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Database: PDB
Entry: 2WVI
LinkDB: 2WVI
Original site: 2WVI 
HEADER    TRANSFERASE                             16-OCT-09   2WVI              
TITLE     CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF BUBR1                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN                
COMPND   3  KINASE BUB1 BETA;                                                   
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: N-TERMINAL TPR DOMAIN, RESIDUES 57-220;                    
COMPND   6 SYNONYM: MAD3/BUB1-RELATED PROTEIN KINASE, HBUBR1, MITOTIC           
COMPND   7  CHECKPOINT KINASE MAD3L, PROTEIN SSK1, BUBR1;                       
COMPND   8 EC: 2.7.11.1;                                                        
COMPND   9 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: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PHAT4                                     
KEYWDS    TUMOR SUPPRESSOR, MITOTIC CHECKPOINT, TPR, KINASE,                    
KEYWDS   2 APOPTOSIS, SERINE/THREONINE-PROTEIN KINASE, CELL DIVISION,           
KEYWDS   3 CELL CYCLE, KINETOCHORE, TRANSFERASE, CYTOSKELETON                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.D'ARCY,O.R.DAVIES,T.L.BLUNDELL,V.M.BOLANOS-GARCIA                   
REVDAT   2   07-JUL-10 2WVI    1       JRNL                                     
REVDAT   1   09-MAR-10 2WVI    0                                                
JRNL        AUTH   S.D'ARCY,O.R.DAVIES,T.L.BLUNDELL,V.M.BOLANOS-GARCIA          
JRNL        TITL   DEFINING THE MOLECULAR BASIS OF BUBR1 KINETOCHORE            
JRNL        TITL 2 INTERACTIONS AND ANAPHASE-PROMOTING                          
JRNL        TITL 3 COMPLEX/CYCLOSOME (APC/C)-CDC20 INHIBITION                   
JRNL        REF    J.BIOL.CHEM.                  V. 285 14764 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20220147                                                     
JRNL        DOI    10.1074/JBC.M109.082016                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.91                          
REMARK   3   NUMBER OF REFLECTIONS             : 18643                          
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) : 0.22373                         
REMARK   3   R VALUE            (WORKING SET) : 0.22188                         
REMARK   3   FREE R VALUE                     : 0.25986                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1005                            
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) : 1.800                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.847                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1367                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.255                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.346                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1358                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 117                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22                             
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.105                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.24                                                 
REMARK   3    B22 (A**2) : 2.24                                                 
REMARK   3    B33 (A**2) : -3.35                                                
REMARK   3    B12 (A**2) : 1.12                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.139         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.135         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.106         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.444         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1398 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1880 ; 1.685 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   158 ;11.934 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    86 ;41.267 ;24.186       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   245 ;16.693 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;17.768 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   186 ; 0.135 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1105 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   699 ; 0.236 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   943 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    91 ; 0.170 ; 0.200       
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):    70 ; 0.301 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.148 ; 0.200       
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):   827 ; 1.064 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1277 ; 1.679 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   666 ; 2.772 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   603 ; 4.257 ; 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  : NULL                                       
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          
REMARK   3   RIDING POSITIONS. DENSITY WAS NOT OBSERVED FOR RESIDUES            
REMARK   3   92-95. ONE ROUND OF TLS WAS CONDUCTED DURING REFINEMENT.           
REMARK   3   TWO GROUPS WERE USED; RESIDUES 57-114 AND 115-220.                 
