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Database: PDB
Entry: 6EIM
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HEADER    TRANSFERASE                             19-SEP-17   6EIM              
TITLE     HUMAN STK10 BOUND TO GW683134A                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 10;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: LYMPHOCYTE-ORIENTED KINASE;                                 
COMPND   5 EC: 2.7.11.1;                                                        
COMPND   6 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: STK10, LOK;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KINASE, INHIBITOR, COMPLEX, LOK, TRANSFERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.J.SORRELL,B.-T.BERGER,E.SALAH,F.VON DELFT,C.BOUNTRA,C.ARROWSMITH,   
AUTHOR   2 A.M.EDWARDS,S.KNAPP,J.M.ELKINS                                       
REVDAT   1   01-NOV-17 6EIM    0                                                
JRNL        AUTH   F.J.SORRELL,J.M.ELKINS                                       
JRNL        TITL   HUMAN STK10 BOUND TO GW683134                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.43 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 1.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.81                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 110494                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.174                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5487                            
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 41.8235 -  4.4417    0.89     3510   179  0.1741 0.1823        
REMARK   3     2  4.4417 -  3.5261    0.94     3582   168  0.1436 0.1320        
REMARK   3     3  3.5261 -  3.0805    0.91     3409   172  0.1527 0.1567        
REMARK   3     4  3.0805 -  2.7989    0.96     3600   190  0.1534 0.1544        
REMARK   3     5  2.7989 -  2.5983    0.97     3571   195  0.1427 0.1632        
REMARK   3     6  2.5983 -  2.4452    0.97     3593   202  0.1396 0.1735        
REMARK   3     7  2.4452 -  2.3227    0.98     3594   182  0.1301 0.1466        
REMARK   3     8  2.3227 -  2.2216    0.94     3459   176  0.1274 0.1583        
REMARK   3     9  2.2216 -  2.1361    0.96     3539   174  0.1327 0.1622        
REMARK   3    10  2.1361 -  2.0624    0.98     3588   203  0.1330 0.1648        
REMARK   3    11  2.0624 -  1.9979    0.97     3589   171  0.1283 0.1525        
REMARK   3    12  1.9979 -  1.9408    0.97     3565   178  0.1320 0.1644        
REMARK   3    13  1.9408 -  1.8897    0.98     3537   203  0.1408 0.1751        
REMARK   3    14  1.8897 -  1.8436    0.98     3577   196  0.1430 0.1877        
REMARK   3    15  1.8436 -  1.8017    0.97     3499   197  0.1457 0.1772        
REMARK   3    16  1.8017 -  1.7633    0.96     3476   225  0.1513 0.1837        
REMARK   3    17  1.7633 -  1.7281    0.90     3314   159  0.1565 0.1896        
REMARK   3    18  1.7281 -  1.6955    0.98     3536   175  0.1631 0.2062        
REMARK   3    19  1.6955 -  1.6652    0.96     3503   175  0.1663 0.2288        
REMARK   3    20  1.6652 -  1.6369    0.97     3521   194  0.1742 0.1915        
REMARK   3    21  1.6369 -  1.6105    0.96     3525   159  0.1782 0.2399        
REMARK   3    22  1.6105 -  1.5858    0.97     3488   194  0.1921 0.2385        
REMARK   3    23  1.5858 -  1.5624    0.96     3508   171  0.1923 0.2616        
REMARK   3    24  1.5624 -  1.5404    0.96     3465   185  0.2062 0.2062        
REMARK   3    25  1.5404 -  1.5196    0.96     3511   183  0.2073 0.2679        
REMARK   3    26  1.5196 -  1.4999    0.96     3417   184  0.2190 0.2451        
REMARK   3    27  1.4999 -  1.4811    0.89     3292   159  0.2296 0.2738        
REMARK   3    28  1.4811 -  1.4633    0.94     3357   179  0.2482 0.2810        
REMARK   3    29  1.4633 -  1.4463    0.94     3417   178  0.2659 0.3109        
REMARK   3    30  1.4463 -  1.4300    0.95     3465   181  0.2835 0.3379        
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.250           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.87                          
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      :  0.004           4847                                  
REMARK   3   ANGLE     :  0.676           6621                                  
