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Database: PDB
Entry: 3Q9Y
LinkDB: 3Q9Y
Original site: 3Q9Y 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       10-JAN-11   3Q9Y              
TITLE     CRYSTAL STRUCTURE OF HUMAN CK2 ALPHA IN COMPLEX WITH QUINALIZARIN AT  
TITLE    2 PH 8.5                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;                            
COMPND   3 CHAIN: A;                                                            
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 3Q9Y    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.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 27519                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1406                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1654                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.4310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2765                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 224                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.71000                                             
REMARK   3    B22 (A**2) : 0.48000                                              
REMARK   3    B33 (A**2) : 0.54000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.41000                                              
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): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2898 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3930 ; 1.867 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   332 ; 6.283 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   157 ;33.995 ;23.057       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   509 ;16.538 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;22.316 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   402 ; 0.136 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2243 ; 0.011 ; 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):  1646 ; 1.150 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2680 ; 1.799 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1252 ; 2.965 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1248 ; 4.273 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
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     3        A    12                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6090  -8.1290  43.9030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0985 T22:   0.0137                                     
REMARK   3      T33:   0.1049 T12:  -0.0009                                     
REMARK   3      T13:   0.0154 T23:   0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7822 L22:   2.0579                                     
REMARK   3      L33:  14.8366 L12:  -2.3715                                     
REMARK   3      L13:  -5.6845 L23:   4.9512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1626 S12:  -0.0048 S13:  -0.1870                       
REMARK   3      S21:  -0.0232 S22:   0.0029 S23:   0.0446                       
REMARK   3      S31:   0.3488 S32:   0.0758 S33:   0.1597                       
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    13        A    31                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.2370  -9.7690  49.6650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1083 T22:   0.0584                                     
REMARK   3      T33:   0.1688 T12:  -0.0229                                     
REMARK   3      T13:  -0.0317 T23:   0.0446                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.0144 L22:   1.3162                                     
REMARK   3      L33:   1.3384 L12:  -1.8877                                     
REMARK   3      L13:   1.6912 L23:   0.0977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0406 S12:  -0.4345 S13:  -0.8570                       
REMARK   3      S21:  -0.0929 S22:   0.0522 S23:   0.4023                       
REMARK   3      S31:   0.2551 S32:  -0.0599 S33:  -0.0928                       
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    32        A    78                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.3790  12.0740  44.3920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0221 T22:   0.0794                                     
REMARK   3      T33:   0.0930 T12:   0.0051                                     
REMARK   3      T13:  -0.0301 T23:   0.0393                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6883 L22:   2.8427                                     
REMARK   3      L33:   2.3675 L12:   0.0234                                     
REMARK   3      L13:  -0.2039 L23:  -0.4182                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0404 S12:  -0.0570 S13:  -0.1100                       
REMARK   3      S21:  -0.0676 S22:  -0.0790 S23:  -0.1943                       
REMARK   3      S31:  -0.0296 S32:  -0.0322 S33:   0.0386                       
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    79        A   112                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0520   4.7830  47.8230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0601 T22:   0.1021                                     
REMARK   3      T33:   0.1086 T12:  -0.0169                                     
REMARK   3      T13:  -0.0072 T23:   0.0490                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9969 L22:   0.4791                                     
REMARK   3      L33:   0.5784 L12:  -0.8766                                     
REMARK   3      L13:   0.5939 L23:  -0.1558                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0307 S12:  -0.2151 S13:  -0.2707                       
REMARK   3      S21:  -0.0620 S22:   0.0899 S23:   0.1294                       
REMARK   3      S31:  -0.0506 S32:  -0.0699 S33:  -0.0592                       
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   113        A   129                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.2520  23.0000  47.4400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3518 T22:   0.3414                                     
REMARK   3      T33:   0.3333 T12:  -0.0987                                     
REMARK   3      T13:  -0.2433 T23:  -0.0930                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3726 L22:   0.3915                                     
REMARK   3      L33:   0.6975 L12:   0.5410                                     
REMARK   3      L13:  -1.1683 L23:  -0.1097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4345 S12:   0.1707 S13:   0.8888                       
REMARK   3      S21:  -0.3393 S22:   0.3349 S23:   0.1651                       
REMARK   3      S31:  -0.0333 S32:  -0.2925 S33:   0.0995                       
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   130        A   280                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4840   8.1380  39.5080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0925 T22:   0.0735                                     
REMARK   3      T33:   0.0796 T12:  -0.0038                                     
REMARK   3      T13:  -0.0154 T23:   0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9239 L22:   0.6665                                     
REMARK   3      L33:   0.6046 L12:   0.1399                                     
