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Database: PDB
Entry: 3H30
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HEADER    TRANSFERASE                             15-APR-09   3H30              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF HUMAN PROTEIN KINASE CK2
TITLE    2 WITH 5,6-DICHLORO-1-BETA-D-RIBOFURANOSYLBENZIMIDAZOLE                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC SUBUNIT, RESIDUES 1-334;                         
COMPND   5 SYNONYM: CK II;                                                      
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 CK2, CASEIN KINASE 2, CASEIN KINASE II, ATP-BINDING,   
KEYWDS   2 KINASE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, SERINE/THREONINE-PROTEIN 
KEYWDS   3 KINASE, TRANSFERASE, WNT SIGNALING PATHWAY                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.NIEFIND,J.RAAF,O.-G.ISSINGER                                        
REVDAT   2   01-NOV-17 3H30    1       REMARK                                   
REVDAT   1   12-MAY-09 3H30    0                                                
SPRSDE     12-MAY-09 3H30      2RKP                                             
JRNL        AUTH   J.RAAF,E.BRUNSTEIN,O.-G.ISSINGER,K.NIEFIND                   
JRNL        TITL   THE CK2ALPHA/CK2BETA INTERFACE OF HUMAN PROTEIN KINASE CK2   
JRNL        TITL 2 HARBORS A BINDING POCKET FOR SMALL MOLECULES                 
JRNL        REF    CHEM.BIOL.                    V.  15   111 2008              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   18291315                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2007.12.012                               
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.NIEFIND,C.W.YDE,I.ERMAKOVA,O.-G.ISSINGER                   
REMARK   1  TITL   EVOLVED TO BE ACTIVE: SULFATE IONS DEFINE SUBSTRATE          
REMARK   1  TITL 2 RECOGNITION SITES OF CK2ALPHA AND EMPHASISE ITS EXCEPTIONAL  
REMARK   1  TITL 3 ROLE WITHIN THE CMGC FAMILY OF EUKARYOTIC PROTEIN KINASES    
REMARK   1  REF    J.MOL.BIOL.                   V. 370   427 2007              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   17524418                                                     
REMARK   1  DOI    10.1016/J.JMB.2007.04.068                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   I.ERMAKOVA,B.BOLDYREFF,O.-G.ISSINGER,K.NIEFIND               
REMARK   1  TITL   CRYSTAL STRUCTURE OF A C-TERMINAL DELETION MUTANT OF HUMAN   
REMARK   1  TITL 2 PROTEIN KINASE CK2 CATALYTIC SUBUNIT                         
REMARK   1  REF    J.MOL.BIOL.                   V. 330   925 2003              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   12860116                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
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) : 1.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 87584                          
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) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1860                            
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) : 1.56                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.60                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6457                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 140                          
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5626                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 617                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.02000                                             
REMARK   3    B22 (A**2) : -1.02000                                             
REMARK   3    B33 (A**2) : 2.03000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.017         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.018         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.040         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.474         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5888 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4098 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7977 ; 1.189 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9844 ; 0.840 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   674 ; 5.708 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   315 ;32.235 ;23.079       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1041 ;13.674 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;13.665 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   828 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6488 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1282 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3360 ; 1.948 ; 6.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1340 ; 0.920 ; 6.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5468 ; 2.495 ; 6.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2528 ; 3.211 ; 9.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2509 ; 4.010 ; 9.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H,K,L                                           
REMARK   3      TWIN FRACTION : 0.502                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : K,H,-L                                          
REMARK   3      TWIN FRACTION : 0.498                                           
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 : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A    12                          
REMARK   3    RESIDUE RANGE :   A   117        A   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.6470  15.9240   2.1330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0464 T22:   0.0255                                     
REMARK   3      T33:   0.0362 T12:   0.0109                                     
REMARK   3      T13:   0.0272 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2323 L22:   0.7696                                     
REMARK   3      L33:   1.2943 L12:  -0.3436                                     
REMARK   3      L13:  -0.1616 L23:   0.5581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0891 S12:  -0.0761 S13:   0.1626                       
REMARK   3      S21:   0.0071 S22:  -0.0002 S23:  -0.0683                       
REMARK   3      S31:  -0.1566 S32:  -0.0791 S33:  -0.0888                       
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   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7830  -4.5290  -5.6760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1037 T22:   0.1959                                     
REMARK   3      T33:   0.0755 T12:  -0.0512                                     
REMARK   3      T13:   0.0063 T23:  -0.0127                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5168 L22:   2.1151                                     
REMARK   3      L33:   1.2887 L12:   0.3800                                     
REMARK   3      L13:  -0.7633 L23:  -0.8519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0113 S12:   0.1800 S13:  -0.0476                       