REMARK   3   CHIRALITY :  0.063            754                                  
REMARK   3   PLANARITY :  0.005            926                                  
REMARK   3   DIHEDRAL  : 24.267           1843                                  
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 6EIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006653.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID30B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.29                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 110558                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.390                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.83900                            
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 2.6.1                                          
REMARK 200 STARTING MODEL: 2J7T                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG1000, 10% PEG8000, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000       24.73400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.91950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.90600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.91950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.73400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.90600            
REMARK 290   SMTRY3   4  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: 4770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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     SER A    16                                                      
REMARK 465     MET A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     TYR A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     HIS A    25                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     ASP A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     ALA A    46                                                      
REMARK 465     PHE A    47                                                      
REMARK 465     GLY A    48                                                      
REMARK 465     SER B    16                                                      
REMARK 465     MET B    17                                                      
REMARK 465     ARG B    18                                                      
REMARK 465     LYS B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     ARG B    21                                                      
REMARK 465     GLU B    22                                                      
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     VAL A  26    CG1  CG2                                            
REMARK 470     ARG A  27    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A  34    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  49    CG   CD   CE   NZ                                   
REMARK 470     GLU A  57    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  68    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     SER A  71    OG                                                  
REMARK 470     GLU A  72    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  74    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  75    CG   CD1  CD2                                       
REMARK 470     GLU A  76    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 105    NZ                                                  
REMARK 470     ARG A 152    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 181    CG   CD   CE   NZ                                   
REMARK 470     LYS A 184    CG   CD   CE   NZ                                   
REMARK 470     LYS A 210    CE   NZ                                             
REMARK 470     TYR B  23    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B  24    CG   CD   OE1  OE2                                  
REMARK 470     HIS B  25    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B  44    CG   OD1  OD2                                       
REMARK 470     LYS B  49    CE   NZ                                             
REMARK 470     LYS B  54    CE   NZ                                             
REMARK 470     GLU B  68    CD   OE1  OE2                                       
REMARK 470     LYS B  70    CG   CD   CE   NZ                                   