REMARK   4                                                                      
REMARK   4 2WVI COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-OCT-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41277.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
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) : 1.06                               
REMARK 200  MONOCHROMATOR                  : SI (111) DOUBLE CRYSTAL            
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : KIRKPATRICK BAEZ BIMORPH           
REMARK 200                                   MIRROR PAIR FOR HORIZONTAL         
REMARK 200                                   AND VERTICAL FOCUSSING             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
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   : 19685                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.62                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 15.6                               
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 15.8                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THIS DATA SET WAS USED IN REFINEMENTS.                       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% (W/V) PEG 8000, 0.17 M             
REMARK 280  TRIS PH 8.0, 0.01 M PRASEODYMIUM(III) ACETATE                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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       60.30000            
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       30.15000            
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       30.15000            
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       60.30000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND                           
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 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     GLY A    92                                                      
REMARK 465     GLY A    93                                                      
REMARK 465     LYS A    94                                                      
REMARK 465     GLU A    95                                                      
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   O    HOH A  2009     O    HOH A  2009     5557     1.36            
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    GLU A 218   CD    GLU A 218   OE1     0.112                       
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    PRO A 185   C   -  N   -  CA  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    PRO A 185   C   -  N   -  CD  ANGL. DEV. = -13.1 DEGREES          
REMARK 500    GLU A 218   CG  -  CD  -  OE1 ANGL. DEV. =  17.4 DEGREES          
REMARK 500    GLU A 218   CG  -  CD  -  OE2 ANGL. DEV. = -12.4 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    ILE A  66       71.36    -69.72                                   
REMARK 500    PHE A  68       43.96    -91.71                                   
REMARK 500    PRO A  90        0.79    -57.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  184     PRO A  185                  -46.79                    
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    GLU A 184        -11.77                                           
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    ARG A  67        19.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 ETHANE-1,2-DIOL (EDO): USED AS CRYOPROTECTANT                        
REMARK 600 PRASEODYMIUM ION (PR): ESSENTIAL FOR HIGH RESOLUTION OF              
REMARK 600  CRYSTALS AND USED FOR PHASING                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PR A1221  PR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 137   OD2                                                    
REMARK 620 2 ACT A1223   O   127.7                                              
REMARK 620 3 ACT A1223   OXT  75.7  52.5                                        
REMARK 620 4 GLU A 134   OE1  85.6  81.6  82.0                                  
REMARK 620 5 GLU A 215   OE2 153.1  68.0 118.4  74.7                            
REMARK 620 6 GLU A 218   OE1 130.3  83.4 115.0 142.0  67.3                      
REMARK 620 7 GLU A 218   OE2  83.7  87.6  73.9 155.4 121.2  57.1                
REMARK 620 8 GLU A 214   OE2  78.6 143.0 146.3  74.6  78.6  98.3 124.4          
REMARK 620 9 GLU A 214   OE1  83.2 143.5 144.9 124.4  92.7  60.4  76.2  49.8    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PR A1222  PR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACT A1223   O                                                      
REMARK 620 2 GLU A 134   OE2  77.0                                              
REMARK 620 3 GLN A 190   OE1 149.1  78.2                                        
REMARK 620 4 GLU A 215   OE2  68.5  76.5 122.4                                  
REMARK 620 5 HOH A2046   O    73.6  75.8  82.8 136.9                            
REMARK 620 6 GLU A 187   OE1 135.6 147.1  71.9 108.6 112.6                      
REMARK 620 7 GLU A 187   OE2 100.1 141.6  88.2 138.8  66.9  51.5                
REMARK 620 8 GLU A 215   OE1 117.1  85.4  78.6  48.7 155.9  75.8 127.1          
REMARK 620 9 HOH A2114   O    66.9 136.5 142.9  68.3 114.1  71.1  70.8  89.9    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  PR A1221                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  PR A1222                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1223                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1224                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1225                 
