GenomeNet

Database: PDB
Entry: 3Q9X
LinkDB: 3Q9X
Original site: 3Q9X 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       10-JAN-11   3Q9X              
TITLE     CRYSTAL STRUCTURE OF HUMAN CK2 ALPHA IN COMPLEX WITH EMODIN AT PH 6.5 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-336;                                        
COMPND   5 SYNONYM: CK2ALPHA, CK II ALPHA;                                      
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CSNK2A1, CK2A1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7-7                                     
KEYWDS    PROTEIN KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.BATTISTUTTA,A.RANCHIO,E.PAPINUTTO                                   
REVDAT   1   11-JAN-12 3Q9X    0                                                
JRNL        AUTH   E.PAPINUTTO,A.RANCHIO,G.LOLLI,L.A.PINNA,R.BATTISTUTTA        
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE FLEXIBLE REGIONS   
JRNL        TITL 2 OF THE CATALYTIC ALPHA-SUBUNIT OF PROTEIN KINASE CK2         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.32                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 44560                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2294                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2977                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 163                          
REMARK   3   BIN FREE R VALUE                    : 0.3430                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5576                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 111                                     
REMARK   3   SOLVENT ATOMS            : 247                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.39000                                              
REMARK   3    B22 (A**2) : 0.39000                                              
REMARK   3    B33 (A**2) : -0.79000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.217         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.128         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.240        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5858 ; 0.023 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7925 ; 1.959 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   664 ; 6.089 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   314 ;35.819 ;23.089       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1021 ;17.727 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    51 ;23.958 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   807 ; 0.141 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4503 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3313 ; 0.898 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5391 ; 1.649 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2545 ; 2.885 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2533 ; 4.556 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 6                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      4       A      31      2                      
REMARK   3           1     B      4       B      31      2                      
REMARK   3           2     A     33       A     100      2                      
REMARK   3           2     B     33       B     100      2                      
REMARK   3           3     A    129       A     159      2                      
REMARK   3           3     B    129       B     159      2                      
REMARK   3           4     A    161       A     174      2                      
REMARK   3           4     B    161       B     174      2                      
REMARK   3           5     A    176       A     229      2                      
REMARK   3           5     B    176       B     229      2                      
REMARK   3           6     A    241       A     329      2                      
REMARK   3           6     B    241       B     329      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1128 ; 0.080 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1261 ; 0.210 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1128 ; 0.230 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1261 ; 0.280 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
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     2        A    36                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3648  45.6280   4.4510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1167 T22:   0.0747                                     
REMARK   3      T33:   0.0838 T12:  -0.0173                                     
REMARK   3      T13:   0.0000 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2202 L22:   0.8718                                     
REMARK   3      L33:   1.0446 L12:  -0.3281                                     
REMARK   3      L13:  -0.0231 L23:  -0.0001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0302 S12:   0.1506 S13:   0.1399                       
REMARK   3      S21:  -0.0289 S22:  -0.0417 S23:  -0.0282                       
REMARK   3      S31:  -0.0868 S32:   0.0190 S33:   0.0114                       
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 :   A    37        A    77                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7205  52.3162  22.2146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1812 T22:   0.1224                                     
REMARK   3      T33:   0.1654 T12:   0.0370                                     
REMARK   3      T13:  -0.0076 T23:  -0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0976 L22:   1.7275                                     
REMARK   3      L33:   3.6847 L12:  -0.0674                                     
REMARK   3      L13:  -1.3405 L23:  -0.9472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0080 S12:  -0.1200 S13:  -0.0189                       
REMARK   3      S21:   0.0242 S22:  -0.0166 S23:  -0.0199                       
REMARK   3      S31:  -0.0468 S32:   0.0561 S33:   0.0085                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    78        A   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1742  49.1006  13.8651              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1072 T22:   0.1247                                     