REMARK 470     GLU B  72    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  73    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  74    CG   CD   OE1  OE2                                  
REMARK 470     LEU B  75    CD1  CD2                                            
REMARK 470     GLU B  76    CG   CD   OE1  OE2                                  
REMARK 470     ILE B  79    CD1                                                 
REMARK 470     GLU B 124    OE1  OE2                                            
REMARK 470     ARG B 152    CZ   NH1  NH2                                       
REMARK 470     LYS B 181    NZ                                                  
REMARK 470     LYS B 184    CD   CE   NZ                                        
REMARK 470     MET B 243    SD   CE                                             
REMARK 470     LYS B 262    CD   CE   NZ                                        
REMARK 470     GLU B 313    CD   OE1  OE2                                       
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   H    CYS B   113     H    B6E B   402              1.33            
REMARK 500   H    CYS A   113     H    B6E A   405              1.35            
REMARK 500   H    SER A   179     O    HOH A   506              1.58            
REMARK 500   O    HOH A   610     O    HOH A   712              1.71            
REMARK 500   O    HOH A   686     O    HOH A   823              1.83            
REMARK 500   O    HOH B   754     O    HOH B   816              1.84            
REMARK 500   O    HOH B   508     O    HOH B   765              1.86            
REMARK 500   O    HOH B   515     O    HOH B   769              1.87            
REMARK 500   O    HOH A   673     O    HOH A   736              1.88            
REMARK 500   OD2  ASP A    31     O    HOH A   501              1.89            
REMARK 500   O    HOH A   706     O    HOH A   836              1.90            
REMARK 500   O    HOH B   791     O    HOH B   793              1.91            
REMARK 500   O    HOH A   827     O    HOH A   866              1.92            
REMARK 500   O    HOH B   770     O    HOH B   772              1.97            
REMARK 500   OE2  GLU B   290     O    HOH B   501              1.98            
REMARK 500   O    HOH B   772     O    HOH B   858              2.00            
REMARK 500   O    HOH B   719     O    HOH B   726              2.00            
REMARK 500   O    LYS B    49     O    HOH B   502              2.00            
REMARK 500   O    HOH A   641     O    HOH A   845              2.03            
REMARK 500   O    HOH B   867     O    HOH B   868              2.07            
REMARK 500   O    HOH B   713     O    HOH B   739              2.08            
REMARK 500   OH   TYR A   214     O    HOH A   502              2.08            
REMARK 500   O    HOH A   859     O    HOH A   862              2.09            
REMARK 500   O    HOH B   701     O    HOH B   719              2.09            
REMARK 500   O    HOH A   757     O    HOH A   769              2.10            
REMARK 500   O    HOH A   853     O    HOH A   862              2.11            
REMARK 500   O2   EDO A   403     O    HOH A   503              2.11            
REMARK 500   O    HOH A   536     O    HOH A   821              2.12            
REMARK 500   O    HOH B   704     O    HOH B   806              2.13            
REMARK 500   OE1  GLU A   207     O    HOH A   504              2.13            
REMARK 500   OD2  ASP B    31     O    HOH B   503              2.13            
REMARK 500   O    HOH A   559     O    HOH A   653              2.15            
REMARK 500   O    HOH B   712     O    HOH B   782              2.16            
REMARK 500   O    HOH A   846     O    HOH A   861              2.16            
REMARK 500   O    HOH B   780     O    HOH B   853              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   756     O    HOH B   803     3645     2.02            
REMARK 500   O    HOH A   718     O    HOH B   720     3545     2.02            
REMARK 500   O    HOH B   528     O    HOH B   735     3645     2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 157       40.04   -140.78                                   
REMARK 500    ILE A 233      -45.06     78.22                                   
REMARK 500    THR B  69      -70.77   -118.28                                   
