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Database: PDB
Entry: 5JJA
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HEADER    SIGNALING PROTEIN                       22-APR-16   5JJA              
TITLE     CRYSTAL STRUCTURE OF A PP2A B56GAMMA/BUBR1 COMPLEX                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 2A 56 KDA REGULATORY  
COMPND   3 SUBUNIT GAMMA ISOFORM;                                               
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: PP2A B SUBUNIT ISOFORM B'-GAMMA,PP2A B SUBUNIT ISOFORM B56- 
COMPND   6 GAMMA,PP2A B SUBUNIT ISOFORM PR61-GAMMA,PP2A B SUBUNIT ISOFORM R5-   
COMPND   7 GAMMA,RENAL CARCINOMA ANTIGEN NY-REN-29;                             
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1    
COMPND  11 BETA;                                                                
COMPND  12 CHAIN: C, D;                                                         
COMPND  13 SYNONYM: MAD3/BUB1-RELATED PROTEIN KINASE,HBUBR1,MITOTIC CHECKPOINT  
COMPND  14 KINASE MAD3L,PROTEIN SSK1;                                           
COMPND  15 EC: 2.7.11.1;                                                        
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP2R5C, KIAA0044;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: BUB1B, BUBR1, MAD3L, SSK1;                                     
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PP2A, BUBR1, B56GAMMA, SIGNALING PROTEIN                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.WANG,J.WANG,Z.RAO,W.XU                                              
REVDAT   1   13-JUL-16 5JJA    0                                                
JRNL        AUTH   J.WANG,Z.WANG,T.YU,H.YANG,D.M.VIRSHUP,G.J.KOPS,S.H.LEE,      
JRNL        AUTH 2 W.ZHOU,X.LI,W.XU,Z.RAO                                       
JRNL        TITL   CRYSTAL STRUCTURE OF A PP2A B56-BUBR1 COMPLEX AND ITS        
JRNL        TITL 2 IMPLICATIONS FOR PP2A SUBSTRATE RECRUITMENT AND              
JRNL        TITL 3 LOCALIZATION.                                                
JRNL        REF    PROTEIN CELL                  V.   7   516 2016              
JRNL        REFN                   ESSN 1674-8018                               
JRNL        PMID   27350047                                                     
JRNL        DOI    10.1007/S13238-016-0283-4                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 54953                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2882                            
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) : 2.36                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.42                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3984                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 218                          
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5687                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 240                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.99000                                              
REMARK   3    B22 (A**2) : -1.69000                                             
REMARK   3    B33 (A**2) : -0.30000                                             
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): 0.188         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.913         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5843 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5708 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7923 ; 1.083 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13171 ; 0.755 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   676 ; 4.777 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   275 ;37.564 ;24.036       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1053 ;12.727 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;11.061 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   881 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6347 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1326 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2722 ; 1.314 ; 3.087       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2721 ; 1.313 ; 3.085       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3392 ; 2.223 ; 4.611       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 2                                          
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    29        A   375                          
REMARK   3    ORIGIN FOR THE GROUP (A):  89.1117  18.2761  15.8956              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0542 T22:   0.0284                                     
REMARK   3      T33:   0.0311 T12:  -0.0026                                     
REMARK   3      T13:   0.0206 T23:  -0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9711 L22:   0.3247                                     
REMARK   3      L33:   1.1858 L12:  -0.1224                                     
REMARK   3      L13:   1.5787 L23:   0.0419                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0018 S12:  -0.0696 S13:  -0.1079                       
REMARK   3      S21:   0.1294 S22:   0.0137 S23:   0.0441                       
