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Database: PDB
Entry: 5ORO
LinkDB: 5ORO
Original site: 5ORO 
HEADER    TRANSFERASE                             16-AUG-17   5ORO              
TITLE     CRYSTAL STRUCTURE OF AURORA-A KINASE IN COMPLEX WITH AN ALLOSTERICALLY
TITLE    2 BINDING FRAGMENT                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AURORA KINASE A;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AURORA 2,AURORA/IPL1-RELATED KINASE 1,HARK1,BREAST TUMOR-   
COMPND   5 AMPLIFIED KINASE,SERINE/THREONINE-PROTEIN KINASE 15,SERINE/THREONINE-
COMPND   6 PROTEIN KINASE 6,SERINE/THREONINE-PROTEIN KINASE AURORA-A;           
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 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: AURKA, AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KINASE, ALLOSTERIC INHIBITOR, FRAGMENT, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.MCINTYRE,P.M.COLLINS,F.VON DELFT,R.BAYLISS                        
REVDAT   3   16-OCT-19 5ORO    1       REMARK                                   
REVDAT   2   29-NOV-17 5ORO    1       JRNL                                     
REVDAT   1   01-NOV-17 5ORO    0                                                
JRNL        AUTH   P.J.MCINTYRE,P.M.COLLINS,L.VRZAL,K.BIRCHALL,L.H.ARNOLD,      
JRNL        AUTH 2 C.MPAMHANGA,P.J.COOMBS,S.G.BURGESS,M.W.RICHARDS,A.WINTER,    
JRNL        AUTH 3 V.VEVERKA,F.V.DELFT,A.MERRITT,R.BAYLISS                      
JRNL        TITL   CHARACTERIZATION OF THREE DRUGGABLE HOT-SPOTS IN THE         
JRNL        TITL 2 AURORA-A/TPX2 INTERACTION USING BIOCHEMICAL, BIOPHYSICAL,    
JRNL        TITL 3 AND FRAGMENT-BASED APPROACHES.                               
JRNL        REF    ACS CHEM. BIOL.               V.  12  2906 2017              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   29045126                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.7B00537                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 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) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.40                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 19847                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1015                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
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)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.640           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.64                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 172 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2358  22.0370 -11.8233              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4064 T22:   0.3652                                     
REMARK   3      T33:   0.4358 T12:  -0.0218                                     
REMARK   3      T13:  -0.0133 T23:  -0.1667                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6979 L22:   0.5410                                     
REMARK   3      L33:   0.3591 L12:  -0.0332                                     
REMARK   3      L13:   0.3954 L23:  -0.2991                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0596 S12:   0.2392 S13:  -0.4257                       
REMARK   3      S21:  -0.0523 S22:   0.0830 S23:  -0.1656                       
REMARK   3      S31:   0.1717 S32:   0.2175 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 173 THROUGH 187 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.2297  20.1510 -16.8237              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5767 T22:   0.5688                                     
REMARK   3      T33:   0.6192 T12:  -0.0618                                     
REMARK   3      T13:  -0.0097 T23:  -0.2692                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1473 L22:   0.0523                                     
REMARK   3      L33:   0.6370 L12:   0.2257                                     
REMARK   3      L13:  -0.5069 L23:  -0.0467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2317 S12:   0.2903 S13:  -1.0375                       
REMARK   3      S21:  -0.8330 S22:  -0.1574 S23:  -0.1776                       
REMARK   3      S31:  -0.2312 S32:  -0.6397 S33:  -0.0577                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 188 THROUGH 287 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -14.4402  33.0530 -10.9973              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4022 T22:   0.4201                                     
REMARK   3      T33:   0.3467 T12:  -0.0287                                     
REMARK   3      T13:  -0.0294 T23:  -0.0638                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3713 L22:   1.3643                                     