REMARK   3      S21:   0.1033 S22:   0.0011 S23:   0.2338                       
REMARK   3      S31:   0.0961 S32:  -0.3293 S33:   0.0101                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B    12                          
REMARK   3    RESIDUE RANGE :   B   117        B   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.9300  -8.3740 -18.7040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0281 T22:   0.0676                                     
REMARK   3      T33:   0.0379 T12:   0.0125                                     
REMARK   3      T13:   0.0008 T23:  -0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8570 L22:   1.3382                                     
REMARK   3      L33:   0.9970 L12:  -0.4342                                     
REMARK   3      L13:  -0.6450 L23:   0.0803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0048 S12:   0.0264 S13:   0.0759                       
REMARK   3      S21:  -0.0884 S22:   0.0743 S23:  -0.1904                       
REMARK   3      S31:   0.0670 S32:   0.1239 S33:  -0.0791                       
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 :   B    13        B   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.1280 -22.2370 -10.9730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2200 T22:   0.1293                                     
REMARK   3      T33:   0.1013 T12:  -0.0751                                     
REMARK   3      T13:   0.0137 T23:   0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0232 L22:   0.4307                                     
REMARK   3      L33:   1.4287 L12:   0.2948                                     
REMARK   3      L13:   0.8566 L23:   0.7564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0128 S12:   0.0579 S13:  -0.2753                       
REMARK   3      S21:   0.2176 S22:  -0.0487 S23:   0.0694                       
REMARK   3      S31:   0.3979 S32:  -0.1324 S33:   0.0358                       
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   336        A   336                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7890  -2.2980   8.3080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8557 T22:   1.1243                                     
REMARK   3      T33:   1.4540 T12:  -0.5341                                     
REMARK   3      T13:  -0.2541 T23:  -0.1863                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  20.3684 L22:  17.0708                                     
REMARK   3      L33:  38.9741 L12: -14.9748                                     
REMARK   3      L13:  27.8227 L23: -22.8743                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.8520 S12:  -1.0715 S13:  -0.1150                       
REMARK   3      S21:   1.6638 S22:   1.8696 S23:  -0.7998                       
REMARK   3      S31:  -2.4972 S32:  -1.9356 S33:  -0.0175                       
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 :   B   336        B   336                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.4160 -18.0770 -23.7930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1284 T22:   0.0989                                     
REMARK   3      T33:   0.1301 T12:  -0.0212                                     
REMARK   3      T13:   0.0188 T23:  -0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.9780 L22:   7.6258                                     
REMARK   3      L33:  17.0056 L12:  -0.4708                                     
REMARK   3      L13:   8.4988 L23:  -9.6378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3361 S12:   0.2777 S13:  -0.4452                       
REMARK   3      S21:  -0.4296 S22:  -0.4087 S23:  -0.2865                       
REMARK   3      S31:   0.7333 S32:   0.6645 S33:   0.0725                       
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   337        A   337                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8320 -16.5010   3.0380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3010 T22:   0.3224                                     
REMARK   3      T33:   0.1999 T12:  -0.0598                                     
REMARK   3      T13:  -0.0323 T23:  -0.0721                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.7809 L22:   9.1653                                     
REMARK   3      L33:   7.1466 L12:  -6.0792                                     
REMARK   3      L13:   0.9866 L23:   5.8002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0054 S12:   0.0448 S13:   0.2094                       
REMARK   3      S21:  -0.0004 S22:  -0.0030 S23:  -0.1024                       
REMARK   3      S31:   0.0292 S32:   0.0770 S33:   0.0084                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3H30 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-APR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000052627.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X12                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89486                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULFATE, 0.2M TRI-SODIUM   
REMARK 280  CITRATE, 0.2M K/NA TARTRATE PH 5.6, THE ENZYME WAS PREINCUBATED     
REMARK 280  WITH 5,6-DICHLORO-1-BETA-D-RIBOFURANOSYLBENZIMIDAZOLE, VAPOR        
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 8.5                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
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,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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       62.89450            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       94.34175            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.44725            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 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 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -369.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     MET B     1                                                      
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   O    HOH A   518     O    HOH A   596              2.09            
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    VAL A 105      -79.06    -75.36                                   
REMARK 500    ASN A 118       42.10    -84.98                                   
REMARK 500    ASN A 118       42.83    -84.98                                   
REMARK 500    ASP A 156       40.61   -149.27                                   
REMARK 500    ASP A 175       61.90     67.26                                   
REMARK 500    ALA A 193      145.84     65.63                                   
REMARK 500    MET A 208       55.89    -92.61                                   
REMARK 500    ASP A 210     -154.07   -148.65                                   
REMARK 500    ARG A 280      131.25    -25.46                                   
REMARK 500    ASP B 156       45.64   -146.94                                   
REMARK 500    ASP B 175       78.47     50.16                                   
