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Database: PDB
Entry: 6NG0
LinkDB: 6NG0
Original site: 6NG0 
HEADER    TRANSFERASE                             21-DEC-18   6NG0              
TITLE     CRYSTAL STRUCTURE OF HPK1 KINASE DOMAIN T165E,S171E PHOSPHOMIMETIC    
TITLE    2 MUTANT IN COMPLEX WITH SUNITINIB IN THE INACTIVE 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_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    KINASE, 3D DOMAIN SWAP, INACTIVE STATE, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.JOHNSON,M.MCTIGUE,C.N.CRONIN                                        
REVDAT   5   13-MAR-24 6NG0    1       COMPND HETNAM                            
REVDAT   4   26-JUN-19 6NG0    1       JRNL                                     
REVDAT   3   19-JUN-19 6NG0    1       JRNL                                     
REVDAT   2   08-MAY-19 6NG0    1       JRNL                                     
REVDAT   1   01-MAY-19 6NG0    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.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 42208                          
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)  : 0.202                          
REMARK   3   R VALUE            (WORKING SET)  : 0.201                          
REMARK   3   FREE R VALUE                      : 0.229                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.120                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2160                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 50                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.05                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.06                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.55                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 845                      
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2200                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 806                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2198                   
REMARK   3   BIN FREE R VALUE                        : 0.2239                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.62                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 39                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4336                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 320                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.17                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.10790                                             
REMARK   3    B22 (A**2) : -0.59080                                             
REMARK   3    B33 (A**2) : 8.69870                                              
REMARK   3    B12 (A**2) : -7.99280                                             
REMARK   3    B13 (A**2) : 6.08210                                              
REMARK   3    B23 (A**2) : -8.13660                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.280               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.185               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.156               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.186               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.158               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4486   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6076   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1535   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 787    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4486   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 578    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 5354   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.99                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.76                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.71                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6NG0 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_1000236783.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-AUG-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 180                                
REMARK 200  PH                             : 8.0                                
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          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43684                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.026                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.176                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.03600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50100                            
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   (%): 52.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 NL PROTEIN (15 MG/ML) PLUS 300 NL    
REMARK 280  RESERVOIR SOLUTION (0.1 M TRIS, PH 8.0, 17.5 % 1,6-HEXANEDIOL,      
REMARK 280  10 MM MAGNESIUM SULFATE, 24 MM BARIUM ACETATE), VAPOR DIFFUSION,    
REMARK 280  SITTING DROP, TEMPERATURE 286.15K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL                        
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     GLY A    26                                                      
REMARK 465     THR A    27                                                      
REMARK 465     TYR A    28                                                      
REMARK 465     GLN A   161                                                      
REMARK 465     ILE A   162                                                      
REMARK 465     GLY A   163                                                      
REMARK 465     ALA A   164                                                      
REMARK 465     GLU A   165                                                      
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     ASP B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     THR B    27                                                      
REMARK 465     TYR B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     MET B    50                                                      
REMARK 465     GLU B    51                                                      
REMARK 465     PRO B    52                                                      
REMARK 465     ASP B    53                                                      
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     ASP A  53    CG   OD1  OD2                                       
REMARK 470     ILE A 158    CG1  CG2  CD1                                       
REMARK 470     SER A 159    OG                                                  
REMARK 470     LEU A 166    CG   CD1  CD2                                       
REMARK 470     ARG A 168    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 169    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 170    CG   CD1  CD2                                       
REMARK 470     GLU A 171    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 172    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 222    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     ASN A 293    CG   OD1  ND2                                       
REMARK 470     LYS A 296    CG   CD   CE   NZ                                   
REMARK 470     ASP B   7    CG   OD1  OD2                                       
REMARK 470     ILE B   8    CG1  CG2  CD1                                       
REMARK 470     ASN B  10    CG   OD1  ND2                                       
REMARK 470     ARG B  11    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  22    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  30    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  49    CG   CD   CE   NZ                                   
