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Database: PDB
Entry: 3SI5
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Original site: 3SI5 
HEADER    CELL CYCLE                              17-JUN-11   3SI5              
TITLE     KINETOCHORE-BUBR1 KINASE COMPLEX                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1    
COMPND   3 BETA;                                                                
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 67-220;                                       
COMPND   6 SYNONYM: MAD3/BUB1-RELATED PROTEIN KINASE, HBUBR1, MITOTIC CHECKPOINT
COMPND   7 KINASE MAD3L, PROTEIN SSK1;                                          
COMPND   8 EC: 2.7.11.1;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: PROTEIN CASC5;                                             
COMPND  12 CHAIN: X, Y;                                                         
COMPND  13 FRAGMENT: UNP RESIDUES 234-252;                                      
COMPND  14 SYNONYM: ALL1-FUSED GENE FROM CHROMOSOME 15Q14 PROTEIN, AF15Q14, BUB-
COMPND  15 LINKING KINETOCHORE PROTEIN, BLINKIN, CANCER SUSCEPTIBILITY CANDIDATE
COMPND  16 GENE 5 PROTEIN, CANCER/TESTIS ANTIGEN 29, CT29, KINETOCHORE-NULL     
COMPND  17 PROTEIN 1, PROTEIN D40/AF15Q14;                                      
COMPND  18 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: BUB1B, BUBR1, MAD3L, SSK1;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: GST;                                  
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CASC5, KIAA1570, KNL1;                                         
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: GST;                                  
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX                                      
KEYWDS    BUBR1-BLINKIN COMPLEX, MITOTIC CHECKPOINT, BUBR1, BLINKIN/KNL1,       
KEYWDS   2 CHROMOSOME SEGREGATION, CELL CYCLE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.L.BLUNDELL,D.Y.CHIRGADZE,V.M.BOLANOS-GARCIA                         
REVDAT   2   30-NOV-11 3SI5    1       JRNL                                     
REVDAT   1   26-OCT-11 3SI5    0                                                
JRNL        AUTH   V.M.BOLANOS-GARCIA,T.LISCHETTI,D.MATAK-VINKOVIC,E.COTA,      
JRNL        AUTH 2 P.J.SIMPSON,D.Y.CHIRGADZE,D.R.SPRING,C.V.ROBINSON,J.NILSSON, 
JRNL        AUTH 3 T.L.BLUNDELL                                                 
JRNL        TITL   STRUCTURE OF A BLINKIN-BUBR1 COMPLEX REVEALS AN INTERACTION  
JRNL        TITL 2 CRUCIAL FOR KINETOCHORE-MITOTIC CHECKPOINT REGULATION VIA AN 
JRNL        TITL 3 UNANTICIPATED BINDING SITE.                                  
JRNL        REF    STRUCTURE                     V.  19  1691 2011              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   22000412                                                     
JRNL        DOI    10.1016/J.STR.2011.09.017                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 18278                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 985                             
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1347                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 70                           
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2756                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 250                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.225         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.159         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.612        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2866 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3875 ; 1.116 ; 1.930       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   340 ; 5.113 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   174 ;40.501 ;23.908       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   491 ;15.141 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;17.699 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   385 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2290 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1667 ; 0.603 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2658 ; 1.133 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1199 ; 1.655 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1211 ; 2.733 ; 4.500       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    54        A   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7898  -0.1732  31.4405              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1553 T22:   0.1385                                     
REMARK   3      T33:   0.1604 T12:  -0.0096                                     
REMARK   3      T13:  -0.0058 T23:   0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3243 L22:   0.1335                                     
REMARK   3      L33:   0.6627 L12:   0.1350                                     
REMARK   3      L13:   0.4737 L23:   0.1689                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0106 S12:  -0.0138 S13:   0.0050                       
REMARK   3      S21:   0.0193 S22:  -0.0257 S23:   0.0016                       
REMARK   3      S31:   0.0243 S32:  -0.0326 S33:   0.0152                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    55        B   203                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.6858   9.7792  13.6067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1600 T22:   0.1301                                     
REMARK   3      T33:   0.1499 T12:  -0.0028                                     
REMARK   3      T13:  -0.0101 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3099 L22:   0.1606                                     
REMARK   3      L33:   1.4972 L12:   0.2216                                     
REMARK   3      L13:  -0.5514 L23:  -0.4061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0035 S12:  -0.0092 S13:  -0.0182                       
REMARK   3      S21:  -0.0026 S22:  -0.0290 S23:   0.0019                       
