GenomeNet

Database: PDB
Entry: 2XNG
LinkDB: 2XNG
Original site: 2XNG 
HEADER    TRANSFERASE                             02-AUG-10   2XNG              
TITLE     STRUCTURE OF AURORA-A BOUND TO A SELECTIVE IMIDAZOPYRAZINE INHIBITOR  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 6;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 122-392;                        
COMPND   5 SYNONYM: AURORA KINASE A, SERINE/THREONINE-PROTEIN KINASE AURORA-A,  
COMPND   6 SERINE/THREONINE-PROTEIN KINASE 15, AURORA/IPL1-RELATED KINASE 1,    
COMPND   7 BREAST TUMOR-AMPLIFIED KINASE, AURORA-RELATED KINASE 1, ARK-1, HARK1;
COMPND   8 EC: 2.7.11.1;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SER-THR PROTEIN KINASE COMPLEX, PROTO-ONCOGENE, KINASE, MITOSIS, CELL 
KEYWDS   2 CYCLE, MICROTUBULE, TRANSFERASE, CYTOSKELETON, CELL DIVISION         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KOSMOPOULOU,R.BAYLISS                                               
REVDAT   3   28-FEB-18 2XNG    1       JRNL                                     
REVDAT   2   29-SEP-10 2XNG    1       JRNL                                     
REVDAT   1   22-SEP-10 2XNG    0                                                
JRNL        AUTH   N.BOULOC,J.M.LARGE,M.KOSMOPOULOU,C.SUN,A.FAISAL,M.MATTEUCCI, 
JRNL        AUTH 2 J.REYNISSON,N.BROWN,B.ATRASH,J.BLAGG,E.MCDONALD,             
JRNL        AUTH 3 S.LINARDOPOULOS,R.BAYLISS,V.BAVETSIAS                        
JRNL        TITL   STRUCTURE-BASED DESIGN OF IMIDAZO[1,2-A]PYRAZINE DERIVATIVES 
JRNL        TITL 2 AS SELECTIVE INHIBITORS OF AURORA-A KINASE IN CELLS.         
JRNL        REF    BIOORG. MED. CHEM. LETT.      V.  20  5988 2010              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   20833547                                                     
JRNL        DOI    10.1016/J.BMCL.2010.08.091                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.10                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.410                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 11101                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 531                             
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 71.1237 -  4.1353    1.00     2814   125  0.2174 0.2490        
REMARK   3     2  4.1353 -  3.2823    1.00     2622   128  0.1937 0.2442        
REMARK   3     3  3.2823 -  2.8674    1.00     2563   156  0.2197 0.3122        
REMARK   3     4  2.8674 -  2.6052    1.00     2571   122  0.2505 0.3251        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 49.17                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.400           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.01630                                             
REMARK   3    B22 (A**2) : -3.01630                                             
REMARK   3    B33 (A**2) : 6.03260                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.008           2067                                  
REMARK   3   ANGLE     :  1.281           2823                                  
REMARK   3   CHIRALITY :  0.069            308                                  
REMARK   3   PLANARITY :  0.005            354                                  
REMARK   3   DIHEDRAL  : 20.289            721                                  
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 2XNG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-AUG-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290044932.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9334                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11148                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 86.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.00                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 99.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.34000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1OL7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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       57.20933            
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      114.41867            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       85.81400            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      143.02333            
