GenomeNet

Database: PDB
Entry: 6GR9
LinkDB: 6GR9
Original site: 6GR9 
HEADER    TRANSFERASE                             10-JUN-18   6GR9              
TITLE     HUMAN AURKC INCENP COMPLEX BOUND TO VX-680                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AURORA KINASE C;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AURORA 3,AURORA/IPL1-RELATED KINASE 3,AURORA-RELATED KINASE 
COMPND   5 3,AURORA/IPL1/EG2 PROTEIN 2,SERINE/THREONINE-PROTEIN KINASE 13,      
COMPND   6 SERINE/THREONINE-PROTEIN KINASE AURORA-C;                            
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: INNER CENTROMERE PROTEIN;                                  
COMPND  11 CHAIN: B;                                                            
COMPND  12 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: AURKC, AIE2, AIK3, AIRK3, ARK3, STK13;                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3);                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHTVAMP1-SGC;                             
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: INCENP;                                                        
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3);                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PHTVAMP1-SGC                              
KEYWDS    KINASE, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.ABDUL AZEEZ,F.J.SORRELL,F.VON DELFT,C.BOUNTRA,S.KNAPP,            
AUTHOR   2 A.M.EDWARDS,C.ARROWSMITH,J.M.ELKINS                                  
REVDAT   1   15-MAY-19 6GR9    0                                                
JRNL        AUTH   K.R.ABDUL AZEEZ,J.M.ELKINS                                   
JRNL        TITL   AURKC INCENP COMPLEX BOUND TO BRD-7880                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0222                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22049                          
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1177                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1591                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.3780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2605                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 162                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.38000                                             
REMARK   3    B22 (A**2) : -0.38000                                             
REMARK   3    B33 (A**2) : 1.23000                                              
REMARK   3    B12 (A**2) : -0.19000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.212         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.184         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.178         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2723 ; 0.008 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A):  2472 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3708 ; 1.329 ; 1.674       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5790 ; 0.824 ; 1.628       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   318 ; 6.465 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   145 ;33.256 ;20.621       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   460 ;16.685 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;23.903 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   340 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2978 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   497 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1269 ; 2.969 ; 4.361       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1268 ; 2.970 ; 4.357       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1582 ; 4.499 ; 6.511       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1583 ; 4.498 ; 6.515       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1454 ; 3.548 ; 4.776       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1451 ; 3.533 ; 4.761       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2116 ; 5.648 ; 7.003       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3030 ; 7.643 ;50.004       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2999 ; 7.557 ;49.856       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6GR9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010438.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 R CDTE 300K       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23264                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6GR8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG3350, 10 % ETHYLENE GLYCOL,      
REMARK 280  0.1 M BIS-TRIS-PROPANE PH 7.5, 0.2 M SODIUM SULFATE, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
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   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       40.33333            
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       80.66667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       80.66667            
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       40.33333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ASN A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     MET B   834                                                      
REMARK 465     GLU B   835                                                      
REMARK 465     ALA B   836                                                      
REMARK 465     HIS B   837                                                      