REMARK 500    ALA B 193      159.32     72.36                                   
REMARK 500    MET B 208       53.49    -94.86                                   
REMARK 500    HIS B 234       69.14   -100.23                                   
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 RFZ A 336                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RFZ A 337                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 338                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 339                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 340                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 341                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 342                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 343                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 344                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 345                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 346                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 347                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 348                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 349                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 350                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 351                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RFZ B 336                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 337                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 338                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 339                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 340                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 341                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 342                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 343                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 344                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 345                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 346                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 347                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 348                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 349                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 350                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 351                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 352                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 353                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JWH   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH A NON-CATALYTIC SUBUNIT: FULL       
REMARK 900 HETEROTETRAMERIC HOLOENZYME OF HUMAN PROTEIN KINASE CK2              
REMARK 900 RELATED ID: 1LP4   RELATED DB: PDB                                   
REMARK 900 BINARY COMPLEX OF THE ORTHOLOG ENZYME FROM ZEA MAYS WITH THE NON-    
REMARK 900 HYDROLYSABLE ATP ANALOGUE ADENYLYL IMIDODIPHOSPHATE (AMPPNP)         
REMARK 900 RELATED ID: 2PVR   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH THE NON-HYDROLYSABLE ATP ANALOGUE   
REMARK 900 ADENYLYL AND WITH TWO SULFATE IONS                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AS DESCRIBED IN REFERENCE 2 THE GENETIC CONSTRUCT CONTAINS A CODON   
REMARK 999 FOR A FINAL GLYCINE RESIDUE (GLY335).                                
REMARK 999 THIS GLYCINE RESIDUE WAS APPARENTLY LOST DURING PROTEIN PREPARATION  
REMARK 999 OR CRYSTALLIZATION.                                                  
DBREF  3H30 A    1   334  UNP    P68400   CSK21_HUMAN      1    334             
DBREF  3H30 B    1   334  UNP    P68400   CSK21_HUMAN      1    334             
SEQRES   1 A  334  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 A  334  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 A  334  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 A  334  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 A  334  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 A  334  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 A  334  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 A  334  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 A  334  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 A  334  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 A  334  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 A  334  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 A  334  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 A  334  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 A  334  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 A  334  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 A  334  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 A  334  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 A  334  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 A  334  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 A  334  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 A  334  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 A  334  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 A  334  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 A  334  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 A  334  THR VAL VAL LYS ASP GLN ALA ARG MET                          
SEQRES   1 B  334  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 B  334  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 B  334  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 B  334  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 B  334  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 B  334  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 B  334  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 B  334  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 B  334  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 B  334  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 B  334  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 B  334  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 B  334  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 B  334  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 B  334  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 B  334  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 B  334  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 B  334  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 B  334  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 B  334  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 B  334  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 B  334  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 B  334  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 B  334  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 B  334  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 B  334  THR VAL VAL LYS ASP GLN ALA ARG MET                          