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       28.60467            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       57.20933            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      114.41867            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      143.02333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       85.81400            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       28.60467            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     SER A   123                                                      
REMARK 465     LYS A   124                                                      
REMARK 465     LYS A   125                                                      
REMARK 465     ARG A   126                                                      
REMARK 465     PRO A   282                                                      
REMARK 465     SER A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     ARG A   285                                                      
REMARK 465     ARG A   286                                                      
REMARK 465     THR A   287                                                      
REMARK 465     THR A   288                                                      
REMARK 465     LEU A   289                                                      
REMARK 465     CYS A   290                                                      
REMARK 465     GLY A   291                                                      
REMARK 465     SER A   391                                                      
REMARK 465     ASN A   392                                                      
REMARK 465     CYS A   393                                                      
REMARK 465     GLN A   394                                                      
REMARK 465     ASN A   395                                                      
REMARK 465     LYS A   396                                                      
REMARK 465     GLU A   397                                                      
REMARK 465     SER A   398                                                      
REMARK 465     ALA A   399                                                      
REMARK 465     SER A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     GLN A   402                                                      
REMARK 465     SER A   403                                                      
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     GLN A 127    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 131    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 141    CG   CD   CE   NZ                                   
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
REMARK 470     ASN A 146    CG   OD1  ND2                                       
REMARK 470     LYS A 166    CG   CD   CE   NZ                                   
REMARK 470     GLN A 168    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 169    CG   CD1  CD2                                       
REMARK 470     GLU A 170    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 171    CG   CD   CE   NZ                                   
REMARK 470     VAL A 174    CG1  CG2                                            
REMARK 470     GLU A 175    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 176    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 177    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 179    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 180    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 183    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 205    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 220    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 224    CG   CD   CE   NZ                                   
REMARK 470     GLN A 231    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 250    CG   CD   CE   NZ                                   
REMARK 470     ARG A 251    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP A 277    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 277    CZ3  CH2                                            
REMARK 470     HIS A 280    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET A 305    CG   SD   CE                                        
REMARK 470     GLU A 336    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 339    CG   CD   CE   NZ                                   
REMARK 470     GLU A 354    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 375    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 389    CG   CD   CE   NZ                                   
REMARK 470     PRO A 390    CA   C    O    CB   CG   CD                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 131        6.87    -69.18                                   