REMARK 465     PRO B   838                                                      
REMARK 465     ARG B   839                                                      
REMARK 465     LYS B   840                                                      
REMARK 465     LYS B   883                                                      
REMARK 465     SER B   884                                                      
REMARK 465     LYS B   885                                                      
REMARK 465     PRO B   886                                                      
REMARK 465     ARG B   887                                                      
REMARK 465     TYR B   888                                                      
REMARK 465     HIS B   889                                                      
REMARK 465     LYS B   890                                                      
REMARK 465     ARG B   891                                                      
REMARK 465     ASN B   898                                                      
REMARK 465     SER B   899                                                      
REMARK 465     PRO B   900                                                      
REMARK 465     PRO B   901                                                      
REMARK 465     LEU B   902                                                      
REMARK 465     GLN B   903                                                      
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     ARG A  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  53    CE   NZ                                             
REMARK 470     ARG A 257    CZ   NH1  NH2                                       
REMARK 470     LYS A 289    CE   NZ                                             
REMARK 470     GLU B 878    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 882    CG   CD   CE   NZ                                   
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 136       -8.61     63.11                                   
REMARK 500    LYS A 161       31.52     70.85                                   
REMARK 500    ASP A 166       46.82   -155.53                                   
REMARK 500    ASP A 217     -158.61   -128.63                                   
REMARK 500    PRO A 303      172.20    -56.93                                   
REMARK 500    CYS A 304     -155.10   -153.47                                   
REMARK 500    PRO B 843      151.57    -42.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 114         0.12    SIDE CHAIN                              
REMARK 500    ARG A 196         0.08    SIDE CHAIN                              
REMARK 500    ARG A 272         0.09    SIDE CHAIN                              
REMARK 500    ARG A 281         0.11    SIDE CHAIN                              
REMARK 500    ARG B 847         0.12    SIDE CHAIN                              
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 VX6 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
DBREF  6GR9 A   36   305  UNP    Q9UQB9   AURKC_HUMAN      2    271             
DBREF  6GR9 B  835   903  UNP    Q9NQS7   INCE_HUMAN     835    903             
SEQADV 6GR9 GLY A   32  UNP  Q9UQB9              EXPRESSION TAG                 
SEQADV 6GR9 ALA A   33  UNP  Q9UQB9              EXPRESSION TAG                 
SEQADV 6GR9 ASN A   34  UNP  Q9UQB9              EXPRESSION TAG                 
SEQADV 6GR9 SER A   35  UNP  Q9UQB9              EXPRESSION TAG                 
SEQADV 6GR9 ASP A  136  UNP  Q9UQB9    GLU   102 CONFLICT                       
SEQADV 6GR9 MET B  834  UNP  Q9NQS7              INITIATING METHIONINE          
SEQRES   1 A  274  GLY ALA ASN SER ARG ARG LEU TPO VAL ASP ASP PHE GLU          
SEQRES   2 A  274  ILE GLY ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN VAL          
SEQRES   3 A  274  TYR LEU ALA ARG LEU LYS GLU SER HIS PHE ILE VAL ALA          
SEQRES   4 A  274  LEU LYS VAL LEU PHE LYS SER GLN ILE GLU LYS GLU GLY          
SEQRES   5 A  274  LEU GLU HIS GLN LEU ARG ARG GLU ILE GLU ILE GLN ALA          
SEQRES   6 A  274  HIS LEU GLN HIS PRO ASN ILE LEU ARG LEU TYR ASN TYR          
SEQRES   7 A  274  PHE HIS ASP ALA ARG ARG VAL TYR LEU ILE LEU GLU TYR          
SEQRES   8 A  274  ALA PRO ARG GLY GLU LEU TYR LYS GLU LEU GLN LYS SER          
SEQRES   9 A  274  ASP LYS LEU ASP GLU GLN ARG THR ALA THR ILE ILE GLU          
SEQRES  10 A  274  GLU LEU ALA ASP ALA LEU THR TYR CYS HIS ASP LYS LYS          
SEQRES  11 A  274  VAL ILE HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU LEU          
SEQRES  12 A  274  GLY PHE ARG GLY GLU VAL LYS ILE ALA ASP PHE GLY TRP          
SEQRES  13 A  274  SER VAL HIS THR PRO SER LEU ARG ARG LYS TPO MET CYS          
SEQRES  14 A  274  GLY THR LEU ASP TYR LEU PRO PRO GLU MET ILE GLU GLY          
SEQRES  15 A  274  ARG THR TYR ASP GLU LYS VAL ASP LEU TRP CYS ILE GLY          
SEQRES  16 A  274  VAL LEU CYS TYR GLU LEU LEU VAL GLY TYR PRO PRO PHE          
SEQRES  17 A  274  GLU SER ALA SER HIS SER GLU THR TYR ARG ARG ILE LEU          
SEQRES  18 A  274  LYS VAL ASP VAL ARG PHE PRO LEU SER MET PRO LEU GLY          
SEQRES  19 A  274  ALA ARG ASP LEU ILE SER ARG LEU LEU ARG TYR GLN PRO          
SEQRES  20 A  274  LEU GLU ARG LEU PRO LEU ALA GLN ILE LEU LYS HIS PRO          
SEQRES  21 A  274  TRP VAL GLN ALA HIS SER ARG ARG VAL LEU PRO PRO CYS          
SEQRES  22 A  274  ALA                                                          
SEQRES   1 B   70  MET GLU ALA HIS PRO ARG LYS PRO ILE PRO THR TRP ALA          
