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Database: PDB
Entry: 1OL6
LinkDB: 1OL6
Original site: 1OL6 
HEADER    TRANSFERASE                             06-AUG-03   1OL6              
TITLE     STRUCTURE OF UNPHOSPHORYLATED D274N MUTANT OF AURORA-A                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE KINASE 6;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 122-403;                        
COMPND   5 SYNONYM: SERINE/THREONINE KINASE 15, AURORA/IPL1-RELATED             
COMPND   6  KINASE 1, AURORA-RELATED KINASE 1, HARK1, AURORA-A,                 
COMPND   7  BREAST-TUMOR-AMPLIFIED KINASE;                                      
COMPND   8 EC: 2.7.1.37;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: 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;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: CODONPLUS RIL;                             
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PETM11                                     
KEYWDS    TRANSFERASE, CELL CYCLE, SERINE/THREONINE-PROTEIN                     
KEYWDS   2 KINASE, ATP-BINDING, PHOSPHORYLATION                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.BAYLISS,E.CONTI                                                     
REVDAT   4   10-SEP-14 1OL6    1       SEQADV                                   
REVDAT   3   30-JAN-13 1OL6    1       HEADER KEYWDS JRNL   REMARK              
REVDAT   3 2                           VERSN  FORMUL                            
REVDAT   2   24-FEB-09 1OL6    1       VERSN                                    
REVDAT   1   30-OCT-03 1OL6    0                                                
JRNL        AUTH   R.BAYLISS,T.SARDON,I.VERNOS,E.CONTI                          
JRNL        TITL   STRUCTURAL BASIS OF AURORA-A ACTIVATION BY TPX2 AT THE       
JRNL        TITL 2 MITOTIC SPINDLE.                                             
JRNL        REF    MOL.CELL                      V.  12   851 2003              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   14580337                                                     
JRNL        DOI    10.1016/S1097-2765(03)00392-7                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3    ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3                              
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 12265                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.277                           
REMARK   3   FREE R VALUE                     : 0.301                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1845                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 3                                       
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) : 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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.0146                          
REMARK   3   BOND ANGLES            (DEGREES) : 1.936                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OL6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  06-AUG-03.                 
REMARK 100 THE PDBE ID CODE IS EBI-13228.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.30                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91839                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12265                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.16500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1FOT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): NULL                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 190 MM NACL,                
REMARK 280  10 MM NAH2PO4, 100 MM TRIS PH 7.3                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.66500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.65500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.65500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       19.33250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.65500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.65500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       57.99750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.65500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.65500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       19.33250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.65500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.65500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       57.99750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       38.66500            
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: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  ENGINEERED MUTATION ASP 274 ASN CHAIN A                             
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     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     GLN A   127                                                      
REMARK 465     GLY A   142                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     VAL A   174                                                      
REMARK 465     ALA A   281                                                      
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     ARG A   304                                                      
REMARK 465     LYS A   389                                                      
REMARK 465     PRO A   390                                                      
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     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     ARG A 151    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 153    CG   CD   CE   NZ                                   
REMARK 470     GLN A 154    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 156    CG   CD   CE   NZ                                   
REMARK 470     PHE A 165    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 168    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 170    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 171    CG   CD   CE   NZ                                   
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     HIS A 201    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 202    CG   OD1  OD2                                       
REMARK 470     THR A 204    OG1  CG2                                            
REMARK 470     TYR A 207    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 220    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 227    CG   CD   CE   NZ                                   
REMARK 470     GLN A 231    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 251    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 293    CG   CD1  CD2                                       
REMARK 470     GLU A 302    CG   CD   OE1  OE2                                  
REMARK 470     MET A 305    CG   SD   CE                                        