REMARK   3      S31:   0.0342 S32:  -0.0218 S33:  -0.0155                       
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    30        B   376                          
REMARK   3    ORIGIN FOR THE GROUP (A):  89.8474 -18.3336 -26.2469              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0854 T22:   0.0210                                     
REMARK   3      T33:   0.0511 T12:  -0.0041                                     
REMARK   3      T13:  -0.0015 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8515 L22:   3.5074                                     
REMARK   3      L33:   1.2152 L12:  -1.2125                                     
REMARK   3      L13:  -0.3817 L23:   1.4945                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0724 S12:  -0.0173 S13:  -0.1652                       
REMARK   3      S21:  -0.1119 S22:  -0.1091 S23:   0.2121                       
REMARK   3      S31:   0.1353 S32:  -0.0294 S33:   0.0367                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 5JJA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220691.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54953                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.50                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2JAK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5 AND 20% PEG 3350,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       43.50850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       83.68600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.79400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       83.68600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.50850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.79400            
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: 1090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: 1090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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     SER A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     ASN A   112                                                      
REMARK 465     PRO A   113                                                      
REMARK 465     THR A   114                                                      
REMARK 465     GLY A   115                                                      
REMARK 465     ALA A   116                                                      
REMARK 465     GLU A   117                                                      
REMARK 465     PHE A   118                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     PRO A   120                                                      
REMARK 465     GLU A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     ASP A   123                                                      
REMARK 465     ARG A   376                                                      
REMARK 465     ASN A   377                                                      
REMARK 465     SER A   378                                                      
REMARK 465     LYS A   379                                                      
REMARK 465     THR A   380                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     SER B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     ASN B   112                                                      
REMARK 465     PRO B   113                                                      
REMARK 465     THR B   114                                                      
REMARK 465     GLY B   115                                                      
REMARK 465     ALA B   116                                                      
REMARK 465     GLU B   117                                                      
REMARK 465     PHE B   118                                                      
REMARK 465     ASP B   119                                                      
REMARK 465     PRO B   120                                                      
REMARK 465     GLU B   121                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     ASP B   123                                                      
REMARK 465     ASN B   377                                                      
REMARK 465     SER B   378                                                      
REMARK 465     LYS B   379                                                      
REMARK 465     THR B   380                                                      
REMARK 465     GLY C   646                                                      
REMARK 465     LYS C   647                                                      
REMARK 465     THR C   648                                                      
REMARK 465     SER C   649                                                      
REMARK 465     GLU C   650                                                      
REMARK 465     ASP C   651                                                      
REMARK 465     GLN C   652                                                      
REMARK 465     GLN C   653                                                      
REMARK 465     THR C   654                                                      
