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Database: PDB
Entry: 4UYN
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HEADER    TRANSFERASE                             02-SEP-14   4UYN              
TITLE     SAR156497 AN EXQUISITELY SELECTIVE INHIBITOR OF AURORA KINASES        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AURORA KINASE A;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 125-399;                           
COMPND   5 SYNONYM: AURORA 2, AURORA/IPL1-RELATED KINASE 1, ARK-1,              
COMPND   6  AURORA-RELATED KINASE 1, HARK1, BREAST TUMOR-AMPLIFIED KINASE,      
COMPND   7  SERINE/THREONINE-PROTEIN KINASE 15, SERINE/THREONINE-PROTEIN        
COMPND   8  KINASE 6, SERINE/THREONINE-PROTEIN KINASE AURORA-A;                 
COMPND   9 EC: 2.7.11.1;                                                        
COMPND  10 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: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.CARRY,F.CLERC,H.MINOUX,L.SCHIO,J.MAUGER,A.NAIR,E.PARMANTIER,      
AUTHOR   2 R.LEMOIGNE,C.DELORME,J.P.NICOLAS,A.KRICK,P.Y.ABECASSIS,              
AUTHOR   3 V.CROCQ-STUERGA,S.POUZIEUX,L.DELARBRE,S.MAIGNAN,T.BERTRAND,          
AUTHOR   4 K.BJERGARDE,N.MA,S.LACHAUD,H.GUIZANI,R.LEBEL,G.DOERFLINGER,S.MONGET, 
AUTHOR   5 S.PERRON,F.GASSE,O.ANGOUILLANT-BONIFACE,B.FILOCHE-ROMME,M.MURER,     
AUTHOR   6 S.GONTIER,C.PREVOST,M.L.MONTEIRO,C.COMBEAU                           
REVDAT   2   21-JAN-15 4UYN    1       JRNL                                     
REVDAT   1   19-NOV-14 4UYN    0                                                
JRNL        AUTH   J.CARRY,F.CLERC,H.MINOUX,L.SCHIO,J.MAUGER,A.NAIR,            
JRNL        AUTH 2 E.PARMANTIER,R.LE MOIGNE,C.DELORME,J.NICOLAS,A.KRICK,        
JRNL        AUTH 3 P.ABECASSIS,V.CROCQ-STUERGA,S.POUZIEUX,L.DELARBRE,S.MAIGNAN, 
JRNL        AUTH 4 T.BERTRAND,K.BJERGARDE,N.MA,S.LACHAUD,H.GUIZANI,R.LEBEL,     
JRNL        AUTH 5 G.DOERFLINGER,S.MONGET,S.PERRON,F.GASSE,                     
JRNL        AUTH 6 O.ANGOUILLANT-BONIFACE,B.FILOCHE-ROMME,M.MURER,S.GONTIER,    
JRNL        AUTH 7 C.PREVOST,M.MONTEIRO,C.COMBEAU                               
JRNL        TITL   SAR156497, AN EXQUISITELY SELECTIVE INHIBITOR OF AURORA      
JRNL        TITL 2 KINASES.                                                     
JRNL        REF    J.MED.CHEM.                   V.  58   362 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25369539                                                     
JRNL        DOI    10.1021/JM501326K                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT 2.9.3                                     
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.9                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2                              
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 20466                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : NULL                           
REMARK   3   R VALUE            (WORKING SET)  : 0.201                          
REMARK   3   FREE R VALUE                      : 0.234                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 7.8                            
REMARK   3   FREE R VALUE TEST SET COUNT       : 1607                           
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               : 10                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.9                      
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.0                      
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.19                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2895                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2031                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2657                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2                      
REMARK   3   BIN FREE R VALUE                        : 0.2372                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 8.22                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 238                      
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            : 2059                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.5569                                               
REMARK   3    B22 (A**2) : -0.5728                                              
REMARK   3    B33 (A**2) : 0.0159                                               
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.2632                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.9359                        
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.9146                        
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2147   ; 2.0    ; 0.030               
REMARK   3    BOND ANGLES               : 2900   ; 2.0    ; 2.65                
REMARK   3    TORSION ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : NULL   ; NULL   ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : NULL   ; NULL   ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : NULL                     
REMARK   3    BOND ANGLES                  (DEGREES) : NULL                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NONE                                      
REMARK   4                                                                      
REMARK   4 4UYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-SEP-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-61661.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97630                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (Q315R)                        