REMARK 500    LYS A 143      -74.91    -69.26                                   
REMARK 500    PHE A 200     -179.37   -176.70                                   
REMARK 500    ASP A 202     -133.95   -124.33                                   
REMARK 500    SER A 226      -63.99     75.94                                   
REMARK 500    ARG A 255      -21.18     78.84                                   
REMARK 500    ASP A 274       70.43     56.36                                   
REMARK 500    PHE A 275       38.13    -73.62                                   
REMARK 500    ARG A 304      170.37    -38.91                                   
REMARK 500    ASP A 307     -160.97   -123.88                                   
REMARK 500    GLU A 308       -8.39    -54.82                                   
REMARK 500    LEU A 364       56.81    -91.59                                   
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 A0H A 1391                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MUO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF AURORA-2, AN ONCOGENIC SERINE-THREONINE KINASE  
REMARK 900 RELATED ID: 2X6D   RELATED DB: PDB                                   
REMARK 900 AURORA-A BOUND TO AN INHIBITOR                                       
REMARK 900 RELATED ID: 2J50   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA-2 IN COMPLEX WITH PHA -739358                    
REMARK 900 RELATED ID: 2W1D   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF AURORA KINASE IN COMPLEX WITH INHIBITOR   
REMARK 900 RELATED ID: 1OL6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF UNPHOSPHORYLATED D274N MUTANT OF AURORA-A               
REMARK 900 RELATED ID: 2BMC   RELATED DB: PDB                                   
REMARK 900 AURORA-2 T287D T288D COMPLEXED WITH PHA- 680632                      
REMARK 900 RELATED ID: 2J4Z   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA-2 IN COMPLEX WITH PHA -680626                    
REMARK 900 RELATED ID: 2C6E   RELATED DB: PDB                                   
REMARK 900 AURORA A KINASE ACTIVATED MUTANT (T287D) IN COMPLEX WITH A 5-        
REMARK 900 AMINOPYRIMIDINYL QUINAZOLINE INHIBITOR                               
REMARK 900 RELATED ID: 1OL5   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA-A 122-403, PHOSPHORYLATED ON THR287, THR288 AND  
REMARK 900 BOUND TO TPX2 1-43                                                   
REMARK 900 RELATED ID: 2X81   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA A IN COMPLEX WITH MLN8054                        
REMARK 900 RELATED ID: 2C6D   RELATED DB: PDB                                   
REMARK 900 AURORA A KINASE ACTIVATED MUTANT (T287D) IN COMPLEX WITH ADPNP       
REMARK 900 RELATED ID: 2WTW   RELATED DB: PDB                                   
REMARK 900 AURORA-A INHIBITOR STRUCTURE (2ND CRYSTAL FORM)                      
REMARK 900 RELATED ID: 2WQE   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF S155R AURORA-A SOMATIC MUTANT                           
REMARK 900 RELATED ID: 2W1C   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF AURORA KINASE IN COMPLEX WITH INHIBITOR   
REMARK 900 RELATED ID: 2W1G   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF AURORA KINASE IN COMPLEX WITH INHIBITOR   
REMARK 900 RELATED ID: 2WTV   RELATED DB: PDB                                   
REMARK 900 AURORA-A INHIBITOR STRUCTURE                                         
REMARK 900 RELATED ID: 1OL7   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN AURORA-A 122-403 PHOSPHORYLATED ON THR287, THR288 
REMARK 900 RELATED ID: 2W1E   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF AURORA KINASE IN COMPLEX WITH INHIBITOR   
REMARK 900 RELATED ID: 2W1F   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF AURORA KINASE IN COMPLEX WITH INHIBITOR   
REMARK 900 RELATED ID: 2X6E   RELATED DB: PDB                                   
REMARK 900 AURORA-A BOUND TO AN INHIBITOR                                       
REMARK 900 RELATED ID: 1MQ4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF AURORA-A PROTEIN KINASE                         
REMARK 900 RELATED ID: 2XNE   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA-A BOUND TO AN IMIDAZOPYRAZINE INHIBITOR          
DBREF  2XNG A  122   403  UNP    O14965   STK6_HUMAN     122    403             
SEQADV 2XNG MET A  121  UNP  O14965              EXPRESSION TAG                 
SEQRES   1 A  283  MET GLU SER LYS LYS ARG GLN TRP ALA LEU GLU ASP PHE          