REMARK 465     ALA C   655                                                      
REMARK 465     CYS C   656                                                      
REMARK 465     GLY C   657                                                      
REMARK 465     THR C   658                                                      
REMARK 465     ILE C   659                                                      
REMARK 465     TYR C   660                                                      
REMARK 465     SER C   661                                                      
REMARK 465     GLN C   662                                                      
REMARK 465     THR C   663                                                      
REMARK 465     LEU C   664                                                      
REMARK 465     SER C   665                                                      
REMARK 465     ILE C   666                                                      
REMARK 465     LYS C   667                                                      
REMARK 465     ASP C   676                                                      
REMARK 465     ARG C   677                                                      
REMARK 465     GLU C   678                                                      
REMARK 465     ALA C   679                                                      
REMARK 465     ASP C   680                                                      
REMARK 465     HIS C   681                                                      
REMARK 465     SER C   682                                                      
REMARK 465     SER C   683                                                      
REMARK 465     GLY C   684                                                      
REMARK 465     PHE C   685                                                      
REMARK 465     SER C   686                                                      
REMARK 465     GLY C   687                                                      
REMARK 465     SER C   688                                                      
REMARK 465     SER C   689                                                      
REMARK 465     ALA C   690                                                      
REMARK 465     SER C   691                                                      
REMARK 465     VAL C   692                                                      
REMARK 465     ALA C   693                                                      
REMARK 465     SER C   694                                                      
REMARK 465     THR C   695                                                      
REMARK 465     SER C   696                                                      
REMARK 465     SER C   697                                                      
REMARK 465     ILE C   698                                                      
REMARK 465     LYS C   699                                                      
REMARK 465     CYS C   700                                                      
REMARK 465     LEU C   701                                                      
REMARK 465     GLN C   702                                                      
REMARK 465     ILE C   703                                                      
REMARK 465     PRO C   704                                                      
REMARK 465     GLU C   705                                                      
REMARK 465     LYS C   706                                                      
REMARK 465     LEU C   707                                                      
REMARK 465     GLU C   708                                                      
REMARK 465     LEU C   709                                                      
REMARK 465     THR C   710                                                      
REMARK 465     ASN C   711                                                      
REMARK 465     GLU C   712                                                      
REMARK 465     THR C   713                                                      
REMARK 465     SER C   714                                                      
REMARK 465     GLU C   715                                                      
REMARK 465     ASN C   716                                                      
REMARK 465     PRO C   717                                                      
REMARK 465     THR C   718                                                      
REMARK 465     GLN C   719                                                      
REMARK 465     SER C   720                                                      
REMARK 465     GLY D   646                                                      
REMARK 465     LYS D   647                                                      
REMARK 465     THR D   648                                                      
REMARK 465     SER D   649                                                      
REMARK 465     GLU D   650                                                      
REMARK 465     ASP D   651                                                      
REMARK 465     GLN D   652                                                      