REMARK   3      L33:   0.2005 L12:  -0.3659                                     
REMARK   3      L13:  -0.4616 L23:   0.4052                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0567 S12:   0.2548 S13:  -0.0434                       
REMARK   3      S21:  -0.0827 S22:   0.1309 S23:  -0.0017                       
REMARK   3      S31:  -0.0459 S32:  -0.0140 S33:  -0.0004                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 289 THROUGH 324 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.7649  32.2661  -3.7511              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4100 T22:   0.4181                                     
REMARK   3      T33:   0.3909 T12:  -0.0756                                     
REMARK   3      T13:  -0.0378 T23:  -0.0757                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3823 L22:   0.3420                                     
REMARK   3      L33:   0.4118 L12:  -0.1781                                     
REMARK   3      L13:   0.2822 L23:  -0.0485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0491 S12:   0.2720 S13:   0.1022                       
REMARK   3      S21:   0.0649 S22:   0.0111 S23:   0.2204                       
REMARK   3      S31:   0.1675 S32:  -0.3231 S33:   0.0019                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 342 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -28.2485  30.6414   7.8354              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5827 T22:   0.4854                                     
REMARK   3      T33:   0.4940 T12:  -0.0297                                     
REMARK   3      T13:   0.1448 T23:  -0.0759                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1242 L22:   0.0491                                     
REMARK   3      L33:   0.1103 L12:  -0.0451                                     
REMARK   3      L13:   0.1128 L23:  -0.0659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5613 S12:  -0.4434 S13:  -0.0204                       
REMARK   3      S21:   0.4480 S22:   0.1982 S23:   0.1958                       
REMARK   3      S31:   0.3010 S32:  -0.4560 S33:  -0.0015                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 343 THROUGH 391 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.7639  45.3997  -4.6169              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3811 T22:   0.3598                                     
REMARK   3      T33:   0.5087 T12:   0.0219                                     
REMARK   3      T13:  -0.0492 T23:  -0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6767 L22:   0.9236                                     
REMARK   3      L33:   0.8778 L12:  -0.6564                                     
REMARK   3      L13:  -0.1536 L23:   0.4543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0128 S12:   0.0379 S13:   0.5042                       
REMARK   3      S21:   0.0504 S22:  -0.0258 S23:   0.4476                       
REMARK   3      S31:  -0.3702 S32:  -0.5432 S33:  -0.0009                       
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 5ORO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006255.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9282                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : DIALS                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20799                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.120                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 18.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.5: 0.5 M NACL: 0.2 M    
REMARK 280  MGCL2: 32.5 % V/V PEG 3350, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 298K                                                    
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       58.68267            
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      117.36533            
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       88.02400            
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      146.70667            
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       29.34133            
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       58.68267            
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      117.36533            
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      146.70667            
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       88.02400            
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       29.34133            
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 TOTAL BURIED SURFACE AREA: 1080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