DBREF  2WVI A   57   220  UNP    O60566   BUB1B_HUMAN     57    220             
SEQRES   1 A  164  GLN GLN LYS ARG ALA PHE GLU TYR GLU ILE ARG PHE TYR          
SEQRES   2 A  164  THR GLY ASN ASP PRO LEU ASP VAL TRP ASP ARG TYR ILE          
SEQRES   3 A  164  SER TRP THR GLU GLN ASN TYR PRO GLN GLY GLY LYS GLU          
SEQRES   4 A  164  SER ASN MET SER THR LEU LEU GLU ARG ALA VAL GLU ALA          
SEQRES   5 A  164  LEU GLN GLY GLU LYS ARG TYR TYR SER ASP PRO ARG PHE          
SEQRES   6 A  164  LEU ASN LEU TRP LEU LYS LEU GLY ARG LEU CYS ASN GLU          
SEQRES   7 A  164  PRO LEU ASP MET TYR SER TYR LEU HIS ASN GLN GLY ILE          
SEQRES   8 A  164  GLY VAL SER LEU ALA GLN PHE TYR ILE SER TRP ALA GLU          
SEQRES   9 A  164  GLU TYR GLU ALA ARG GLU ASN PHE ARG LYS ALA ASP ALA          
SEQRES  10 A  164  ILE PHE GLN GLU GLY ILE GLN GLN LYS ALA GLU PRO LEU          
SEQRES  11 A  164  GLU ARG LEU GLN SER GLN HIS ARG GLN PHE GLN ALA ARG          
SEQRES  12 A  164  VAL SER ARG GLN THR LEU LEU ALA LEU GLU LYS GLU GLU          
SEQRES  13 A  164  GLU GLU GLU VAL PHE GLU SER SER                              
HET     PR  A1221       1                                                       
HET     PR  A1222       1                                                       
HET    ACT  A1223       4                                                       
HET    EDO  A1224       4                                                       
HET    EDO  A1225       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETNAM      PR PRASEODYMIUM ION                                                 
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    2(C2 H6 O2)                                                  
FORMUL   3  ACT    C2 H3 O2 1-                                                  
FORMUL   4   PR    2(PR 3+)                                                     
FORMUL   5  HOH   *117(H2 O)                                                    
HELIX    1   1 LYS A   59  ILE A   66  1                                   8    
HELIX    2   2 PRO A   74  TYR A   89  1                                  16    
HELIX    3   3 ASN A   97  LEU A  109  1                                  13    
HELIX    4   4 GLU A  112  TYR A  116  5                                   5    
HELIX    5   5 ASP A  118  CYS A  132  1                                  15    
HELIX    6   6 GLU A  134  GLN A  145  1                                  12    
HELIX    7   7 LEU A  151  ARG A  165  1                                  15    
HELIX    8   8 ASN A  167  GLN A  181  1                                  15    
HELIX    9   9 PRO A  185  SER A  219  1                                  35    
LINK        PR    PR A1221                 OD2 ASP A 137     1555   6666  2.37  
LINK        PR    PR A1221                 O   ACT A1223     1555   1555  2.45  
LINK        PR    PR A1221                 OXT ACT A1223     1555   1555  2.57  
LINK        PR    PR A1221                 OE1 GLU A 134     1555   6666  2.53  
LINK        PR    PR A1221                 OE2 GLU A 215     1555   1555  2.62  
LINK        PR    PR A1221                 OE1 GLU A 218     1555   1555  1.49  
LINK        PR    PR A1221                 OE2 GLU A 218     1555   1555  2.61  
LINK        PR    PR A1221                 OE2 GLU A 214     1555   1555  2.63  
LINK        PR    PR A1221                 OE1 GLU A 214     1555   1555  2.64  
LINK        PR    PR A1222                 OE2 GLU A 134     1555   6666  2.41  
LINK        PR    PR A1222                 OE1 GLN A 190     1555   4557  2.49  
LINK        PR    PR A1222                 OE2 GLU A 215     1555   1555  2.55  
LINK        PR    PR A1222                 O   HOH A2046     1555   6666  2.64  
LINK        PR    PR A1222                 OE1 GLU A 187     1555   4557  2.47  
LINK        PR    PR A1222                 OE2 GLU A 187     1555   4557  2.50  
LINK        PR    PR A1222                 OE1 GLU A 215     1555   1555  2.62  
LINK        PR    PR A1222                 O   HOH A2114     1555   1555  2.34  
LINK        PR    PR A1222                 O   ACT A1223     1555   1555  2.50  
SITE     1 AC1  6 GLU A 134  ASP A 137  GLU A 214  GLU A 215                    
SITE     2 AC1  6 GLU A 218  ACT A1223                                          
SITE     1 AC2  7 GLU A 134  GLU A 187  GLN A 190  GLU A 215                    
SITE     2 AC2  7 ACT A1223  HOH A2046  HOH A2114                               
SITE     1 AC3 11 GLU A 134  PRO A 135  LEU A 136  ASP A 137                    
SITE     2 AC3 11 ARG A 165  GLU A 215  GLU A 218   PR A1221                    
SITE     3 AC3 11  PR A1222  HOH A2046  HOH A2114                               
SITE     1 AC4  8 ALA A 164  ARG A 165  GLU A 184  PRO A 185                    
SITE     2 AC4  8 LEU A 186  GLU A 187  HOH A2115  HOH A2116                    
SITE     1 AC5  6 GLU A 134  ARG A 194  GLU A 211  GLU A 214                    
SITE     2 AC5  6 GLU A 215  HOH A2117                                          
CRYST1   62.796   62.796   90.450  90.00  90.00 120.00 P 32 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      0.015925  0.009194  0.000000        0.00000                         
SCALE2      0.000000  0.018388  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011056        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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