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20475                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.5                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.14                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.2                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350 21% TRIS 50MM PH 8               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       22.95650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 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   124                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     TRP A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     VAL A   279                                                      
REMARK 465     HIS A   280                                                      
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     ASP A   288                                                      
REMARK 465     LEU A   289                                                      
REMARK 465     CYS A   290                                                      
REMARK 465     GLY A   291                                                      
REMARK 465     THR A   292                                                      
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     ALA A   400                                                      
REMARK 465     ALA A   401                                                      
REMARK 465     ALA A   402                                                      
REMARK 465     LEU A   403                                                      
REMARK 465     GLU A   404                                                      
REMARK 465     HIS A   405                                                      
REMARK 465     HIS A   406                                                      
REMARK 465     HIS A   407                                                      
REMARK 465     HIS A   408                                                      
REMARK 465     HIS A   409                                                      
REMARK 465     HIS A   410                                                      
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   OE1  GLU A   302     NH1  ARG A   304              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CZ   PHE A   157     OH   TYR A   334     1545     2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A 157   C     ILE A 158   N      -0.290                       
REMARK 500    ILE A 158   C     LEU A 159   N       0.141                       
REMARK 500    GLY A 303   C     ARG A 304   N       0.292                       
REMARK 500    ARG A 304   C     MET A 305   N      -0.470                       
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    LYS A 156   CA  -  C   -  N   ANGL. DEV. = -15.5 DEGREES          
REMARK 500    LYS A 156   O   -  C   -  N   ANGL. DEV. =  14.4 DEGREES          
REMARK 500    PHE A 157   C   -  N   -  CA  ANGL. DEV. = -19.1 DEGREES          
REMARK 500    LEU A 178   N   -  CA  -  C   ANGL. DEV. =  18.0 DEGREES          
REMARK 500    GLY A 303   CA  -  C   -  N   ANGL. DEV. =  15.6 DEGREES          
REMARK 500    GLY A 303   O   -  C   -  N   ANGL. DEV. = -16.6 DEGREES          
REMARK 500    ARG A 304   C   -  N   -  CA  ANGL. DEV. =  16.4 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 156       27.07     80.41                                   
REMARK 500    ALA A 167      -94.04    -47.31                                   
REMARK 500    LEU A 169      -19.26    173.46                                   
REMARK 500    GLU A 175     -177.58    -65.90                                   
REMARK 500    GLN A 177       92.84    160.87                                   
REMARK 500    LEU A 178      -44.62     19.36                                   
REMARK 500    ASP A 202     -142.89   -122.83                                   
REMARK 500    THR A 204       -4.20   -142.32                                   
REMARK 500    SER A 226      -38.51     80.14                                   
REMARK 500    ASP A 274     -124.06    -11.88                                   
REMARK 500    PHE A 275       86.61    104.64                                   
REMARK 500    ASP A 307     -156.79   -138.07                                   
REMARK 500    LEU A 364       42.71    -95.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PHE A 157        -16.24                                           
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    LYS A 125       -32.7      L          D   WRONG HAND              
REMARK 500    LYS A 153        23.2      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 168        22.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 174       -30.2      L          D   WRONG HAND              
REMARK 500    LEU A 178        21.5      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 183       -29.3      L          D   WRONG HAND              
REMARK 500    ASP A 274       -32.7      L          D   WRONG HAND              
REMARK 500    PHE A 275       -32.7      L          D   WRONG HAND              
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 Y3M A1392                 
DBREF  4UYN A  125   399  UNP    O14965   AURKA_HUMAN    125    399             
SEQADV 4UYN MET A  124  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN ALA A  400  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN ALA A  401  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN ALA A  402  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN LEU A  403  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN GLU A  404  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN HIS A  405  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN HIS A  406  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN HIS A  407  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN HIS A  408  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN HIS A  409  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN HIS A  410  UNP  O14965              EXPRESSION TAG                 