REMARK   3      T33:   0.1210 T12:  -0.0042                                     
REMARK   3      T13:  -0.0249 T23:  -0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7862 L22:   0.1917                                     
REMARK   3      L33:   1.7640 L12:   0.1382                                     
REMARK   3      L13:  -0.1209 L23:  -0.4295                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0251 S12:  -0.0162 S13:   0.1996                       
REMARK   3      S21:   0.0036 S22:   0.0039 S23:   0.0976                       
REMARK   3      S31:  -0.1968 S32:  -0.1829 S33:  -0.0290                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   113        A   125                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6545  40.5698  31.3921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2755 T22:   0.2879                                     
REMARK   3      T33:   0.2286 T12:  -0.0221                                     
REMARK   3      T13:  -0.0379 T23:   0.0586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6406 L22:   0.9087                                     
REMARK   3      L33:   2.6855 L12:  -0.5166                                     
REMARK   3      L13:   1.0603 L23:  -1.3561                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0486 S12:  -0.3110 S13:  -0.1682                       
REMARK   3      S21:   0.1574 S22:   0.0851 S23:  -0.0177                       
REMARK   3      S31:   0.1565 S32:  -0.2097 S33:  -0.1336                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   126        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2242  34.9990  24.7379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1054 T22:   0.1042                                     
REMARK   3      T33:   0.1090 T12:  -0.0074                                     
REMARK   3      T13:   0.0063 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9843 L22:   1.7879                                     
REMARK   3      L33:   0.8493 L12:   0.2000                                     
REMARK   3      L13:   0.1458 L23:  -0.7594                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0152 S12:  -0.2356 S13:  -0.0521                       
REMARK   3      S21:   0.2765 S22:   0.0219 S23:   0.2008                       
REMARK   3      S31:   0.0040 S32:  -0.1861 S33:  -0.0371                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   168        A   243                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5171  44.7976  23.1888              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1084 T22:   0.0876                                     
REMARK   3      T33:   0.1188 T12:   0.0086                                     
REMARK   3      T13:   0.0034 T23:  -0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1528 L22:   0.6356                                     
REMARK   3      L33:   1.7920 L12:  -0.3419                                     
REMARK   3      L13:   0.4462 L23:   0.1181                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0103 S12:  -0.1562 S13:   0.0596                       
REMARK   3      S21:   0.1405 S22:  -0.0206 S23:   0.0036                       
REMARK   3      S31:  -0.1029 S32:   0.0597 S33:   0.0104                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   244        A   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4225  36.3615  27.3169              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1075 T22:   0.1267                                     
REMARK   3      T33:   0.1336 T12:   0.0519                                     
REMARK   3      T13:  -0.0006 T23:  -0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4618 L22:   1.4043                                     
REMARK   3      L33:   2.0105 L12:   0.2415                                     
REMARK   3      L13:  -0.1344 L23:  -0.2662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0399 S12:  -0.0796 S13:   0.1066                       
REMARK   3      S21:   0.1020 S22:  -0.0424 S23:  -0.0346                       
REMARK   3      S31:  -0.1122 S32:   0.1227 S33:   0.0024                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B     9                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.8029  36.0562 -21.5614              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2722 T22:   0.2856                                     
REMARK   3      T33:   0.2206 T12:   0.0306                                     
REMARK   3      T13:   0.0305 T23:   0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8422 L22:   8.8081                                     
REMARK   3      L33:   2.0143 L12:  -6.4562                                     
REMARK   3      L13:  -2.1147 L23:   2.7301                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1958 S12:   0.3836 S13:  -0.0326                       
REMARK   3      S21:  -0.2822 S22:  -0.2575 S23:  -0.3499                       
REMARK   3      S31:   0.2938 S32:   0.3362 S33:   0.0617                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    10        B   113                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8818  68.2136 -14.9317              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0961 T22:   0.0985                                     
REMARK   3      T33:   0.0918 T12:   0.0135                                     
REMARK   3      T13:   0.0003 T23:   0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9970 L22:   1.5371                                     
REMARK   3      L33:   1.2369 L12:   0.5605                                     
REMARK   3      L13:   0.2556 L23:   0.9571                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0066 S12:  -0.0476 S13:   0.0633                       
REMARK   3      S21:  -0.0007 S22:   0.0443 S23:  -0.1605                       
REMARK   3      S31:  -0.1082 S32:   0.1613 S33:  -0.0509                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   114        B   127                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.4839  64.9419   2.4182              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3819 T22:   0.3880                                     