REMARK   3      S31:  -0.0591 S32:  -0.0215 S33:   0.0255                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X     2        X    19                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0900   7.7074  17.5814              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1951 T22:   0.2051                                     
REMARK   3      T33:   0.1001 T12:  -0.0330                                     
REMARK   3      T13:   0.0030 T23:  -0.0424                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.8371 L22:   9.1263                                     
REMARK   3      L33:   0.0347 L12:  -5.6074                                     
REMARK   3      L13:  -0.2818 L23:   1.7082                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2274 S12:   0.3935 S13:  -0.1987                       
REMARK   3      S21:  -0.6638 S22:  -0.1728 S23:   0.1254                       
REMARK   3      S31:  -0.1653 S32:   0.1390 S33:  -0.0546                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y     6        Y    18                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.2230   5.7306   6.0214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0294 T22:   0.8969                                     
REMARK   3      T33:   0.1625 T12:  -0.2080                                     
REMARK   3      T13:  -0.1167 T23:   0.4503                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.5119 L22:  23.3269                                     
REMARK   3      L33:  10.9089 L12:   0.8577                                     
REMARK   3      L13:  -1.9466 L23:  15.4918                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4008 S12:  -0.0045 S13:  -0.1507                       
REMARK   3      S21:  -0.6329 S22:   0.0663 S23:   0.2502                       
REMARK   3      S31:  -0.2076 S32:  -1.3103 S33:  -0.4671                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3SI5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066231.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR-H             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : HELIOS MX  MIRRORS                 
REMARK 200  OPTICS                         : HELIOS MX CU X-RAY OPTICS FOR X8   
REMARK 200                                   PROTEUM/MICROSTAR                  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER PLATINUM 135                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SADABS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19266                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : 0.11900                            
REMARK 200  R SYM                      (I) : 0.11900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.46500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 2WVI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 6000, 0.1M MAGNESIUM ACETATE,    
REMARK 280  0.1M SODIUM CACODYLATE, PH 6.0, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 292K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       62.19900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.07150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       62.19900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       20.07150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 1170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 930 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 9690 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Y                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 280  LIES ON A SPECIAL POSITION.                          
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     THR A    45                                                      
REMARK 465     GLY A    46                                                      
REMARK 465     SER A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     GLY A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     THR A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     SER A    53                                                      
REMARK 465     LEU A   206                                                      
REMARK 465     ALA A   207                                                      
REMARK 465     LEU A   208                                                      
REMARK 465     GLU A   209                                                      
REMARK 465     LYS A   210                                                      
REMARK 465     GLU A   211                                                      
REMARK 465     GLU A   212                                                      
REMARK 465     GLU A   213                                                      
REMARK 465     GLU A   214                                                      
REMARK 465     GLU A   215                                                      
REMARK 465     VAL A   216                                                      
REMARK 465     PHE A   217                                                      
REMARK 465     GLU A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     SER A   220                                                      
REMARK 465     THR B    45                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     SER B    47                                                      
REMARK 465     THR B    48                                                      
REMARK 465     GLY B    49                                                      
REMARK 465     SER B    50                                                      
REMARK 465     THR B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     THR B    54                                                      
REMARK 465     THR B   204                                                      
REMARK 465     LEU B   205                                                      
REMARK 465     LEU B   206                                                      
REMARK 465     ALA B   207                                                      
REMARK 465     LEU B   208                                                      
REMARK 465     GLU B   209                                                      