REMARK 500    LYS B  70       -3.29     86.37                                   
REMARK 500    ASP B 157       41.40   -148.65                                   
REMARK 500    PRO B 213       -9.84    -59.75                                   
REMARK 500    ILE B 233      -44.13     76.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 870        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH A 871        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH A 872        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH A 873        DISTANCE =  6.88 ANGSTROMS                       
REMARK 525    HOH A 874        DISTANCE =  7.70 ANGSTROMS                       
REMARK 525    HOH B 865        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH B 866        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH B 867        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH B 868        DISTANCE =  7.02 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue B6E A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue B6E B 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5OWR   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH A DIFFERENT LIGAND                                 
REMARK 900 RELATED ID: 5OWQ   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH A DIFFERENT LIGAND                                 
DBREF  6EIM A   18   317  UNP    O94804   STK10_HUMAN     18    317             
DBREF  6EIM B   18   317  UNP    O94804   STK10_HUMAN     18    317             
SEQADV 6EIM SER A   16  UNP  O94804              EXPRESSION TAG                 
SEQADV 6EIM MET A   17  UNP  O94804              EXPRESSION TAG                 
SEQADV 6EIM ALA A  248  UNP  O94804    LYS   248 CONFLICT                       
SEQADV 6EIM ALA A  251  UNP  O94804    LYS   251 CONFLICT                       
SEQADV 6EIM ALA A  272  UNP  O94804    LYS   272 CONFLICT                       
SEQADV 6EIM SER B   16  UNP  O94804              EXPRESSION TAG                 
SEQADV 6EIM MET B   17  UNP  O94804              EXPRESSION TAG                 
SEQADV 6EIM ALA B  248  UNP  O94804    LYS   248 CONFLICT                       
SEQADV 6EIM ALA B  251  UNP  O94804    LYS   251 CONFLICT                       
SEQADV 6EIM ALA B  272  UNP  O94804    LYS   272 CONFLICT                       
SEQRES   1 A  302  SER MET ARG LYS SER ARG GLU TYR GLU HIS VAL ARG ARG          
SEQRES   2 A  302  ASP LEU ASP PRO ASN GLU VAL TRP GLU ILE VAL GLY GLU          
SEQRES   3 A  302  LEU GLY ASP GLY ALA PHE GLY LYS VAL TYR LYS ALA LYS          
SEQRES   4 A  302  ASN LYS GLU THR GLY ALA LEU ALA ALA ALA LYS VAL ILE          
SEQRES   5 A  302  GLU THR LYS SER GLU GLU GLU LEU GLU ASP TYR ILE VAL          
SEQRES   6 A  302  GLU ILE GLU ILE LEU ALA THR CYS ASP HIS PRO TYR ILE          
SEQRES   7 A  302  VAL LYS LEU LEU GLY ALA TYR TYR HIS ASP GLY LYS LEU          
SEQRES   8 A  302  TRP ILE MET ILE GLU PHE CYS PRO GLY GLY ALA VAL ASP          
SEQRES   9 A  302  ALA ILE MET LEU GLU LEU ASP ARG GLY LEU THR GLU PRO          
SEQRES  10 A  302  GLN ILE GLN VAL VAL CYS ARG GLN MET LEU GLU ALA LEU          
SEQRES  11 A  302  ASN PHE LEU HIS SER LYS ARG ILE ILE HIS ARG ASP LEU          
SEQRES  12 A  302  LYS ALA GLY ASN VAL LEU MET THR LEU GLU GLY ASP ILE          
SEQRES  13 A  302  ARG LEU ALA ASP PHE GLY VAL SER ALA LYS ASN LEU LYS          
SEQRES  14 A  302  THR LEU GLN LYS ARG ASP SER PHE ILE GLY THR PRO TYR          
SEQRES  15 A  302  TRP MET ALA PRO GLU VAL VAL MET CYS GLU THR MET LYS          
SEQRES  16 A  302  ASP THR PRO TYR ASP TYR LYS ALA ASP ILE TRP SER LEU          
SEQRES  17 A  302  GLY ILE THR LEU ILE GLU MET ALA GLN ILE GLU PRO PRO          
SEQRES  18 A  302  HIS HIS GLU LEU ASN PRO MET ARG VAL LEU LEU ALA ILE          
SEQRES  19 A  302  ALA ALA SER ASP PRO PRO THR LEU LEU THR PRO SER LYS          
SEQRES  20 A  302  TRP SER VAL GLU PHE ARG ASP PHE LEU ALA ILE ALA LEU          
SEQRES  21 A  302  ASP LYS ASN PRO GLU THR ARG PRO SER ALA ALA GLN LEU          
SEQRES  22 A  302  LEU GLU HIS PRO PHE VAL SER SER ILE THR SER ASN LYS          
SEQRES  23 A  302  ALA LEU ARG GLU LEU VAL ALA GLU ALA LYS ALA GLU VAL          
SEQRES  24 A  302  MET GLU GLU                                                  
SEQRES   1 B  302  SER MET ARG LYS SER ARG GLU TYR GLU HIS VAL ARG ARG          
SEQRES   2 B  302  ASP LEU ASP PRO ASN GLU VAL TRP GLU ILE VAL GLY GLU          