SEQRES   2 A  283  GLU ILE GLY ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN          
SEQRES   3 A  283  VAL TYR LEU ALA ARG GLU LYS GLN SER LYS PHE ILE LEU          
SEQRES   4 A  283  ALA LEU LYS VAL LEU PHE LYS ALA GLN LEU GLU LYS ALA          
SEQRES   5 A  283  GLY VAL GLU HIS GLN LEU ARG ARG GLU VAL GLU ILE GLN          
SEQRES   6 A  283  SER HIS LEU ARG HIS PRO ASN ILE LEU ARG LEU TYR GLY          
SEQRES   7 A  283  TYR PHE HIS ASP ALA THR ARG VAL TYR LEU ILE LEU GLU          
SEQRES   8 A  283  TYR ALA PRO LEU GLY THR VAL TYR ARG GLU LEU GLN LYS          
SEQRES   9 A  283  LEU SER LYS PHE ASP GLU GLN ARG THR ALA THR TYR ILE          
SEQRES  10 A  283  THR GLU LEU ALA ASN ALA LEU SER TYR CYS HIS SER LYS          
SEQRES  11 A  283  ARG VAL ILE HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU          
SEQRES  12 A  283  LEU GLY SER ALA GLY GLU LEU LYS ILE ALA ASP PHE GLY          
SEQRES  13 A  283  TRP SER VAL HIS ALA PRO SER SER ARG ARG THR THR LEU          
SEQRES  14 A  283  CYS GLY THR LEU ASP TYR LEU PRO PRO GLU MET ILE GLU          
SEQRES  15 A  283  GLY ARG MET HIS ASP GLU LYS VAL ASP LEU TRP SER LEU          
SEQRES  16 A  283  GLY VAL LEU CYS TYR GLU PHE LEU VAL GLY LYS PRO PRO          
SEQRES  17 A  283  PHE GLU ALA ASN THR TYR GLN GLU THR TYR LYS ARG ILE          
SEQRES  18 A  283  SER ARG VAL GLU PHE THR PHE PRO ASP PHE VAL THR GLU          
SEQRES  19 A  283  GLY ALA ARG ASP LEU ILE SER ARG LEU LEU LYS HIS ASN          
SEQRES  20 A  283  PRO SER GLN ARG PRO MET LEU ARG GLU VAL LEU GLU HIS          
SEQRES  21 A  283  PRO TRP ILE THR ALA ASN SER SER LYS PRO SER ASN CYS          
SEQRES  22 A  283  GLN ASN LYS GLU SER ALA SER LYS GLN SER                      
HET    A0H  A1391      70                                                       
HETNAM     A0H N-(3-{3-CHLORO-8-[(4-MORPHOLIN-4-YLPHENYL)                       
HETNAM   2 A0H  AMINO]IMIDAZO[1,2-A]PYRAZIN-6-YL}BENZYL)                        
HETNAM   3 A0H  METHANESULFONAMIDE                                              
FORMUL   2  A0H    C24 H25 CL N6 O3 S                                           
FORMUL   3  HOH   *25(H2 O)                                                     
HELIX    1   1 ALA A  129  GLU A  131  5                                   3    
HELIX    2   2 LYS A  166  ALA A  172  1                                   7    
HELIX    3   3 VAL A  174  LEU A  188  1                                  15    
HELIX    4   4 THR A  217  SER A  226  1                                  10    
HELIX    5   5 ASP A  229  LYS A  250  1                                  22    
HELIX    6   6 LYS A  258  GLU A  260  5                                   3    
HELIX    7   7 PRO A  297  GLU A  302  1                                   6    
HELIX    8   8 LYS A  309  GLY A  325  1                                  17    
HELIX    9   9 THR A  333  ARG A  343  1                                  11    
HELIX   10  10 THR A  353  LEU A  364  1                                  12    
HELIX   11  11 ASN A  367  ARG A  371  5                                   5    
HELIX   12  12 MET A  373  GLU A  379  1                                   7    
HELIX   13  13 HIS A  380  SER A  387  1                                   8    
SHEET    1  AA 5 PHE A 133  LYS A 141  0                                        
SHEET    2  AA 5 ASN A 146  GLU A 152 -1  O  VAL A 147   N  LEU A 139           
SHEET    3  AA 5 ILE A 158  PHE A 165 -1  O  LEU A 159   N  ALA A 150           
SHEET    4  AA 5 ARG A 205  LEU A 210 -1  O  VAL A 206   N  LEU A 164           
SHEET    5  AA 5 LEU A 196  HIS A 201 -1  N  TYR A 197   O  ILE A 209           
SHEET    1  AB 2 LEU A 262  LEU A 264  0                                        
SHEET    2  AB 2 LEU A 270  ILE A 272 -1  O  LYS A 271   N  LEU A 263           
SITE     1 AC1 18 ARG A 137  LEU A 139  GLY A 140  LYS A 141                    
SITE     2 AC1 18 ALA A 160  LEU A 210  GLU A 211  TYR A 212                    
SITE     3 AC1 18 ALA A 213  PRO A 214  GLY A 216  THR A 217                    
SITE     4 AC1 18 TYR A 219  ARG A 220  LEU A 263  SER A 342                    
SITE     5 AC1 18 ARG A 343  HIS A 366                                          
CRYST1   82.096   82.096  171.628  90.00  90.00 120.00 P 61 2 2     12          
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      0.012181  0.007033  0.000000        0.00000                         
SCALE2      0.000000  0.014065  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005827        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system