REMARK   3      T33:   0.3950 T12:   0.0031                                     
REMARK   3      T13:  -0.0017 T23:   0.1166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2540 L22:   0.1364                                     
REMARK   3      L33:   0.1566 L12:   0.1124                                     
REMARK   3      L13:  -0.1017 L23:   0.0552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0039 S12:  -0.2497 S13:  -0.2582                       
REMARK   3      S21:   0.1836 S22:  -0.1047 S23:  -0.1155                       
REMARK   3      S31:   0.2087 S32:   0.1077 S33:   0.1008                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   128        B   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.0700  58.2095  -6.6057              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1045 T22:   0.1037                                     
REMARK   3      T33:   0.1061 T12:   0.0027                                     
REMARK   3      T13:  -0.0145 T23:  -0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9407 L22:   0.7847                                     
REMARK   3      L33:   0.8548 L12:  -0.2488                                     
REMARK   3      L13:  -0.7179 L23:  -0.1813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0222 S12:  -0.2541 S13:   0.2199                       
REMARK   3      S21:   0.1959 S22:   0.0182 S23:   0.0645                       
REMARK   3      S31:  -0.1964 S32:  -0.0366 S33:  -0.0405                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   168        B   221                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.6843  50.3292 -10.7156              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0833 T22:   0.1118                                     
REMARK   3      T33:   0.1073 T12:  -0.0143                                     
REMARK   3      T13:  -0.0074 T23:   0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6346 L22:   1.5146                                     
REMARK   3      L33:   1.9918 L12:   0.5135                                     
REMARK   3      L13:   0.2302 L23:  -0.1910                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0185 S12:  -0.0939 S13:   0.0118                       
REMARK   3      S21:   0.1024 S22:   0.0198 S23:  -0.0699                       
REMARK   3      S31:   0.0535 S32:   0.0842 S33:  -0.0013                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   222        B   258                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6178  40.2759   1.6674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1516 T22:   0.1444                                     
REMARK   3      T33:   0.1291 T12:  -0.0116                                     
REMARK   3      T13:   0.0027 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6173 L22:   0.9741                                     
REMARK   3      L33:   0.7961 L12:  -0.8025                                     
REMARK   3      L13:  -0.1014 L23:  -0.2793                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0408 S12:  -0.1710 S13:   0.1151                       
REMARK   3      S21:   0.1510 S22:   0.0848 S23:  -0.1707                       
REMARK   3      S31:   0.0112 S32:   0.1253 S33:  -0.0441                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   259        B   331                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.3690  41.4535  -2.9725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1289 T22:   0.0984                                     
REMARK   3      T33:   0.1299 T12:  -0.0541                                     
REMARK   3      T13:  -0.0108 T23:  -0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4772 L22:   1.3398                                     
REMARK   3      L33:   2.0110 L12:  -0.1576                                     
REMARK   3      L13:  -0.3842 L23:   0.1174                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0453 S12:  -0.1145 S13:  -0.0293                       
REMARK   3      S21:   0.0887 S22:   0.0418 S23:  -0.0717                       
REMARK   3      S31:   0.0889 S32:   0.0555 S33:   0.0035                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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                                                  
REMARK   4                                                                      
REMARK   4 3Q9X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063378.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.972937                           
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44592                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.320                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.5                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : 0.08600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.58300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
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: PDB ENTRY 2PVR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 5000 MME, 0.2M AMMONIUM          
REMARK 280  SULFATE, 0.1M MES, PH 6.5, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.29850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       64.00500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       64.00500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       93.44775            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       64.00500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       64.00500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.14925            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       64.00500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       64.00500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       93.44775            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       64.00500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       64.00500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.14925            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       62.29850            