SEQRES   3 B  302  LEU GLY ASP GLY ALA PHE GLY LYS VAL TYR LYS ALA LYS          
SEQRES   4 B  302  ASN LYS GLU THR GLY ALA LEU ALA ALA ALA LYS VAL ILE          
SEQRES   5 B  302  GLU THR LYS SER GLU GLU GLU LEU GLU ASP TYR ILE VAL          
SEQRES   6 B  302  GLU ILE GLU ILE LEU ALA THR CYS ASP HIS PRO TYR ILE          
SEQRES   7 B  302  VAL LYS LEU LEU GLY ALA TYR TYR HIS ASP GLY LYS LEU          
SEQRES   8 B  302  TRP ILE MET ILE GLU PHE CYS PRO GLY GLY ALA VAL ASP          
SEQRES   9 B  302  ALA ILE MET LEU GLU LEU ASP ARG GLY LEU THR GLU PRO          
SEQRES  10 B  302  GLN ILE GLN VAL VAL CYS ARG GLN MET LEU GLU ALA LEU          
SEQRES  11 B  302  ASN PHE LEU HIS SER LYS ARG ILE ILE HIS ARG ASP LEU          
SEQRES  12 B  302  LYS ALA GLY ASN VAL LEU MET THR LEU GLU GLY ASP ILE          
SEQRES  13 B  302  ARG LEU ALA ASP PHE GLY VAL SER ALA LYS ASN LEU LYS          
SEQRES  14 B  302  THR LEU GLN LYS ARG ASP SER PHE ILE GLY THR PRO TYR          
SEQRES  15 B  302  TRP MET ALA PRO GLU VAL VAL MET CYS GLU THR MET LYS          
SEQRES  16 B  302  ASP THR PRO TYR ASP TYR LYS ALA ASP ILE TRP SER LEU          
SEQRES  17 B  302  GLY ILE THR LEU ILE GLU MET ALA GLN ILE GLU PRO PRO          
SEQRES  18 B  302  HIS HIS GLU LEU ASN PRO MET ARG VAL LEU LEU ALA ILE          
SEQRES  19 B  302  ALA ALA SER ASP PRO PRO THR LEU LEU THR PRO SER LYS          
SEQRES  20 B  302  TRP SER VAL GLU PHE ARG ASP PHE LEU ALA ILE ALA LEU          
SEQRES  21 B  302  ASP LYS ASN PRO GLU THR ARG PRO SER ALA ALA GLN LEU          
SEQRES  22 B  302  LEU GLU HIS PRO PHE VAL SER SER ILE THR SER ASN LYS          
SEQRES  23 B  302  ALA LEU ARG GLU LEU VAL ALA GLU ALA LYS ALA GLU VAL          
SEQRES  24 B  302  MET GLU GLU                                                  
HET    EDO  A 401      10                                                       
HET    EDO  A 402      10                                                       
HET    EDO  A 403      10                                                       
HET    EDO  A 404      10                                                       
HET    B6E  A 405      56                                                       
HET    EDO  B 401      10                                                       
HET    B6E  B 402      56                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     B6E ~{N}-[5-[4-[[2-FLUORANYL-5-(TRIFLUOROMETHYL)                     
HETNAM   2 B6E  PHENYL]CARBAMOYLAMINO]PHENOXY]-1~{H}-BENZIMIDAZOL-2-            
HETNAM   3 B6E  YL]FURAN-2-CARBOXAMIDE                                          
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    5(C2 H6 O2)                                                  
FORMUL   7  B6E    2(C26 H17 F4 N5 O4)                                          
FORMUL  10  HOH   *742(H2 O)                                                    
HELIX    1 AA1 ASP A   31  GLU A   34  5                                   4    
HELIX    2 AA2 SER A   71  CYS A   88  1                                  18    
HELIX    3 AA3 VAL A  118  ASP A  126  1                                   9    
HELIX    4 AA4 THR A  130  LYS A  151  1                                  22    
HELIX    5 AA5 LYS A  159  GLY A  161  5                                   3    
HELIX    6 AA6 SER A  179  LYS A  188  1                                  10    
HELIX    7 AA7 THR A  195  MET A  199  5                                   5    
HELIX    8 AA8 ALA A  200  THR A  208  1                                   9    
HELIX    9 AA9 THR A  212  ASP A  215  5                                   4    
HELIX   10 AB1 TYR A  216  ILE A  233  1                                  18    
HELIX   11 AB2 ASN A  241  SER A  252  1                                  12    
HELIX   12 AB3 THR A  259  TRP A  263  5                                   5    
HELIX   13 AB4 SER A  264  LEU A  275  1                                  12    
HELIX   14 AB5 SER A  284  LEU A  289  1                                   6    
HELIX   15 AB6 ASN A  300  MET A  315  1                                  16    
HELIX   16 AB7 ASP B   31  GLU B   34  5                                   4    
HELIX   17 AB8 SER B   71  CYS B   88  1                                  18    
HELIX   18 AB9 VAL B  118  ASP B  126  1                                   9    