SEQRES   2 B   70  ARG GLY THR PRO LEU SER GLN ALA ILE ILE HIS GLN TYR          
SEQRES   3 B   70  TYR HIS PRO PRO ASN LEU LEU GLU LEU PHE GLY THR ILE          
SEQRES   4 B   70  LEU PRO LEU ASP LEU GLU ASP ILE PHE LYS LYS SER LYS          
SEQRES   5 B   70  PRO ARG TYR HIS LYS ARG THR SEP SEP ALA VAL TRP ASN          
SEQRES   6 B   70  SER PRO PRO LEU GLN                                          
MODRES 6GR9 TPO A   39  THR  MODIFIED RESIDUE                                   
MODRES 6GR9 TPO A  198  THR  MODIFIED RESIDUE                                   
MODRES 6GR9 SEP B  893  SER  MODIFIED RESIDUE                                   
MODRES 6GR9 SEP B  894  SER  MODIFIED RESIDUE                                   
HET    TPO  A  39      11                                                       
HET    TPO  A 198      11                                                       
HET    SEP  B 893      10                                                       
HET    SEP  B 894      10                                                       
HET    VX6  A 401      33                                                       
HET    SO4  A 402       5                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     VX6 CYCLOPROPANECARBOXYLIC ACID {4-[4-(4-METHYL-PIPERAZIN-           
HETNAM   2 VX6  1-YL)-6-(5-METHYL-2H-PYRAZOL-3-YLAMINO)-PYRIMIDIN-2-            
HETNAM   3 VX6  YLSULFANYL]-PHENYL}-AMIDE                                       
HETNAM     SO4 SULFATE ION                                                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   2  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  VX6    C23 H28 N8 O S                                               
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *162(H2 O)                                                    
HELIX    1 AA1 TPO A   39  ASP A   41  5                                   3    
HELIX    2 AA2 GLY A   50  LYS A   53  5                                   4    
HELIX    3 AA3 LYS A   76  GLU A   82  1                                   7    
HELIX    4 AA4 LEU A   84  HIS A   97  1                                  14    
HELIX    5 AA5 LEU A  128  ASP A  136  1                                   9    
HELIX    6 AA6 ASP A  139  LYS A  160  1                                  22    
HELIX    7 AA7 LYS A  168  GLU A  170  5                                   3    
HELIX    8 AA8 THR A  202  LEU A  206  5                                   5    
HELIX    9 AA9 PRO A  207  GLU A  212  1                                   6    
HELIX   10 AB1 LYS A  219  GLY A  235  1                                  17    
HELIX   11 AB2 SER A  243  LYS A  253  1                                  11    
HELIX   12 AB3 PRO A  263  LEU A  274  1                                  12    
HELIX   13 AB4 GLN A  277  ARG A  281  5                                   5    
HELIX   14 AB5 PRO A  283  LYS A  289  1                                   7    
HELIX   15 AB6 HIS A  290  SER A  297  1                                   8    
HELIX   16 AB7 PRO B  843  ALA B  846  5                                   4    
HELIX   17 AB8 ARG B  847  HIS B  861  1                                  15    
HELIX   18 AB9 ASN B  864  GLY B  870  1                                   7    
HELIX   19 AC1 ASP B  876  LYS B  882  1                                   7    
HELIX   20 AC2 THR B  892  VAL B  896  5                                   5    
SHEET    1 AA1 5 PHE A  43  PRO A  48  0                                        
SHEET    2 AA1 5 ASN A  56  LEU A  62 -1  O  LEU A  59   N  GLY A  46           
SHEET    3 AA1 5 ILE A  68  PHE A  75 -1  O  LEU A  71   N  TYR A  58           
SHEET    4 AA1 5 ARG A 115  LEU A 120 -1  O  VAL A 116   N  LEU A  74           
SHEET    5 AA1 5 LEU A 106  HIS A 111 -1  N  ASN A 108   O  ILE A 119           
SHEET    1 AA2 3 GLY A 126  GLU A 127  0                                        
SHEET    2 AA2 3 LEU A 172  LEU A 174 -1  O  LEU A 174   N  GLY A 126           
SHEET    3 AA2 3 VAL A 180  ILE A 182 -1  O  LYS A 181   N  LEU A 173           
SHEET    1 AA3 2 VAL A 162  ILE A 163  0                                        
SHEET    2 AA3 2 VAL A 189  HIS A 190 -1  O  VAL A 189   N  ILE A 163           
LINK         C   LEU A  38                 N   TPO A  39     1555   1555  1.35  
LINK         C   TPO A  39                 N   VAL A  40     1555   1555  1.34  
LINK         C   LYS A 197                 N   TPO A 198     1555   1555  1.34  
LINK         C   TPO A 198                 N   MET A 199     1555   1555  1.33  
LINK         C   THR B 892                 N   SEP B 893     1555   1555  1.34  
LINK         C   SEP B 893                 N   SEP B 894     1555   1555  1.34  
LINK         C   SEP B 894                 N   ALA B 895     1555   1555  1.34  
SITE     1 AC1 11 GLY A  50  PHE A  54  ALA A  70  GLU A 121                    
SITE     2 AC1 11 TYR A 122  ALA A 123  PRO A 124  GLY A 126                    
SITE     3 AC1 11 LEU A 173  ALA A 183  HOH A 526                               
SITE     1 AC2  3 SER A  77  ARG A 114  HOH A 504                               
CRYST1   82.617   82.617  121.000  90.00  90.00 120.00 P 31 2 1      6          
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      0.012104  0.006988  0.000000        0.00000                         
SCALE2      0.000000  0.013977  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008264        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system