REMARK   3      L13:  -0.1364 L23:  -0.0433                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0215 S12:  -0.0299 S13:   0.0163                       
REMARK   3      S21:  -0.1004 S22:   0.0248 S23:   0.0699                       
REMARK   3      S31:  -0.0030 S32:  -0.0491 S33:  -0.0032                       
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   281        A   329                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3350  13.7990  48.5020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0716 T22:   0.0818                                     
REMARK   3      T33:   0.0844 T12:   0.0014                                     
REMARK   3      T13:  -0.0044 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4585 L22:   1.2974                                     
REMARK   3      L33:   1.0371 L12:   0.1892                                     
REMARK   3      L13:  -0.0899 L23:   0.1411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0453 S12:  -0.0824 S13:   0.0506                       
REMARK   3      S21:  -0.0050 S22:  -0.0183 S23:   0.0015                       
REMARK   3      S31:  -0.0683 S32:   0.0680 S33:  -0.0270                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES                                                  
REMARK   4                                                                      
REMARK   4 3Q9Y 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 RCSB063379.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27533                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.470                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : 0.09100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.50000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
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   (%): 37.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.2M LITHIUM SULFATE,      
REMARK 280  0.1M TRISHCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       22.95500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     GLN A   331                                                      
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 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  47   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP A 266   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 306   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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       24.77     41.12                                   
REMARK 500    PRO A  72       25.98    -74.95                                   
REMARK 500    LYS A  74       78.79     52.42                                   
REMARK 500    ASP A 156       45.55   -147.31                                   
REMARK 500    ASP A 175       66.64     61.90                                   
REMARK 500    ALA A 193      163.12     55.21                                   
REMARK 500    ASP A 205       30.71     73.02                                   
REMARK 500    MET A 208       54.88    -91.43                                   
REMARK 500    HIS A 234       67.25   -107.97                                   
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 TXQ A 337                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 338                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 339                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 340                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3Q9W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3Q9X   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  3Q9Y A    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                  
HET    TXQ  A 337      20                                                       
HET    SO4  A 338       5                                                       
HET    SO4  A 339       5                                                       
HET    SO4  A 340       5                                                       
HETNAM     TXQ 1,2,5,8-TETRAHYDROXYANTHRACENE-9,10-DIONE                        
HETNAM     SO4 SULFATE ION                                                      
HETSYN     TXQ 1,2,5,8-TETRAHYDROXY-ANTHRAQUINONE                               
FORMUL   2  TXQ    C14 H8 O6                                                    
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  HOH   *224(H2 O)                                                    
HELIX    1   1 PRO A   20  ASP A   25  1                                   6    
HELIX    2   2 TYR A   26  HIS A   29  5                                   4    
HELIX    3   3 ASN A   35  ASP A   37  5                                   3    
HELIX    4   4 LYS A   75  ARG A   89  1                                  15    
HELIX    5   5 ASP A  120  LEU A  128  1                                   9    
HELIX    6   6 THR A  129  MET A  150  1                                  22    
HELIX    7   7 LYS A  158  HIS A  160  5                                   3    
HELIX    8   8 SER A  194  LYS A  198  5                                   5    
HELIX    9   9 GLY A  199  VAL A  204  1                                   6    
HELIX   10  10 TYR A  211  ARG A  228  1                                  18    
HELIX   11  11 ASP A  237  GLY A  250  1                                  14    
HELIX   12  12 GLY A  250  ASN A  262  1                                  13    
HELIX   13  13 ASP A  266  ILE A  272  5                                   7    
HELIX   14  14 ARG A  280  VAL A  285  5                                   6    
HELIX   15  15 ASN A  289  VAL A  293  5                                   5    
HELIX   16  16 SER A  294  LEU A  305  1                                  12    
HELIX   17  17 ASP A  308  ARG A  312  5                                   5    
HELIX   18  18 THR A  314  GLU A  320  1                                   7    
HELIX   19  19 HIS A  321  TYR A  325  5                                   5    
SHEET    1   A 5 TYR A  39  ARG A  47  0                                        
SHEET    2   A 5 SER A  51  ASN A  58 -1  O  VAL A  53   N  LEU A  45           
SHEET    3   A 5 LYS A  64  LEU A  70 -1  O  VAL A  67   N  PHE A  54           
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  ASP A  99   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           
CISPEP   1 GLU A  230    PRO A  231          0       -12.28                     
SITE     1 AC1  8 LEU A  45  VAL A  53  VAL A  66  LYS A  68                    
SITE     2 AC1  8 PHE A 113  ILE A 174  ASP A 175  HOH A 347                    
SITE     1 AC2  8 ASP A 253  ARG A 278  ARG A 306  TYR A 307                    
SITE     2 AC2  8 ASP A 308  HOH A 448  HOH A 450  HOH A 466                    
SITE     1 AC3  5 LYS A  77  ARG A  80  ARG A 155  ASN A 189                    
SITE     2 AC3  5 HOH A 390                                                     
SITE     1 AC4  3 ARG A 191  LYS A 198  ASN A 238                               
CRYST1   58.664   45.910   63.628  90.00 111.89  90.00 P 1 21 1      2          
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      0.017046  0.000000  0.006850        0.00000                         
SCALE2      0.000000  0.021782  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016938        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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