REMARK 470     ASP B  54    CG   OD1  OD2                                       
REMARK 470     ASP B  55    CG   OD1  OD2                                       
REMARK 470     VAL B  56    CG1  CG2                                            
REMARK 470     SER B  57    OG                                                  
REMARK 470     LEU B  59    CG   CD1  CD2                                       
REMARK 470     GLN B  60    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  82    CG   CD1  CD2                                       
REMARK 470     TRP B  83    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  83    CZ3  CH2                                            
REMARK 470     LEU B  84    CG   CD1  CD2                                       
REMARK 470     GLN B  85    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 165    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 168    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 169    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 171    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 172    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE B 173    CG1  CG2  CD1                                       
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
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    SER A 108      141.39    -39.84                                   
REMARK 500    ARG A 136       -8.02     77.74                                   
REMARK 500    LYS A 240      -74.47   -106.43                                   
REMARK 500    LEU A 255       38.73    -92.55                                   
REMARK 500    ASP B  12      129.22    -39.20                                   
REMARK 500    LEU B  20     -165.85   -122.51                                   
REMARK 500    GLN B  85       -0.29     66.81                                   
REMARK 500    ARG B 136       -7.21     68.34                                   
REMARK 500    ASP B 137       44.79   -141.90                                   
REMARK 500    LYS B 189       23.99   -146.59                                   
REMARK 500    LEU B 255       44.11    -91.96                                   
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 9000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue B49 B 9000                
DBREF  6NG0 A    1   307  UNP    Q92918   M4K1_HUMAN       1    307             
DBREF  6NG0 B    1   307  UNP    Q92918   M4K1_HUMAN       1    307             
SEQADV 6NG0 GLY A   -1  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6NG0 SER A    0  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6NG0 GLU A  165  UNP  Q92918    THR   165 ENGINEERED MUTATION            
SEQADV 6NG0 GLU A  171  UNP  Q92918    SER   171 ENGINEERED MUTATION            
SEQADV 6NG0 GLY B   -1  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6NG0 SER B    0  UNP  Q92918              EXPRESSION TAG                 
SEQADV 6NG0 GLU B  165  UNP  Q92918    THR   165 ENGINEERED MUTATION            
SEQADV 6NG0 GLU B  171  UNP  Q92918    SER   171 ENGINEERED MUTATION            
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 GLU LEU ALA          
SEQRES  14 A  309  ARG ARG LEU GLU 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 GLU LEU ALA          
SEQRES  14 B  309  ARG ARG LEU GLU 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                      
HET    B49  A9000      29                                                       
HET    B49  B9000      29                                                       
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-CARBO XAMIDE                                          
HETSYN     B49 SUNITINIB                                                        
FORMUL   3  B49    2(C22 H27 F N4 O2)                                           
FORMUL   5  HOH   *320(H2 O)                                                    
HELIX    1 AA1 ASP A   12  ASP A   15  5                                   4    
HELIX    2 AA2 ASP A   55  THR A   68  1                                  14    
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 ARG A  168  ILE A  173  1                                   6    
HELIX    7 AA7 ALA A  180  GLY A  190  1                                  11    
HELIX    8 AA8 LEU A  195  LEU A  211  1                                  17    
HELIX    9 AA9 HIS A  219  LYS A  229  1                                  11    
HELIX   10 AB1 SER A  244  LEU A  255  1                                  12    
HELIX   11 AB2 SER A  264  LEU A  269  1                                   6    
HELIX   12 AB3 HIS A  271  GLN A  276  1                                   6    
HELIX   13 AB4 ARG A  281  ASN A  293  1                                  13    
HELIX   14 AB5 ASP B   12  ASP B   15  5                                   4    
HELIX   15 AB6 ASP B   55  THR B   68  1                                  14    
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 ILE B  158  PHE B  172  1                                  15    
HELIX   20 AC2 ALA B  180  GLY B  190  1                                  11    
HELIX   21 AC3 LEU B  195  LEU B  211  1                                  17    
HELIX   22 AC4 HIS B  219  THR B  228  1                                  10    
HELIX   23 AC5 GLU B  239  TRP B  243  5                                   5    
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  ASN B  293  1                                  13    
SHEET    1 AA1 6 ILE A   8  PHE A   9  0                                        
SHEET    2 AA1 6 TYR A  77  LEU A  82  1  O  SER A  80   N  PHE A   9           
SHEET    3 AA1 6 LYS A  86  GLU A  92 -1  O  CYS A  90   N  GLY A  79           
SHEET    4 AA1 6 LEU A  42  LYS A  49 -1  N  LYS A  46   O  ILE A  89           
SHEET    5 AA1 6 GLU A  30  ASP A  36 -1  N  GLU A  30   O  MET A  47           
SHEET    6 AA1 6 TYR A  17  GLY A  24 -1  N  GLY A  24   O  VAL A  31           
SHEET    1 AA2 2 ILE A 143  ILE A 145  0                                        
SHEET    2 AA2 2 VAL A 151  LEU A 153 -1  O  ARG A 152   N  LEU A 144           
SHEET    1 AA3 6 ILE B   8  PHE B   9  0                                        
SHEET    2 AA3 6 TYR B  77  TRP B  83  1  O  LEU B  82   N  PHE B   9           
SHEET    3 AA3 6 LYS B  86  GLU B  92 -1  O  CYS B  90   N  GLY B  79           
SHEET    4 AA3 6 LEU B  42  VAL B  48 -1  N  VAL B  48   O  LEU B  87           
SHEET    5 AA3 6 VAL B  31  ASP B  36 -1  N  PHE B  32   O  LEU B  45           
SHEET    6 AA3 6 TYR B  17  GLY B  24 -1  N  LEU B  23   O  VAL B  31           
SHEET    1 AA4 2 ILE B 143  ILE B 145  0                                        
SHEET    2 AA4 2 VAL B 151  LEU B 153 -1  O  ARG B 152   N  LEU B 144           
SITE     1 AC1 12 LEU A  23  ALA A  44  MET A  91  GLU A  92                    
SITE     2 AC1 12 PHE A  93  CYS A  94  GLY A  95  GLY A  97                    
SITE     3 AC1 12 ASP A 101  LEU A 144  ALA A 154  ASP A 155                    
SITE     1 AC2 13 LEU B  23  ALA B  44  MET B  91  GLU B  92                    
SITE     2 AC2 13 PHE B  93  CYS B  94  GLY B  95  GLY B  97                    
SITE     3 AC2 13 ASP B 101  LEU B 144  ASP B 155  PHE B 156                    
SITE     4 AC2 13 HOH B9139                                                     
CRYST1   55.810   58.920   60.930  82.44  82.31  64.34 P 1           2          
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      0.017918 -0.008608 -0.001716        0.00000                         
SCALE2      0.000000  0.018829 -0.001557        0.00000                         
SCALE3      0.000000  0.000000  0.016618        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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