REMARK 465     GLN D   653                                                      
REMARK 465     THR D   654                                                      
REMARK 465     ALA D   655                                                      
REMARK 465     CYS D   656                                                      
REMARK 465     GLY D   657                                                      
REMARK 465     THR D   658                                                      
REMARK 465     ILE D   659                                                      
REMARK 465     TYR D   660                                                      
REMARK 465     SER D   661                                                      
REMARK 465     GLN D   662                                                      
REMARK 465     THR D   663                                                      
REMARK 465     LEU D   664                                                      
REMARK 465     SER D   665                                                      
REMARK 465     ILE D   666                                                      
REMARK 465     LYS D   667                                                      
REMARK 465     ASP D   676                                                      
REMARK 465     ARG D   677                                                      
REMARK 465     GLU D   678                                                      
REMARK 465     ALA D   679                                                      
REMARK 465     ASP D   680                                                      
REMARK 465     HIS D   681                                                      
REMARK 465     SER D   682                                                      
REMARK 465     SER D   683                                                      
REMARK 465     GLY D   684                                                      
REMARK 465     PHE D   685                                                      
REMARK 465     SER D   686                                                      
REMARK 465     GLY D   687                                                      
REMARK 465     SER D   688                                                      
REMARK 465     SER D   689                                                      
REMARK 465     ALA D   690                                                      
REMARK 465     SER D   691                                                      
REMARK 465     VAL D   692                                                      
REMARK 465     ALA D   693                                                      
REMARK 465     SER D   694                                                      
REMARK 465     THR D   695                                                      
REMARK 465     SER D   696                                                      
REMARK 465     SER D   697                                                      
REMARK 465     ILE D   698                                                      
REMARK 465     LYS D   699                                                      
REMARK 465     CYS D   700                                                      
REMARK 465     LEU D   701                                                      
REMARK 465     GLN D   702                                                      
REMARK 465     ILE D   703                                                      
REMARK 465     PRO D   704                                                      
REMARK 465     GLU D   705                                                      
REMARK 465     LYS D   706                                                      
REMARK 465     LEU D   707                                                      
REMARK 465     GLU D   708                                                      
REMARK 465     LEU D   709                                                      
REMARK 465     THR D   710                                                      
REMARK 465     ASN D   711                                                      
REMARK 465     GLU D   712                                                      
REMARK 465     THR D   713                                                      
REMARK 465     SER D   714                                                      
REMARK 465     GLU D   715                                                      
REMARK 465     ASN D   716                                                      
REMARK 465     PRO D   717                                                      
REMARK 465     THR D   718                                                      
REMARK 465     GLN D   719                                                      
REMARK 465     SER D   720                                                      
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    GLU A 214      -72.01   -125.78                                   
REMARK 500    GLU B 214      -66.25   -121.38                                   
REMARK 500    ASN B 362       34.33   -143.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5JJA A   30   380  UNP    Q13362   2A5G_HUMAN      30    380             
DBREF  5JJA B   30   380  UNP    Q13362   2A5G_HUMAN      30    380             
