          
SEQRES  21 B  309  PRO LYS LYS ARG PRO SER ALA THR LYS MET LEU SER HIS          
SEQRES  22 B  309  GLN LEU VAL SER GLN PRO GLY LEU ASN ARG GLY LEU ILE          
SEQRES  23 B  309  LEU ASP LEU LEU ASP LYS LEU LYS ASN PRO GLY LYS GLY          
SEQRES  24 B  309  PRO SER ILE GLY ASP ILE GLU ASP GLU GLU                      
MODRES 6NFZ TPO A  165  THR  MODIFIED RESIDUE                                   
MODRES 6NFZ SEP A  171  SER  MODIFIED RESIDUE                                   
MODRES 6NFZ SEP B  171  SER  MODIFIED RESIDUE                                   
HET    TPO  A 165      16                                                       
HET    SEP  A 171      14                                                       
HET    SEP  B 171      13                                                       
HET    B49  A 401      56                                                       
HET    B49  B9001      56                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     B49 N-[2-(DIETHYLAMINO)ETHYL]-5-[(Z)-(5-FLUORO-2-OXO-1,2-            
HETNAM   2 B49  DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]-2,4-DIMETHYL-1H-             
HETNAM   3 B49  PYRROLE-3-CARBOXAMIDE                                           
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     B49 SUNITINIB                                                        
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  B49    2(C22 H27 F N4 O2)                                           
HELIX    1 AA1 ASP A   12  HIS A   16  5                                   5    
HELIX    2 AA2 LYS A   61  LYS A   67  1                                   7    
HELIX    3 AA3 SER A   98  GLY A  107  1                                  10    
HELIX    4 AA4 SER A  110  GLN A  131  1                                  22    
HELIX    5 AA5 LYS A  139  ALA A  141  5                                   3    
HELIX    6 AA6 THR A  175  MET A  179  5                                   5    
HELIX    7 AA7 ALA A  180  ALA A  185  1                                   6    
HELIX    8 AA8 GLU A  194  LEU A  211  1                                  18    
HELIX    9 AA9 HIS A  219  MET A  227  1                                   9    
HELIX   10 AB1 SER A  244  LEU A  255  1                                  12    
HELIX   11 AB2 SER A  258  ARG A  262  5                                   5    
HELIX   12 AB3 SER A  264  LEU A  269  1                                   6    
HELIX   13 AB4 ARG A  281  LYS A  292  1                                  12    
HELIX   14 AB5 ASP B   12  ASP B   15  5                                   4    
HELIX   15 AB6 GLN B   60  THR B   68  1                                   9    
HELIX   16 AB7 SER B   98  GLY B  107  1                                  10    
HELIX   17 AB8 SER B  110  GLN B  131  1                                  22    
HELIX   18 AB9 LYS B  139  ALA B  141  5                                   3    
HELIX   19 AC1 THR B  175  MET B  179  5                                   5    
HELIX   20 AC2 ALA B  180  ALA B  185  1                                   6    
HELIX   21 AC3 ALA B  185  GLY B  190  1                                   6    
HELIX   22 AC4 LEU B  195  LEU B  211  1                                  17    
HELIX   23 AC5 HIS B  219  LYS B  229  1                                  11    
HELIX   24 AC6 SER B  244  LEU B  255  1                                  12    
HELIX   25 AC7 SER B  264  LEU B  269  1                                   6    
HELIX   26 AC8 HIS B  271  GLN B  276  1                                   6    
HELIX   27 AC9 ARG B  281  LYS B  290  1                                  10    
SHEET    1 AA1 5 GLN A  21  LEU A  23  0                                        
SHEET    2 AA1 5 VAL A  31  ARG A  35 -1  O  VAL A  31   N  LEU A  23           
SHEET    3 AA1 5 LEU A  42  MET A  47 -1  O  VAL A  43   N  ALA A  34           
SHEET    4 AA1 5 TRP A  88  GLU A  92 -1  O  MET A  91   N  ALA A  44           
SHEET    5 AA1 5 TYR A  77  SER A  80 -1  N  GLY A  79   O  CYS A  90           
SHEET    1 AA2 2 LYS A 133  ILE A 134  0                                        
SHEET    2 AA2 2 ALA A 160  GLN A 161 -1  O  ALA A 160   N  ILE A 134           
SHEET    1 AA3 2 ILE A 143  ILE A 145  0                                        
SHEET    2 AA3 2 VAL A 151  LEU A 153 -1  O  ARG A 152   N  LEU A 144           
SHEET    1 AA4 5 TYR B  17  ARG B  22  0                                        
SHEET    2 AA4 5 GLU B  30  ASP B  36 -1  O  LYS B  33   N  LEU B  20           
SHEET    3 AA4 5 LEU B  42  LYS B  49 -1  O  MET B  47   N  GLU B  30           
SHEET    4 AA4 5 LYS B  86  MET B  91 -1  O  MET B  91   N  ALA B  44           
SHEET    5 AA4 5 TYR B  77  TRP B  83 -1  N  TYR B  81   O  TRP B  88           
SHEET    1 AA5 2 LYS B 133  ILE B 134  0                                        
SHEET    2 AA5 2 ALA B 160  GLN B 161 -1  O  ALA B 160   N  ILE B 134           
SHEET    1 AA6 2 ILE B 143  ILE B 145  0                                        
SHEET    2 AA6 2 VAL B 151  LEU B 153 -1  O  ARG B 152   N  LEU B 144           
LINK         C   ALA A 164                 N   TPO A 165     1555   1555  1.33  
LINK         C   TPO A 165                 N   LEU A 166     1555   1555  1.33  
LINK         C   LEU A 170                 N   SEP A 171     1555   1555  1.33  
LINK         C   SEP A 171                 N   PHE A 172     1555   1555  1.33  
LINK         C   LEU B 170                 N   SEP B 171     1555   1555  1.33  
LINK         C   SEP B 171                 N   PHE B 172     1555   1555  1.33  
SITE     1 AC1 10 LEU A  23  GLY A  24  VAL A  31  MET A  91                    
SITE     2 AC1 10 GLU A  92  CYS A  94  GLY A  95  GLY A  97                    
SITE     3 AC1 10 ASP A 101  LEU A 144                                          
SITE     1 AC2 11 LEU B  23  ALA B  44  LYS B  46  VAL B  75                    
SITE     2 AC2 11 MET B  91  GLU B  92  PHE B  93  CYS B  94                    
SITE     3 AC2 11 GLY B  95  ASP B 101  LEU B 144                               
CRYST1  149.932  149.932  156.754  90.00  90.00 120.00 H 3 2        36          
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      0.006670  0.003851  0.000000        0.00000                         
SCALE2      0.000000  0.007701  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006379        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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