REMARK 465     LYS B   210                                                      
REMARK 465     GLU B   211                                                      
REMARK 465     GLU B   212                                                      
REMARK 465     GLU B   213                                                      
REMARK 465     GLU B   214                                                      
REMARK 465     GLU B   215                                                      
REMARK 465     VAL B   216                                                      
REMARK 465     PHE B   217                                                      
REMARK 465     GLU B   218                                                      
REMARK 465     SER B   219                                                      
REMARK 465     SER B   220                                                      
REMARK 465     GLY X   203                                                      
REMARK 465     PRO X   204                                                      
REMARK 465     LEU X   205                                                      
REMARK 465     GLY X   206                                                      
REMARK 465     SER X   207                                                      
REMARK 465     LYS X   226                                                      
REMARK 465     GLY Y   203                                                      
REMARK 465     PRO Y   204                                                      
REMARK 465     LEU Y   205                                                      
REMARK 465     GLY Y   206                                                      
REMARK 465     SER Y   207                                                      
REMARK 465     SER Y   208                                                      
REMARK 465     SER Y   209                                                      
REMARK 465     GLU Y   210                                                      
REMARK 465     ASN Y   211                                                      
REMARK 465     GLY Y   225                                                      
REMARK 465     LYS Y   226                                                      
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     SER A  56    OG                                                  
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     ARG A 130    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B  56    OG                                                  
REMARK 470     LYS B  94    CG   CD   CE   NZ                                   
REMARK 470     GLU B  95    CG   CD   OE1  OE2                                  
REMARK 470     SER X 208    OG                                                  
REMARK 470     GLU X 210    CG   CD   OE1  OE2                                  
REMARK 470     LYS Y 212    CG   CD   CE   NZ                                   
REMARK 470     ARG Y 221    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS Y 223    CG   CD   CE   NZ                                   
REMARK 470     THR Y 224    OG1  CG2                                            
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    GLN B 110      120.66    -37.18                                   
REMARK 500    GLU X 210      -82.17      0.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 261        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH A 264        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH B 238        DISTANCE =  6.69 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WVI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF BUBR1                  
REMARK 900 RELATED ID: 3ESL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CONSERVED N-TERMINAL DOMAIN OF THE          
REMARK 900 MITOTIC CHECKPOINT COMPONENT BUB1                                    
REMARK 900 RELATED ID: 2LAH   RELATED DB: PDB                                   
REMARK 900 SOLUTION NMR STRUCTURE OF MITOTIC CHECKPOINT SERINE/                 
REMARK 900 THREONINE-PROTEIN KINASE BUB1 N-TERMINAL DOMAIN FROM HOMO            
REMARK 900 SAPIENS                                                              
REMARK 900 RELATED ID: 3E7E   RELATED DB: PDB                                   
REMARK 900 STRUCTURE AND SUBSTRATE RECRUITMENT OF THE HUMAN SPINDLE             
REMARK 900 CHECKPOINT KINASE BUB                                                
REMARK 900 RELATED ID: 2I3S   RELATED DB: PDB                                   
REMARK 900 BUB3 COMPLEX WITH BUB1 GLEBS MOTIF                                   
DBREF  3SI5 A   57   220  UNP    O60566   BUB1B_HUMAN     67    230             
DBREF  3SI5 B   57   220  UNP    O60566   BUB1B_HUMAN     67    230             
DBREF  3SI5 X  208   226  UNP    Q8NG31   CASC5_HUMAN    234    252             
DBREF  3SI5 Y  208   226  UNP    Q8NG31   CASC5_HUMAN    234    252             
SEQADV 3SI5 THR A   45  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 GLY A   46  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 SER A   47  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 THR A   48  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 GLY A   49  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 SER A   50  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 THR A   51  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 GLY A   52  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 SER A   53  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 THR A   54  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 GLY A   55  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 SER A   56  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 THR B   45  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 GLY B   46  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 SER B   47  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 THR B   48  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 GLY B   49  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 SER B   50  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 THR B   51  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 GLY B   52  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 SER B   53  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 THR B   54  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 GLY B   55  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 SER B   56  UNP  O60566              EXPRESSION TAG                 