DBREF  5JJA C  647   720  UNP    O60566   BUB1B_HUMAN    661    734             
DBREF  5JJA D  647   720  UNP    O60566   BUB1B_HUMAN    661    734             
SEQADV 5JJA GLY A   29  UNP  Q13362              EXPRESSION TAG                 
SEQADV 5JJA GLY B   29  UNP  Q13362              EXPRESSION TAG                 
SEQADV 5JJA GLY C  646  UNP  O60566              EXPRESSION TAG                 
SEQADV 5JJA ASP C  670  UNP  O60566    SER   684 ENGINEERED MUTATION            
SEQADV 5JJA ASP C  676  UNP  O60566    SER   690 ENGINEERED MUTATION            
SEQADV 5JJA ASP C  680  UNP  O60566    THR   694 ENGINEERED MUTATION            
SEQADV 5JJA GLY D  646  UNP  O60566              EXPRESSION TAG                 
SEQADV 5JJA ASP D  670  UNP  O60566    SER   684 ENGINEERED MUTATION            
SEQADV 5JJA ASP D  676  UNP  O60566    SER   690 ENGINEERED MUTATION            
SEQADV 5JJA ASP D  680  UNP  O60566    THR   694 ENGINEERED MUTATION            
SEQRES   1 A  352  GLY ILE ARG ASP VAL PRO PRO ALA ASP GLN GLU LYS LEU          
SEQRES   2 A  352  PHE ILE GLN LYS LEU ARG GLN CYS CYS VAL LEU PHE ASP          
SEQRES   3 A  352  PHE VAL SER ASP PRO LEU SER ASP LEU LYS TRP LYS GLU          
SEQRES   4 A  352  VAL LYS ARG ALA ALA LEU SER GLU MET VAL GLU TYR ILE          
SEQRES   5 A  352  THR HIS ASN ARG ASN VAL ILE THR GLU PRO ILE TYR PRO          
SEQRES   6 A  352  GLU VAL VAL HIS MET PHE ALA VAL ASN MET PHE ARG THR          
SEQRES   7 A  352  LEU PRO PRO SER SER ASN PRO THR GLY ALA GLU PHE ASP          
SEQRES   8 A  352  PRO GLU GLU ASP GLU PRO THR LEU GLU ALA ALA TRP PRO          
SEQRES   9 A  352  HIS LEU GLN LEU VAL TYR GLU PHE PHE LEU ARG PHE LEU          
SEQRES  10 A  352  GLU SER PRO ASP PHE GLN PRO ASN ILE ALA LYS LYS TYR          
SEQRES  11 A  352  ILE ASP GLN LYS PHE VAL LEU GLN LEU LEU GLU LEU PHE          
SEQRES  12 A  352  ASP SER GLU ASP PRO ARG GLU ARG ASP PHE LEU LYS THR          
SEQRES  13 A  352  THR LEU HIS ARG ILE TYR GLY LYS PHE LEU GLY LEU ARG          
SEQRES  14 A  352  ALA TYR ILE ARG LYS GLN ILE ASN ASN ILE PHE TYR ARG          
SEQRES  15 A  352  PHE ILE TYR GLU THR GLU HIS HIS ASN GLY ILE ALA GLU          
SEQRES  16 A  352  LEU LEU GLU ILE LEU GLY SER ILE ILE ASN GLY PHE ALA          
SEQRES  17 A  352  LEU PRO LEU LYS GLU GLU HIS LYS ILE PHE LEU LEU LYS          
SEQRES  18 A  352  VAL LEU LEU PRO LEU HIS LYS VAL LYS SER LEU SER VAL          
SEQRES  19 A  352  TYR HIS PRO GLN LEU ALA TYR CYS VAL VAL GLN PHE LEU          
SEQRES  20 A  352  GLU LYS ASP SER THR LEU THR GLU PRO VAL VAL MET ALA          
SEQRES  21 A  352  LEU LEU LYS TYR TRP PRO LYS THR HIS SER PRO LYS GLU          
SEQRES  22 A  352  VAL MET PHE LEU ASN GLU LEU GLU GLU ILE LEU ASP VAL          
SEQRES  23 A  352  ILE GLU PRO SER GLU PHE VAL LYS ILE MET GLU PRO LEU          
SEQRES  24 A  352  PHE ARG GLN LEU ALA LYS CYS VAL SER SER PRO HIS PHE          
SEQRES  25 A  352  GLN VAL ALA GLU ARG ALA LEU TYR TYR TRP ASN ASN GLU          
SEQRES  26 A  352  TYR ILE MET SER LEU ILE SER ASP ASN ALA ALA LYS ILE          
SEQRES  27 A  352  LEU PRO ILE MET PHE PRO SER LEU TYR ARG ASN SER LYS          
SEQRES  28 A  352  THR                                                          
SEQRES   1 B  352  GLY ILE ARG ASP VAL PRO PRO ALA ASP GLN GLU LYS LEU          
SEQRES   2 B  352  PHE ILE GLN LYS LEU ARG GLN CYS CYS VAL LEU PHE ASP          
SEQRES   3 B  352  PHE VAL SER ASP PRO LEU SER ASP LEU LYS TRP LYS GLU          
SEQRES   4 B  352  VAL LYS ARG ALA ALA LEU SER GLU MET VAL GLU TYR ILE          
SEQRES   5 B  352  THR HIS ASN ARG ASN VAL ILE THR GLU PRO ILE TYR PRO          
SEQRES   6 B  352  GLU VAL VAL HIS MET PHE ALA VAL ASN MET PHE ARG THR          
SEQRES   7 B  352  LEU PRO PRO SER SER ASN PRO THR GLY ALA GLU PHE ASP          
SEQRES   8 B  352  PRO GLU GLU ASP GLU PRO THR LEU GLU ALA ALA TRP PRO          
SEQRES   9 B  352  HIS LEU GLN LEU VAL TYR GLU PHE PHE LEU ARG PHE LEU          
SEQRES  10 B  352  GLU SER PRO ASP PHE GLN PRO ASN ILE ALA LYS LYS TYR          
SEQRES  11 B  352  ILE ASP GLN LYS PHE VAL LEU GLN LEU LEU GLU LEU PHE          
SEQRES  12 B  352  ASP SER GLU ASP PRO ARG GLU ARG ASP PHE LEU LYS THR          
SEQRES  13 B  352  THR LEU HIS ARG ILE TYR GLY LYS PHE LEU GLY LEU ARG          
SEQRES  14 B  352  ALA TYR ILE ARG LYS GLN ILE ASN ASN ILE PHE TYR ARG          
SEQRES  15 B  352  PHE ILE TYR GLU THR GLU HIS HIS ASN GLY ILE ALA GLU          
SEQRES  16 B  352  LEU LEU GLU ILE LEU GLY SER ILE ILE ASN GLY PHE ALA          
SEQRES  17 B  352  LEU PRO LEU LYS GLU GLU HIS LYS ILE PHE LEU LEU LYS          
SEQRES  18 B  352  VAL LEU LEU PRO LEU HIS LYS VAL LYS SER LEU SER VAL          
SEQRES  19 B  352  TYR HIS PRO GLN LEU ALA TYR CYS VAL VAL GLN PHE LEU          
SEQRES  20 B  352  GLU LYS ASP SER THR LEU THR GLU PRO VAL VAL MET ALA          
SEQRES  21 B  352  LEU LEU LYS TYR TRP PRO LYS THR HIS SER PRO LYS GLU          
SEQRES  22 B  352  VAL MET PHE LEU ASN GLU LEU GLU GLU ILE LEU ASP VAL          
SEQRES  23 B  352  ILE GLU PRO SER GLU PHE VAL LYS ILE MET GLU PRO LEU          
SEQRES  24 B  352  PHE ARG GLN LEU ALA LYS CYS VAL SER SER PRO HIS PHE          
SEQRES  25 B  352  GLN VAL ALA GLU ARG ALA LEU TYR TYR TRP ASN ASN GLU          