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 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     LYS A 141    CG   CD   CE   NZ                                   
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
REMARK 470     LYS A 171    CG   CD   CE   NZ                                   
REMARK 470     ARG A 220    CG   CD   NE   CZ   NH1  NH2                        
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 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   O    ALA A   267     O    HOH A   501              1.83            
REMARK 500   O    HOH A   557     O    HOH A   563              1.94            
REMARK 500   NH1  ARG A   343     O    HOH A   502              1.98            
REMARK 500   O    ALA A   290     O    HOH A   503              1.98            
REMARK 500   OD1  ASN A   192     O    HOH A   504              2.08            
REMARK 500   NZ   LYS A   389     O    HOH A   505              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A 305   CB  -  CG  -  SD  ANGL. DEV. = -30.2 DEGREES          
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 202       32.74   -154.66                                   
REMARK 500    ALA A 203      -16.12     80.75                                   
REMARK 500    SER A 226      -58.77     71.47                                   
REMARK 500    ARG A 255       -3.23     74.24                                   
REMARK 500    ASP A 274       77.77     60.46                                   
REMARK 500    ARG A 304     -178.26    -66.28                                   
REMARK 500    LEU A 364       56.47    -93.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 261   OD1                                                    
REMARK 620 2 ASP A 274   OD2  87.1                                              
REMARK 620 3 ADP A 401   O3B 173.6  96.6                                        
REMARK 620 4 ADP A 401   O2A  90.6  93.2  84.0                                  
REMARK 620 5 HOH A 522   O    85.2 171.0  90.7  82.3                            
REMARK 620 6 HOH A 540   O    93.7  95.4  91.1 170.6  89.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 274   OD1                                                    
REMARK 620 2 ADP A 401   O1B  74.0                                              
REMARK 620 3 HOH A 508   O    88.9  88.3                                        
REMARK 620 4 HOH A 561   O   150.8 107.6  62.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue A5H A 404                 
DBREF  5ORO A  127   391  UNP    O14965   AURKA_HUMAN    127    391             
SEQADV 5ORO ALA A  290  UNP  O14965    CYS   290 CONFLICT                       
SEQRES   1 A  265  GLN TRP ALA LEU GLU ASP PHE GLU ILE GLY ARG PRO LEU          
SEQRES   2 A  265  GLY LYS GLY LYS PHE GLY ASN VAL TYR LEU ALA ARG GLU          
SEQRES   3 A  265  LYS GLN SER LYS PHE ILE LEU ALA LEU LYS VAL LEU PHE          
SEQRES   4 A  265  LYS ALA GLN LEU GLU LYS ALA GLY VAL GLU HIS GLN LEU          
SEQRES   5 A  265  ARG ARG GLU VAL GLU ILE GLN SER HIS LEU ARG HIS PRO          
SEQRES   6 A  265  ASN ILE LEU ARG LEU TYR GLY TYR PHE HIS ASP ALA THR          
SEQRES   7 A  265  ARG VAL TYR LEU ILE LEU GLU TYR ALA PRO LEU GLY THR          
SEQRES   8 A  265  VAL TYR ARG GLU LEU GLN LYS LEU SER LYS PHE ASP GLU          
SEQRES   9 A  265  GLN ARG THR ALA THR TYR ILE THR GLU LEU ALA ASN ALA          
SEQRES  10 A  265  LEU SER TYR CYS HIS SER LYS ARG VAL ILE HIS ARG ASP          
SEQRES  11 A  265  ILE LYS PRO GLU ASN LEU LEU LEU GLY SER ALA GLY GLU          
SEQRES  12 A  265  LEU LYS ILE ALA ASP PHE GLY TRP SER VAL HIS ALA PRO          
SEQRES  13 A  265  SER SER ARG ARG THR TPO LEU ALA GLY THR LEU ASP TYR          
SEQRES  14 A  265  LEU PRO PRO GLU MET ILE GLU GLY ARG MET HIS ASP GLU          
SEQRES  15 A  265  LYS VAL ASP LEU TRP SER LEU GLY VAL LEU CYS TYR GLU          
SEQRES  16 A  265  PHE LEU VAL GLY LYS PRO PRO PHE GLU ALA ASN THR TYR          
SEQRES  17 A  265  GLN GLU THR TYR LYS ARG ILE SER ARG VAL GLU PHE THR          
SEQRES  18 A  265  PHE PRO ASP PHE VAL THR GLU GLY ALA ARG ASP LEU ILE          
SEQRES  19 A  265  SER ARG LEU LEU LYS HIS ASN PRO SER GLN ARG PRO MET          
SEQRES  20 A  265  LEU ARG GLU VAL LEU GLU HIS PRO TRP ILE THR ALA ASN          
SEQRES  21 A  265  SER SER LYS PRO SER                                          
MODRES 5ORO TPO A  288  THR  MODIFIED RESIDUE                                   
HET    TPO  A 288      11                                                       
HET    ADP  A 401      27                                                       
HET     MG  A 402       1                                                       