SEQADV 4UYN ASP A  288  UNP  O14965    THR   288 CONFLICT                       
SEQRES   1 A  287  MET LYS ARG GLN TRP ALA LEU GLU ASP PHE GLU ILE GLY          
SEQRES   2 A  287  ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN VAL TYR LEU          
SEQRES   3 A  287  ALA ARG GLU LYS GLN SER LYS PHE ILE LEU ALA LEU LYS          
SEQRES   4 A  287  VAL LEU PHE LYS ALA GLN LEU GLU LYS ALA GLY VAL GLU          
SEQRES   5 A  287  HIS GLN LEU ARG ARG GLU VAL GLU ILE GLN SER HIS LEU          
SEQRES   6 A  287  ARG HIS PRO ASN ILE LEU ARG LEU TYR GLY TYR PHE HIS          
SEQRES   7 A  287  ASP ALA THR ARG VAL TYR LEU ILE LEU GLU TYR ALA PRO          
SEQRES   8 A  287  LEU GLY THR VAL TYR ARG GLU LEU GLN LYS LEU SER LYS          
SEQRES   9 A  287  PHE ASP GLU GLN ARG THR ALA THR TYR ILE THR GLU LEU          
SEQRES  10 A  287  ALA ASN ALA LEU SER TYR CYS HIS SER LYS ARG VAL ILE          
SEQRES  11 A  287  HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU LEU GLY SER          
SEQRES  12 A  287  ALA GLY GLU LEU LYS ILE ALA ASP PHE GLY TRP SER VAL          
SEQRES  13 A  287  HIS ALA PRO SER SER ARG ARG THR ASP LEU CYS GLY THR          
SEQRES  14 A  287  LEU ASP TYR LEU PRO PRO GLU MET ILE GLU GLY ARG MET          
SEQRES  15 A  287  HIS ASP GLU LYS VAL ASP LEU TRP SER LEU GLY VAL LEU          
SEQRES  16 A  287  CYS TYR GLU PHE LEU VAL GLY LYS PRO PRO PHE GLU ALA          
SEQRES  17 A  287  ASN THR TYR GLN GLU THR TYR LYS ARG ILE SER ARG VAL          
SEQRES  18 A  287  GLU PHE THR PHE PRO ASP PHE VAL THR GLU GLY ALA ARG          
SEQRES  19 A  287  ASP LEU ILE SER ARG LEU LEU LYS HIS ASN PRO SER GLN          
SEQRES  20 A  287  ARG PRO MET LEU ARG GLU VAL LEU GLU HIS PRO TRP ILE          
SEQRES  21 A  287  THR ALA ASN SER SER LYS PRO SER ASN CYS GLN ASN LYS          
SEQRES  22 A  287  GLU SER ALA ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS          
SEQRES  23 A  287  HIS                                                          
HET    Y3M  A1392      34                                                       
HETNAM     Y3M ETHYL (9S)-9-[5-(1H-BENZIMIDAZOL-2-                              
HETNAM   2 Y3M  YLSULFANYL)FURAN-2-YL]-8-HYDROXY-5,6,7,9-TETRAHYDRO-2H-         
HETNAM   3 Y3M  PYRROLO[3,4-B]QUINOLINE-3-CARBOXYLATE                           
FORMUL   2  Y3M    C25 H22 N4 O4 S                                              
FORMUL   3  HOH   *89(H2 O)                                                     
HELIX    1   1 ALA A  129  GLU A  131  5                                   3    
HELIX    2   2 LEU A  178  LEU A  188  1                                  11    
HELIX    3   3 THR A  217  SER A  226  1                                  10    
HELIX    4   4 ASP A  229  LYS A  250  1                                  22    
HELIX    5   5 LYS A  258  GLU A  260  5                                   3    
HELIX    6   6 PRO A  297  GLU A  302  1                                   6    
HELIX    7   7 LYS A  309  GLY A  325  1                                  17    
HELIX    8   8 THR A  333  ARG A  343  1                                  11    
HELIX    9   9 THR A  353  LEU A  364  1                                  12    
HELIX   10  10 ASN A  367  ARG A  371  5                                   5    
HELIX   11  11 MET A  373  GLU A  379  1                                   7    
HELIX   12  12 HIS A  380  SER A  387  1                                   8    
SHEET    1  AA 5 PHE A 133  GLY A 142  0                                        
SHEET    2  AA 5 GLY A 145  GLU A 152 -1  O  GLY A 145   N  GLY A 142           
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           
LINK         CD1 PHE A 157                 CE2 TYR A 334     1555   1545  1.63  
LINK         CD1 PHE A 157                 CZ  TYR A 334     1555   1545  1.56  
LINK         CD1 PHE A 157                 OH  TYR A 334     1555   1545  1.60  
LINK         CE1 PHE A 157                 CE2 TYR A 334     1555   1545  1.71  
LINK         CE1 PHE A 157                 CZ  TYR A 334     1555   1545  1.69  
LINK         CE1 PHE A 157                 OH  TYR A 334     1555   1545  1.44  
LINK         CD1 PHE A 157                 CE2 TYR A 334     1565   1555  1.63  
LINK         CE1 PHE A 157                 CE2 TYR A 334     1565   1555  1.71  
LINK         CD1 PHE A 157                 CZ  TYR A 334     1565   1555  1.56  
LINK         CE1 PHE A 157                 CZ  TYR A 334     1565   1555  1.69  
LINK         CD1 PHE A 157                 OH  TYR A 334     1565   1555  1.60  
LINK         CE1 PHE A 157                 OH  TYR A 334     1565   1555  1.44  
CISPEP   1 GLN A  177    LEU A  178          0       -18.29                     
SITE     1 AC1 14 VAL A 147  ALA A 160  LYS A 162  LEU A 164                    
SITE     2 AC1 14 GLN A 185  LEU A 208  LEU A 210  GLU A 211                    
SITE     3 AC1 14 TYR A 212  ALA A 213  GLY A 216  LEU A 263                    
SITE     4 AC1 14 ALA A 273  PHE A 275                                          
CRYST1   48.355   45.913   59.595  90.00  97.82  90.00 P 1 21 1      1          
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      0.020680  0.000000  0.002840        0.00000                         
SCALE2      0.000000  0.021780  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016937        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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