SEQRES  26 B  352  TYR ILE MET SER LEU ILE SER ASP ASN ALA ALA LYS ILE          
SEQRES  27 B  352  LEU PRO ILE MET PHE PRO SER LEU TYR ARG ASN SER LYS          
SEQRES  28 B  352  THR                                                          
SEQRES   1 C   75  GLY LYS THR SER GLU ASP GLN GLN THR ALA CYS GLY THR          
SEQRES   2 C   75  ILE TYR SER GLN THR LEU SER ILE LYS LYS LEU ASP PRO          
SEQRES   3 C   75  ILE ILE GLU ASP ASP ARG GLU ALA ASP HIS SER SER GLY          
SEQRES   4 C   75  PHE SER GLY SER SER ALA SER VAL ALA SER THR SER SER          
SEQRES   5 C   75  ILE LYS CYS LEU GLN ILE PRO GLU LYS LEU GLU LEU THR          
SEQRES   6 C   75  ASN GLU THR SER GLU ASN PRO THR GLN SER                      
SEQRES   1 D   75  GLY LYS THR SER GLU ASP GLN GLN THR ALA CYS GLY THR          
SEQRES   2 D   75  ILE TYR SER GLN THR LEU SER ILE LYS LYS LEU ASP PRO          
SEQRES   3 D   75  ILE ILE GLU ASP ASP ARG GLU ALA ASP HIS SER SER GLY          
SEQRES   4 D   75  PHE SER GLY SER SER ALA SER VAL ALA SER THR SER SER          
SEQRES   5 D   75  ILE LYS CYS LEU GLN ILE PRO GLU LYS LEU GLU LEU THR          
SEQRES   6 D   75  ASN GLU THR SER GLU ASN PRO THR GLN SER                      
FORMUL   5  HOH   *240(H2 O)                                                    
HELIX    1 AA1 GLY A   29  VAL A   33  5                                   5    
HELIX    2 AA2 ASP A   37  CYS A   49  1                                  13    
HELIX    3 AA3 ASP A   62  ASN A   83  1                                  22    
HELIX    4 AA4 PRO A   90  PHE A  104  1                                  15    
HELIX    5 AA5 ALA A  130  SER A  147  1                                  18    
HELIX    6 AA6 GLN A  151  LYS A  156  1                                   6    
HELIX    7 AA7 ASP A  160  LEU A  170  1                                  11    
HELIX    8 AA8 PHE A  171  SER A  173  5                                   3    
HELIX    9 AA9 ASP A  175  PHE A  193  1                                  19    
HELIX   10 AB1 LEU A  196  GLU A  214  1                                  19    
HELIX   11 AB2 GLY A  220  GLY A  234  1                                  15    
HELIX   12 AB3 LYS A  240  VAL A  250  1                                  11    
HELIX   13 AB4 LEU A  252  VAL A  257  5                                   6    
HELIX   14 AB5 SER A  259  VAL A  262  5                                   4    
HELIX   15 AB6 TYR A  263  ASP A  278  1                                  16    
HELIX   16 AB7 LEU A  281  TRP A  293  1                                  13    
HELIX   17 AB8 LYS A  300  VAL A  314  1                                  15    
HELIX   18 AB9 GLU A  316  SER A  336  1                                  21    
HELIX   19 AC1 HIS A  339  TYR A  348  1                                  10    
HELIX   20 AC2 TYR A  349  ASN A  351  5                                   3    
HELIX   21 AC3 ASN A  352  ASP A  361  1                                  10    
HELIX   22 AC4 ASN A  362  PHE A  371  1                                  10    
HELIX   23 AC5 PRO B   34  ALA B   36  5                                   3    
HELIX   24 AC6 ASP B   37  CYS B   49  1                                  13    
HELIX   25 AC7 ASP B   62  ASN B   83  1                                  22    
HELIX   26 AC8 PRO B   90  PHE B  104  1                                  15    
HELIX   27 AC9 ALA B  130  SER B  147  1                                  18    
HELIX   28 AD1 GLN B  151  LYS B  156  1                                   6    
HELIX   29 AD2 ASP B  160  LEU B  170  1                                  11    
HELIX   30 AD3 PHE B  171  SER B  173  5                                   3    
HELIX   31 AD4 ASP B  175  PHE B  193  1                                  19    
HELIX   32 AD5 LEU B  196  GLU B  214  1                                  19    
HELIX   33 AD6 GLY B  220  GLY B  234  1                                  15    
HELIX   34 AD7 LYS B  240  VAL B  250  1                                  11    
HELIX   35 AD8 LEU B  252  VAL B  257  5                                   6    
HELIX   36 AD9 SER B  259  ASP B  278  1                                  20    
HELIX   37 AE1 LEU B  281  TRP B  293  1                                  13    
HELIX   38 AE2 LYS B  300  VAL B  314  1                                  15    
HELIX   39 AE3 GLU B  316  SER B  336  1                                  21    
HELIX   40 AE4 HIS B  339  TYR B  348  1                                  10    
HELIX   41 AE5 TYR B  349  ASN B  351  5                                   3    
HELIX   42 AE6 ASN B  352  ASP B  361  1                                  10    
HELIX   43 AE7 ASN B  362  PHE B  371  1                                  10    
CISPEP   1 LEU A  237    PRO A  238          0         0.04                     
CISPEP   2 LEU B  237    PRO B  238          0        -3.65                     
CRYST1   87.017   95.588  167.372  90.00  90.00  90.00 P 21 21 21    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      0.011492  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010462  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005975        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system