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: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A   332                                                      
REMARK 465     ARG A   333                                                      
REMARK 465     MET A   334                                                      
REMARK 465     GLY A   335                                                      
REMARK 465     SER A   336                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   332                                                      
REMARK 465     ARG B   333                                                      
REMARK 465     MET B   334                                                      
REMARK 465     GLY B   335                                                      
REMARK 465     SER B   336                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER B    28     O    HOH B   397              1.96            
REMARK 500   NE2  GLN A    36     CD   PRO A   104              2.03            
REMARK 500   NH1  ARG B   107     O4   SO4 B   341              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU A   296     OE2  GLU B   296     6555     2.07            
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    TYR A  26   CZ    TYR A  26   CE2    -0.081                       
REMARK 500    TYR A  39   CE1   TYR A  39   CZ     -0.095                       
REMARK 500    TYR A  39   CZ    TYR A  39   CE2    -0.082                       
REMARK 500    GLU A 114   CB    GLU A 114   CG      0.145                       
REMARK 500    TYR B  39   CE1   TYR B  39   CZ     -0.093                       
REMARK 500    GLU B 114   CB    GLU B 114   CG      0.142                       
REMARK 500    TYR B 211   CG    TYR B 211   CD2    -0.083                       
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    ARG A  10   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    CYS A 147   CA  -  CB  -  SG  ANGL. DEV. =   6.6 DEGREES          
REMARK 500    GLU A 180   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ASP A 210   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A 278   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 278   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A 280   CD  -  NE  -  CZ  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ARG A 280   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG A 280   NE  -  CZ  -  NH2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A 312   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 316   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG B  10   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B  89   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    GLU B 180   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    ASP B 210   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG B 278   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 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    ASN A  62       19.25     59.01                                   
REMARK 500    VAL A 105      -69.18    -92.79                                   
REMARK 500    ARG A 107       15.67     56.78                                   
REMARK 500    GLU A 114      136.89    -38.04                                   
REMARK 500    ASN A 117       69.89   -109.86                                   
REMARK 500    ASP A 156       47.28   -150.93                                   
REMARK 500    ASP A 175       74.84     51.33                                   
REMARK 500    ALA A 193      161.17     62.65                                   
REMARK 500    ASP B 103      108.72    -57.51                                   
REMARK 500    GLU B 114      134.71    -35.15                                   
REMARK 500    ASN B 118       65.38    -69.21                                   
REMARK 500    TYR B 125       45.24    -76.75                                   
REMARK 500    GLN B 126        8.54   -155.56                                   
REMARK 500    ASP B 156       42.60   -145.03                                   
REMARK 500    ALA B 193      155.89     75.61                                   
REMARK 500    ASP B 210     -157.91   -148.10                                   
REMARK 500    ASP B 237     -177.58   -174.38                                   
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    THR A  17        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 175        23.2      L          L   OUTSIDE RANGE           
REMARK 500    ARG B  10        24.1      L          L   OUTSIDE RANGE           
REMARK 500    THR B  17        22.6      L          L   OUTSIDE RANGE           
REMARK 500    TYR B 125        21.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 328        23.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMO A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 337                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7PE A 338                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 339                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 340                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 341                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMO B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 337                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 338                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 339                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 340                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 341                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 342                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3Q9W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3Q9Y   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3Q9Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3QA0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PZH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P04   RELATED DB: PDB                                   
DBREF  3Q9X A    1   336  UNP    P68400   CSK21_HUMAN      1    336             