SEQADV 3SI5 GLY X  203  UNP  Q8NG31              EXPRESSION TAG                 
SEQADV 3SI5 PRO X  204  UNP  Q8NG31              EXPRESSION TAG                 
SEQADV 3SI5 LEU X  205  UNP  Q8NG31              EXPRESSION TAG                 
SEQADV 3SI5 GLY X  206  UNP  Q8NG31              EXPRESSION TAG                 
SEQADV 3SI5 SER X  207  UNP  Q8NG31              EXPRESSION TAG                 
SEQADV 3SI5 GLY Y  203  UNP  Q8NG31              EXPRESSION TAG                 
SEQADV 3SI5 PRO Y  204  UNP  Q8NG31              EXPRESSION TAG                 
SEQADV 3SI5 LEU Y  205  UNP  Q8NG31              EXPRESSION TAG                 
SEQADV 3SI5 GLY Y  206  UNP  Q8NG31              EXPRESSION TAG                 
SEQADV 3SI5 SER Y  207  UNP  Q8NG31              EXPRESSION TAG                 
SEQRES   1 A  176  THR GLY SER THR GLY SER THR GLY SER THR GLY SER GLN          
SEQRES   2 A  176  GLN LYS ARG ALA PHE GLU TYR GLU ILE ARG PHE TYR THR          
SEQRES   3 A  176  GLY ASN ASP PRO LEU ASP VAL TRP ASP ARG TYR ILE SER          
SEQRES   4 A  176  TRP THR GLU GLN ASN TYR PRO GLN GLY GLY LYS GLU SER          
SEQRES   5 A  176  ASN MET SER THR LEU LEU GLU ARG ALA VAL GLU ALA LEU          
SEQRES   6 A  176  GLN GLY GLU LYS ARG TYR TYR SER ASP PRO ARG PHE LEU          
SEQRES   7 A  176  ASN LEU TRP LEU LYS LEU GLY ARG LEU CYS ASN GLU PRO          
SEQRES   8 A  176  LEU ASP MET TYR SER TYR LEU HIS ASN GLN GLY ILE GLY          
SEQRES   9 A  176  VAL SER LEU ALA GLN PHE TYR ILE SER TRP ALA GLU GLU          
SEQRES  10 A  176  TYR GLU ALA ARG GLU ASN PHE ARG LYS ALA ASP ALA ILE          
SEQRES  11 A  176  PHE GLN GLU GLY ILE GLN GLN LYS ALA GLU PRO LEU GLU          
SEQRES  12 A  176  ARG LEU GLN SER GLN HIS ARG GLN PHE GLN ALA ARG VAL          
SEQRES  13 A  176  SER ARG GLN THR LEU LEU ALA LEU GLU LYS GLU GLU GLU          
SEQRES  14 A  176  GLU GLU VAL PHE GLU SER SER                                  
SEQRES   1 B  176  THR GLY SER THR GLY SER THR GLY SER THR GLY SER GLN          
SEQRES   2 B  176  GLN LYS ARG ALA PHE GLU TYR GLU ILE ARG PHE TYR THR          
SEQRES   3 B  176  GLY ASN ASP PRO LEU ASP VAL TRP ASP ARG TYR ILE SER          
SEQRES   4 B  176  TRP THR GLU GLN ASN TYR PRO GLN GLY GLY LYS GLU SER          
SEQRES   5 B  176  ASN MET SER THR LEU LEU GLU ARG ALA VAL GLU ALA LEU          
SEQRES   6 B  176  GLN GLY GLU LYS ARG TYR TYR SER ASP PRO ARG PHE LEU          
SEQRES   7 B  176  ASN LEU TRP LEU LYS LEU GLY ARG LEU CYS ASN GLU PRO          
SEQRES   8 B  176  LEU ASP MET TYR SER TYR LEU HIS ASN GLN GLY ILE GLY          
SEQRES   9 B  176  VAL SER LEU ALA GLN PHE TYR ILE SER TRP ALA GLU GLU          
SEQRES  10 B  176  TYR GLU ALA ARG GLU ASN PHE ARG LYS ALA ASP ALA ILE          
SEQRES  11 B  176  PHE GLN GLU GLY ILE GLN GLN LYS ALA GLU PRO LEU GLU          
SEQRES  12 B  176  ARG LEU GLN SER GLN HIS ARG GLN PHE GLN ALA ARG VAL          
SEQRES  13 B  176  SER ARG GLN THR LEU LEU ALA LEU GLU LYS GLU GLU GLU          
SEQRES  14 B  176  GLU GLU VAL PHE GLU SER SER                                  
SEQRES   1 X   24  GLY PRO LEU GLY SER SER SER GLU ASN LYS ILE ASP PHE          
SEQRES   2 X   24  ASN ASP PHE ILE LYS ARG LEU LYS THR GLY LYS                  
SEQRES   1 Y   24  GLY PRO LEU GLY SER SER SER GLU ASN LYS ILE ASP PHE          
SEQRES   2 Y   24  ASN ASP PHE ILE LYS ARG LEU LYS THR GLY LYS                  
FORMUL   5  HOH   *250(H2 O)                                                    
HELIX    1   1 THR A   54  TYR A   69  1                                  16    
HELIX    2   2 PRO A   74  TYR A   89  1                                  16    
HELIX    3   3 GLY A   93  SER A   96  5                                   4    
HELIX    4   4 ASN A   97  GLN A  110  1                                  14    
HELIX    5   5 GLU A  112  TYR A  116  5                                   5    
HELIX    6   6 ASP A  118  ARG A  130  1                                  13    
HELIX    7   7 GLU A  134  GLY A  146  1                                  13    
HELIX    8   8 LEU A  151  ARG A  165  1                                  15    
HELIX    9   9 ASN A  167  GLN A  181  1                                  15    
HELIX   10  10 PRO A  185  GLN A  203  1                                  19    
HELIX   11  11 SER B   56  PHE B   68  1                                  13    
HELIX   12  12 ASP B   73  TYR B   89  1                                  17    
HELIX   13  13 ASN B   97  GLN B  110  1                                  14    
HELIX   14  14 GLU B  112  TYR B  116  5                                   5    
HELIX   15  15 ASP B  118  ARG B  130  1                                  13    
HELIX   16  16 GLU B  134  GLY B  146  1                                  13    
HELIX   17  17 LEU B  151  ARG B  165  1                                  15    
HELIX   18  18 ASN B  167  GLN B  181  1                                  15    
HELIX   19  19 PRO B  185  VAL B  200  1                                  16    
HELIX   20  20 SER B  201  GLN B  203  5                                   3    
HELIX   21  21 ASP X  214  GLY X  225  1                                  12    
HELIX   22  22 ASP Y  214  THR Y  224  1                                  11    
CISPEP   1 GLU A  184    PRO A  185          0        -3.68                     
CISPEP   2 GLU B  184    PRO B  185          0        -8.23                     
CRYST1  124.398   40.143   75.391  90.00  91.38  90.00 C 1 2 1       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      0.008039  0.000000  0.000194        0.00000                         
SCALE2      0.000000  0.024911  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013268        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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