REMARK 470     ASP A 307    CG   OD1  OD2                                       
REMARK 470     LYS A 326    CG   CD   CE   NZ                                   
REMARK 470     ASN A 332    CG   OD1  ND2                                       
REMARK 470     TYR A 334    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A 335    CG   CD   OE1  NE2                                  
REMARK 470     THR A 337    OG1  CG2                                            
REMARK 470     TYR A 338    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 339    CG   CD   CE   NZ                                   
REMARK 470     ARG A 340    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 343    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 354    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 375    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 388    CA   C    O    CB   OG                              
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    ASP A 307   N   -  CA  -  C   ANGL. DEV. =  19.9 DEGREES          
REMARK 500    PRO A 368   C   -  N   -  CA  ANGL. DEV. =   9.8 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    LYS A 153       -5.04    -52.43                                   
REMARK 500    LYS A 171      -36.77    -33.36                                   
REMARK 500    GLU A 181      -79.97    -57.07                                   
REMARK 500    VAL A 182      -55.62    -28.48                                   
REMARK 500    ARG A 189       85.17   -154.80                                   
REMARK 500    SER A 226      -35.65     68.71                                   
REMARK 500    ASP A 256       51.98   -144.94                                   
REMARK 500    ASN A 274       77.03     52.45                                   
REMARK 500    GLU A 308      -23.83   -156.62                                   
REMARK 500    PRO A 349     -152.64    -53.92                                   
REMARK 500    LEU A 364       52.21    -92.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP A 307        20.6      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 308        24.0      L          L   OUTSIDE RANGE           
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 ATP A1388                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MUO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AURORA-2, AN ONCOGENIC                         
REMARK 900   SERINE-THREONINE KINASE                                            
REMARK 900 RELATED ID: 1OL5   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF AURORA-A 122-403,                                      
REMARK 900  PHOSPHORYLATED ON THR287, THR288 AND BOUND                          
REMARK 900  TO TPX2 1-43                                                        
REMARK 900 RELATED ID: 1OL7   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN AURORA-A 122-403 PHOSPHORYLATED                  
REMARK 900  ON THR287, THR288                                                   
DBREF  1OL6 A  122   403  UNP    O14965   STK6_HUMAN     122    403             
SEQADV 1OL6 ASN A  274  UNP  O14965    ASP   274 ENGINEERED MUTATION            
SEQRES   1 A  282  GLU SER LYS LYS ARG GLN TRP ALA LEU GLU ASP PHE GLU          
SEQRES   2 A  282  ILE GLY ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN VAL          
SEQRES   3 A  282  TYR LEU ALA ARG GLU LYS GLN SER LYS PHE ILE LEU ALA          
SEQRES   4 A  282  LEU LYS VAL LEU PHE LYS ALA GLN LEU GLU LYS ALA GLY          
SEQRES   5 A  282  VAL GLU HIS GLN LEU ARG ARG GLU VAL GLU ILE GLN SER          
SEQRES   6 A  282  HIS LEU ARG HIS PRO ASN ILE LEU ARG LEU TYR GLY TYR          
SEQRES   7 A  282  PHE HIS ASP ALA THR ARG VAL TYR LEU ILE LEU GLU TYR          
SEQRES   8 A  282  ALA PRO LEU GLY THR VAL TYR ARG GLU LEU GLN LYS LEU          
SEQRES   9 A  282  SER LYS PHE ASP GLU GLN ARG THR ALA THR TYR ILE THR          
SEQRES  10 A  282  GLU LEU ALA ASN ALA LEU SER TYR CYS HIS SER LYS ARG          
SEQRES  11 A  282  VAL ILE HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU LEU          
SEQRES  12 A  282  GLY SER ALA GLY GLU LEU LYS ILE ALA ASN PHE GLY TRP          
SEQRES  13 A  282  SER VAL HIS ALA PRO SER SER ARG ARG THR THR LEU CYS          
SEQRES  14 A  282  GLY THR LEU ASP TYR LEU PRO PRO GLU MET ILE GLU GLY          
SEQRES  15 A  282  ARG MET HIS ASP GLU LYS VAL ASP LEU TRP SER LEU GLY          
SEQRES  16 A  282  VAL LEU CYS TYR GLU PHE LEU VAL GLY LYS PRO PRO PHE          
SEQRES  17 A  282  GLU ALA ASN THR TYR GLN GLU THR TYR LYS ARG ILE SER          
SEQRES  18 A  282  ARG VAL GLU PHE THR PHE PRO ASP PHE VAL THR GLU GLY          
SEQRES  19 A  282  ALA ARG ASP LEU ILE SER ARG LEU LEU LYS HIS ASN PRO          
SEQRES  20 A  282  SER GLN ARG PRO MET LEU ARG GLU VAL LEU GLU HIS PRO          
SEQRES  21 A  282  TRP ILE THR ALA ASN SER SER LYS PRO SER ASN CYS GLN          
SEQRES  22 A  282  ASN LYS GLU SER ALA SER LYS GLN SER                          
HET    ATP  A1388      31                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   2  ATP    C10 H16 N5 O13 P3                                            
FORMUL   3  HOH   *3(H2 O)                                                      
HELIX    1   1 ALA A  129  PHE A  133  5                                   5    
HELIX    2   2 LYS A  166  ALA A  172  1                                   7    
HELIX    3   3 HIS A  176  LEU A  188  1                                  13    
HELIX    4   4 THR A  217  SER A  226  1                                  10    
HELIX    5   5 ASP A  229  SER A  249  1                                  21    
HELIX    6   6 LYS A  258  GLU A  260  5                                   3    
HELIX    7   7 THR A  292  LEU A  296  5                                   5    
HELIX    8   8 PRO A  297  GLU A  302  1                                   6    
HELIX    9   9 LYS A  309  GLY A  325  1                                  17    
HELIX   10  10 THR A  333  ARG A  343  1                                  11    
HELIX   11  11 THR A  353  LEU A  364  1                                  12    
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 GLU A 134  GLY A 140  0                                        
SHEET    2  AA 5 ASN A 146  ARG A 151 -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 13 LEU A 139  GLY A 140  LYS A 141  LYS A 143                    
SITE     2 AC1 13 GLY A 145  VAL A 147  LYS A 162  LEU A 194                    
SITE     3 AC1 13 GLU A 211  ALA A 213  THR A 217  LEU A 263                    
SITE     4 AC1 13 ASN A 274                                                     
CRYST1   87.310   87.310   77.330  90.00  90.00  90.00 P 41 21 2     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      0.011453  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011453  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012931        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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