HET     MG  A 403       1                                                       
HET    A5H  A 404      15                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     A5H 3-(4-CHLOROPHENYL)-5,6-DIHYDROIMIDAZO[2,1-B][1,                  
HETNAM   2 A5H  3]THIAZOLE                                                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   2  ADP    C10 H15 N5 O10 P2                                            
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  A5H    C11 H9 CL N2 S                                               
FORMUL   6  HOH   *63(H2 O)                                                     
HELIX    1 AA1 ALA A  129  GLU A  131  5                                   3    
HELIX    2 AA2 LYS A  166  ALA A  172  1                                   7    
HELIX    3 AA3 VAL A  174  LEU A  188  1                                  15    
HELIX    4 AA4 THR A  217  SER A  226  1                                  10    
HELIX    5 AA5 ASP A  229  SER A  249  1                                  21    
HELIX    6 AA6 LYS A  258  GLU A  260  5                                   3    
HELIX    7 AA7 PRO A  297  GLU A  302  1                                   6    
HELIX    8 AA8 GLU A  308  GLY A  325  1                                  18    
HELIX    9 AA9 THR A  333  VAL A  344  1                                  12    
HELIX   10 AB1 THR A  353  LEU A  364  1                                  12    
HELIX   11 AB2 ASN A  367  ARG A  371  5                                   5    
HELIX   12 AB3 MET A  373  GLU A  379  1                                   7    
HELIX   13 AB4 HIS A  380  SER A  387  1                                   8    
SHEET    1 AA1 5 PHE A 133  LYS A 141  0                                        
SHEET    2 AA1 5 ASN A 146  GLU A 152 -1  O  LEU A 149   N  GLY A 136           
SHEET    3 AA1 5 ILE A 158  PHE A 165 -1  O  LEU A 161   N  TYR A 148           
SHEET    4 AA1 5 ARG A 205  LEU A 210 -1  O  LEU A 210   N  ALA A 160           
SHEET    5 AA1 5 LEU A 196  HIS A 201 -1  N  PHE A 200   O  TYR A 207           
SHEET    1 AA2 2 VAL A 252  ILE A 253  0                                        
SHEET    2 AA2 2 VAL A 279  HIS A 280 -1  O  VAL A 279   N  ILE A 253           
SHEET    1 AA3 2 LEU A 262  LEU A 264  0                                        
SHEET    2 AA3 2 LEU A 270  ILE A 272 -1  O  LYS A 271   N  LEU A 263           
LINK         OD1 ASN A 261                MG    MG A 402     1555   1555  2.31  
LINK         OD1 ASP A 274                MG    MG A 403     1555   1555  2.67  
LINK         OD2 ASP A 274                MG    MG A 402     1555   1555  2.15  
LINK         C   THR A 287                 N   TPO A 288     1555   1555  1.33  
LINK         C   TPO A 288                 N   LEU A 289     1555   1555  1.33  
LINK         O1B ADP A 401                MG    MG A 403     1555   1555  2.36  
LINK         O3B ADP A 401                MG    MG A 402     1555   1555  1.99  
LINK         O2A ADP A 401                MG    MG A 402     1555   1555  2.14  
LINK        MG    MG A 402                 O   HOH A 522     1555   1555  1.91  
LINK        MG    MG A 402                 O   HOH A 540     1555   1555  2.01  
LINK        MG    MG A 403                 O   HOH A 508     1555   1555  2.51  
LINK        MG    MG A 403                 O   HOH A 561     1555   1555  2.10  
CISPEP   1 ALA A  281    PRO A  282          0        -0.76                     
SITE     1 AC1 23 LEU A 139  GLY A 140  GLY A 142  LYS A 143                    
SITE     2 AC1 23 GLY A 145  VAL A 147  ALA A 160  LYS A 162                    
SITE     3 AC1 23 LEU A 194  GLU A 211  ALA A 213  THR A 217                    
SITE     4 AC1 23 GLU A 260  ASN A 261  LEU A 263  ASP A 274                    
SITE     5 AC1 23  MG A 402   MG A 403  HOH A 522  HOH A 533                    
SITE     6 AC1 23 HOH A 540  HOH A 552  HOH A 555                               
SITE     1 AC2  5 ASN A 261  ASP A 274  ADP A 401  HOH A 522                    
SITE     2 AC2  5 HOH A 540                                                     
SITE     1 AC3  4 ASP A 274  ADP A 401  HOH A 508  HOH A 561                    
SITE     1 AC4  6 TRP A 128  PHE A 133  GLU A 152  PHE A 157                    
SITE     2 AC4  6 TYR A 197  TYR A 334                                          
CRYST1   82.313   82.313  176.048  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      0.012149  0.007014  0.000000        0.00000                         
SCALE2      0.000000  0.014028  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005680        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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