DBREF  3Q9X B    1   336  UNP    P68400   CSK21_HUMAN      1    336             
SEQRES   1 A  336  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 A  336  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 A  336  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 A  336  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 A  336  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 A  336  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 A  336  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 A  336  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 A  336  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 A  336  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 A  336  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 A  336  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 A  336  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 A  336  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 A  336  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 A  336  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 A  336  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 A  336  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 A  336  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 A  336  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 A  336  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 A  336  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 A  336  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 A  336  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 A  336  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 A  336  THR VAL VAL LYS ASP GLN ALA ARG MET GLY SER                  
SEQRES   1 B  336  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 B  336  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 B  336  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 B  336  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 B  336  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 B  336  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 B  336  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 B  336  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 B  336  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 B  336  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 B  336  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 B  336  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 B  336  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 B  336  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 B  336  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 B  336  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 B  336  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 B  336  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 B  336  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 B  336  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 B  336  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 B  336  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 B  336  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 B  336  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 B  336  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 B  336  THR VAL VAL LYS ASP GLN ALA ARG MET GLY SER                  
HET    EMO  A 400      20                                                       
HET    EDO  A 337       4                                                       
HET    7PE  A 338      21                                                       
HET    SO4  A 339       5                                                       
HET    SO4  A 340       5                                                       
HET    SO4  A 341       5                                                       
HET    EMO  B 401      20                                                       
HET    PEG  B 337       7                                                       
HET    EDO  B 338       4                                                       
HET    SO4  B 339       5                                                       
HET    SO4  B 340       5                                                       
HET    SO4  B 341       5                                                       
HET    SO4  B 342       5                                                       
HETNAM     EMO 3-METHYL-1,6,8-TRIHYDROXYANTHRAQUINONE                           
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     7PE 2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)              
HETNAM   2 7PE  ETHOXY)ETHANOL                                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     EMO EMODIN                                                           
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     7PE POLYETHYLENE GLYCOL FRAGMENT                                     
FORMUL   3  EMO    2(C15 H10 O5)                                                
FORMUL   4  EDO    2(C2 H6 O2)                                                  
FORMUL   5  7PE    C14 H30 O7                                                   
FORMUL   6  SO4    7(O4 S 2-)                                                   
FORMUL  10  PEG    C4 H10 O3                                                    
FORMUL  16  HOH   *247(H2 O)                                                    
HELIX    1   1 VAL A   15  ARG A   19  5                                   5    
HELIX    2   2 PRO A   20  ASP A   25  1                                   6    
HELIX    3   3 TYR A   26  HIS A   29  5                                   4    
HELIX    4   4 ASN A   35  ASP A   37  5                                   3    
HELIX    5   5 LYS A   74  ARG A   89  1                                  16    
HELIX    6   6 ASP A  120  TYR A  125  1                                   6    
HELIX    7   7 THR A  129  MET A  150  1                                  22    
HELIX    8   8 LYS A  158  HIS A  160  5                                   3    
HELIX    9   9 SER A  194  LYS A  198  5                                   5    
HELIX   10  10 GLY A  199  VAL A  204  1                                   6    
HELIX   11  11 TYR A  211  ARG A  228  1                                  18    