HELIX   19 AC1 THR B  130  LYS B  151  1                                  22    
HELIX   20 AC2 LYS B  159  GLY B  161  5                                   3    
HELIX   21 AC3 SER B  179  LYS B  181  5                                   3    
HELIX   22 AC4 ASN B  182  LYS B  188  1                                   7    
HELIX   23 AC5 THR B  195  MET B  199  5                                   5    
HELIX   24 AC6 ALA B  200  THR B  208  1                                   9    
HELIX   25 AC7 THR B  212  ASP B  215  5                                   4    
HELIX   26 AC8 TYR B  216  ILE B  233  1                                  18    
HELIX   27 AC9 MET B  243  SER B  252  1                                  10    
HELIX   28 AD1 THR B  259  TRP B  263  5                                   5    
HELIX   29 AD2 SER B  264  LEU B  275  1                                  12    
HELIX   30 AD3 SER B  284  LEU B  289  1                                   6    
HELIX   31 AD4 ASN B  300  MET B  315  1                                  16    
SHEET    1 AA1 5 TRP A  36  GLU A  41  0                                        
SHEET    2 AA1 5 VAL A  50  ASN A  55 -1  O  LYS A  54   N  GLU A  37           
SHEET    3 AA1 5 LEU A  61  GLU A  68 -1  O  ALA A  62   N  ALA A  53           
SHEET    4 AA1 5 LYS A 105  GLU A 111 -1  O  ILE A 110   N  ALA A  63           
SHEET    5 AA1 5 LEU A  96  HIS A 102 -1  N  TYR A 100   O  TRP A 107           
SHEET    1 AA2 3 GLY A 116  ALA A 117  0                                        
SHEET    2 AA2 3 VAL A 163  MET A 165 -1  O  MET A 165   N  GLY A 116           
SHEET    3 AA2 3 ILE A 171  LEU A 173 -1  O  ARG A 172   N  LEU A 164           
SHEET    1 AA3 5 TRP B  36  GLU B  41  0                                        
SHEET    2 AA3 5 VAL B  50  ASN B  55 -1  O  LYS B  52   N  VAL B  39           
SHEET    3 AA3 5 LEU B  61  GLU B  68 -1  O  ALA B  62   N  ALA B  53           
SHEET    4 AA3 5 LYS B 105  GLU B 111 -1  O  ILE B 110   N  ALA B  63           
SHEET    5 AA3 5 LEU B  96  HIS B 102 -1  N  TYR B 100   O  TRP B 107           
SHEET    1 AA4 3 GLY B 116  ALA B 117  0                                        
SHEET    2 AA4 3 VAL B 163  MET B 165 -1  O  MET B 165   N  GLY B 116           
SHEET    3 AA4 3 ILE B 171  LEU B 173 -1  O  ARG B 172   N  LEU B 164           
SSBOND   1 CYS A  206    CYS B  206                          1555   1555  2.04  
SITE     1 AC1  7 GLY A 115  GLU A 124  ALA A 310  B6E A 405                    
SITE     2 AC1  7 HOH A 573  HOH A 597  HOH A 602                               
SITE     1 AC2  5 THR A 259  GLN A 287  HOH A 538  HOH A 583                    
SITE     2 AC2  5 HOH A 640                                                     
SITE     1 AC3  4 LYS A 159  GLY A 161  HOH A 503  HOH A 551                    
SITE     1 AC4  5 GLU A 234  HIS A 238  HOH A 534  HOH A 549                    
SITE     2 AC4  5 HOH A 692                                                     
SITE     1 AC5 20 ALA A  63  GLU A  81  ILE A  84  ILE A  93                    
SITE     2 AC5 20 VAL A  94  ILE A 110  GLU A 111  PHE A 112                    
SITE     3 AC5 20 CYS A 113  PRO A 114  GLY A 116  LEU A 148                    
SITE     4 AC5 20 HIS A 155  ALA A 174  ASP A 175  PHE A 176                    
SITE     5 AC5 20 LEU A 183  EDO A 401  HOH A 576  HOH A 684                    
SITE     1 AC6  7 LEU A 167  GLU A 168  ARG A 304  ASN B 146                    
SITE     2 AC6  7 PHE B 147  SER B 150  HOH B 633                               
SITE     1 AC7 21 VAL B  50  ALA B  63  GLU B  81  ILE B  84                    
SITE     2 AC7 21 ILE B  93  VAL B  94  ILE B 110  GLU B 111                    
SITE     3 AC7 21 PHE B 112  CYS B 113  PRO B 114  GLY B 116                    
SITE     4 AC7 21 LEU B 148  LEU B 173  ALA B 174  ASP B 175                    
SITE     5 AC7 21 PHE B 176  LEU B 183  HOH B 552  HOH B 683                    
SITE     6 AC7 21 HOH B 806                                                     
CRYST1   49.468   99.812  125.839  90.00  90.00  90.00 P 21 21 21    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      0.020215  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010019  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007947        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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