HELIX   12  12 ASP A  237  GLY A  250  1                                  14    
HELIX   13  13 THR A  251  ASN A  262  1                                  12    
HELIX   14  14 ASP A  266  ARG A  268  5                                   3    
HELIX   15  15 PHE A  269  GLY A  274  1                                   6    
HELIX   16  16 ARG A  280  VAL A  285  5                                   6    
HELIX   17  17 ASN A  289  VAL A  293  5                                   5    
HELIX   18  18 SER A  294  LEU A  305  1                                  12    
HELIX   19  19 ASP A  308  ARG A  312  5                                   5    
HELIX   20  20 THR A  314  GLU A  320  1                                   7    
HELIX   21  21 HIS A  321  TYR A  323  5                                   3    
HELIX   22  22 PHE A  324  GLN A  331  1                                   8    
HELIX   23  23 PRO B   20  ASP B   25  1                                   6    
HELIX   24  24 TYR B   26  HIS B   29  5                                   4    
HELIX   25  25 ASN B   35  ASP B   37  5                                   3    
HELIX   26  26 LYS B   74  ARG B   89  1                                  16    
HELIX   27  27 ASP B  120  TYR B  125  1                                   6    
HELIX   28  28 THR B  129  MET B  150  1                                  22    
HELIX   29  29 LYS B  158  HIS B  160  5                                   3    
HELIX   30  30 SER B  194  LYS B  198  5                                   5    
HELIX   31  31 GLY B  199  VAL B  204  1                                   6    
HELIX   32  32 TYR B  211  ARG B  228  1                                  18    
HELIX   33  33 ASP B  237  GLY B  250  1                                  14    
HELIX   34  34 THR B  251  ASN B  262  1                                  12    
HELIX   35  35 ASP B  266  ARG B  268  5                                   3    
HELIX   36  36 PHE B  269  GLY B  274  1                                   6    
HELIX   37  37 ARG B  280  VAL B  285  5                                   6    
HELIX   38  38 ASN B  289  VAL B  293  5                                   5    
HELIX   39  39 SER B  294  LEU B  305  1                                  12    
HELIX   40  40 ASP B  308  ARG B  312  5                                   5    
HELIX   41  41 THR B  314  GLU B  320  1                                   7    
HELIX   42  42 HIS B  321  TYR B  323  5                                   3    
HELIX   43  43 PHE B  324  GLN B  331  1                                   8    
SHEET    1   A 5 TYR A  39  ARG A  47  0                                        
SHEET    2   A 5 SER A  51  ASN A  58 -1  O  GLU A  55   N  VAL A  42           
SHEET    3   A 5 GLU A  63  LEU A  70 -1  O  GLU A  63   N  ASN A  58           
SHEET    4   A 5 PRO A 109  GLU A 114 -1  O  LEU A 111   N  LYS A  68           
SHEET    5   A 5 LEU A  97  LYS A 102 -1  N  ALA A  98   O  VAL A 112           
SHEET    1   B 2 ILE A 152  MET A 153  0                                        
SHEET    2   B 2 GLU A 180  PHE A 181 -1  O  GLU A 180   N  MET A 153           
SHEET    1   C 2 VAL A 162  ASP A 165  0                                        
SHEET    2   C 2 LYS A 170  LEU A 173 -1  O  LYS A 170   N  ASP A 165           
SHEET    1   D 5 TYR B  39  ARG B  47  0                                        
SHEET    2   D 5 SER B  51  ASN B  58 -1  O  GLU B  55   N  VAL B  42           
SHEET    3   D 5 GLU B  63  LEU B  70 -1  O  GLU B  63   N  ASN B  58           
SHEET    4   D 5 PRO B 109  GLU B 114 -1  O  PHE B 113   N  VAL B  66           
SHEET    5   D 5 LEU B  97  LYS B 102 -1  N  ALA B  98   O  VAL B 112           
SHEET    1   E 2 ILE B 152  MET B 153  0                                        
SHEET    2   E 2 GLU B 180  PHE B 181 -1  O  GLU B 180   N  MET B 153           
SHEET    1   F 2 VAL B 162  ASP B 165  0                                        
SHEET    2   F 2 LYS B 170  LEU B 173 -1  O  LYS B 170   N  ASP B 165           
CISPEP   1 GLU A  230    PRO A  231          0        -4.78                     
CISPEP   2 GLU B  230    PRO B  231          0        -8.05                     
SITE     1 AC1  8 VAL A  66  LYS A  68  ILE A  95  PHE A 113                    
SITE     2 AC1  8 HIS A 160  ILE A 174  ASP A 175  HOH A 347                    
SITE     1 AC2  5 TRP A  24  ASP A  25  TYR A  26  GLU A  27                    
SITE     2 AC2  5 LYS A  44                                                     
SITE     1 AC3 12 GLU A 252  ASP A 253  SER A 277  ARG A 278                    
SITE     2 AC3 12 ARG A 280  ARG A 283  HOH A 365  GLU B 252                    
SITE     3 AC3 12 ASP B 253  SER B 277  ARG B 278  ARG B 280                    
SITE     1 AC4  4 TRP A  33  LYS A  75  LYS A 102  HOH A 430                    
SITE     1 AC5  4 ARG A  80  ARG A 155  ASN A 189  HOH A 375                    
SITE     1 AC6  3 ARG A 191  LYS A 198  ASN A 238                               
SITE     1 AC7 11 VAL B  53  VAL B  66  LYS B  68  ILE B  95                    
SITE     2 AC7 11 PHE B 113  VAL B 116  ASN B 118  MET B 163                    
SITE     3 AC7 11 ILE B 174  ASP B 175  HOH B 357                               
SITE     1 AC8  6 GLN B  36  TYR B  39  VAL B 101  ASP B 103                    
SITE     2 AC8  6 THR B 108  ALA B 110                                          
SITE     1 AC9  2 HIS B 276  LYS B 279                                          
SITE     1 BC1  4 ARG B  80  ARG B 155  ASN B 189  HOH B 384                    
SITE     1 BC2  6 TRP B  33  LYS B  75  LYS B 102  HOH B 403                    
SITE     2 BC2  6 HOH B 437  HOH B 472                                          
SITE     1 BC3  4 LYS A  74  LYS B  75  LYS B 102  ARG B 107                    
SITE     1 BC4  3 ARG B 191  LYS B 198  ASN B 238                               
CRYST1  128.010  128.010  124.597  90.00  90.00  90.00 P 43 21 2    16          
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      0.007812  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007812  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008026        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system