HET    RFZ  A 336      20                                                       
HET    RFZ  A 337      20                                                       
HET     CL  A 338       1                                                       
HET     CL  A 339       1                                                       
HET     CL  A 340       1                                                       
HET     CL  A 341       1                                                       
HET     CL  A 342       1                                                       
HET     CL  A 343       1                                                       
HET     CL  A 344       1                                                       
HET     CL  A 345       1                                                       
HET     CL  A 346       1                                                       
HET     CL  A 347       1                                                       
HET     CL  A 348       1                                                       
HET     CL  A 349       1                                                       
HET     CL  A 350       1                                                       
HET     CL  A 351       1                                                       
HET    RFZ  B 336      20                                                       
HET     CL  B 337       1                                                       
HET     CL  B 338       1                                                       
HET     CL  B 339       1                                                       
HET     CL  B 340       1                                                       
HET     CL  B 341       1                                                       
HET     CL  B 342       1                                                       
HET     CL  B 343       1                                                       
HET     CL  B 344       1                                                       
HET     CL  B 345       1                                                       
HET     CL  B 346       1                                                       
HET     CL  B 347       1                                                       
HET     CL  B 348       1                                                       
HET     CL  B 349       1                                                       
HET     CL  B 350       1                                                       
HET     CL  B 351       1                                                       
HET     CL  B 352       1                                                       
HET     CL  B 353       1                                                       
HET     CL  B 354       1                                                       
HETNAM     RFZ 5,6-DICHLORO-1-BETA-D-RIBOFURANOSYL-1H-BENZIMIDAZOLE             
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3  RFZ    3(C12 H12 CL2 N2 O4)                                         
FORMUL   5   CL    32(CL 1-)                                                    
FORMUL  38  HOH   *617(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   74  ARG A   89  1                                  16    
HELIX    5   5 ASP A  120  LEU A  128  5                                   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  TYR A  261  1                                  12    
HELIX   13  13 ASP A  266  GLY A  274  1                                   9    
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    
HELIX   20  20 THR A  326  ASP A  330  5                                   5    
HELIX   21  21 ASP B   14  ARG B   19  1                                   6    
HELIX   22  22 PRO B   20  ASP B   25  1                                   6    
HELIX   23  23 TYR B   26  HIS B   29  5                                   4    
HELIX   24  24 ASN B   35  ASP B   37  5                                   3    
HELIX   25  25 LYS B   74  LEU B   88  1                                  15    
HELIX   26  26 ASP B  120  LEU B  124  5                                   5    
HELIX   27  27 THR B  129  MET B  150  1                                  22    
HELIX   28  28 LYS B  158  HIS B  160  5                                   3    
HELIX   29  29 SER B  194  LYS B  198  5                                   5    
HELIX   30  30 GLY B  199  VAL B  204  1                                   6    
HELIX   31  31 TYR B  211  ARG B  228  1                                  18    
HELIX   32  32 ASP B  237  GLY B  250  1                                  14    
HELIX   33  33 GLY B  250  TYR B  261  1                                  12    
HELIX   34  34 ASP B  266  GLY B  274  1                                   9    
HELIX   35  35 ARG B  280  VAL B  285  5                                   6    
HELIX   36  36 ASN B  289  VAL B  293  5                                   5    
HELIX   37  37 SER B  294  LEU B  305  1                                  12    
HELIX   38  38 ASP B  308  ARG B  312  5                                   5    
HELIX   39  39 THR B  314  GLU B  320  1                                   7    
HELIX   40  40 HIS B  321  TYR B  325  5                                   5    
HELIX   41  41 THR B  326  ASP B  330  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  GLU A  55   N  VAL A  42           
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  PHE A 113   N  VAL A  66           
SHEET    5   A 5 LEU A  97  LYS A 102 -1  N  VAL A 101   O  ALA A 110           
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  GLY B  48  0                                        
SHEET    2   D 5 SER B  51  ASN B  58 -1  O  VAL B  53   N  LEU B  45           
SHEET    3   D 5 LYS B  64  LEU B  70 -1  O  ILE B  69   N  GLU B  52           
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  ARG B 172   N  MET B 163           
CISPEP   1 GLU A  230    PRO A  231          0       -10.04                     
CISPEP   2 GLU B  230    PRO B  231          0        -2.71                     
SITE     1 AC1  7 LEU A  45  VAL A  53  VAL A 116  ASN A 118                    
SITE     2 AC1  7 MET A 163  ILE A 174  HOH A 554                               
SITE     1 AC2 14 THR A  17  HIS A  18  ARG A  19  ARG A  21                    
SITE     2 AC2 14 GLN A  40  LEU A  41  ILE A  69  VAL A 101                    
SITE     3 AC2 14 ASP A 103  PRO A 104  ALA A 110  HOH A 409                    
SITE     4 AC2 14 HOH A 449  HOH A 595                                          
SITE     1 AC3  3 VAL A  11  HIS A 148  ALA A 315                               
SITE     1 AC4  3 LYS A  68  ASP A 175  HOH A 429                               
SITE     1 AC5  2 PRO A 159  HIS A 160                                          
SITE     1 AC6  4 LYS A  77  ARG A  80  ARG A 155   CL A 342                    
SITE     1 AC7  4 ARG A 155  GLU A 180   CL A 341  HOH A 553                    
SITE     1 AC8  2 HOH A 401  HOH A 565                                          
SITE     1 AC9  4 HIS A  29  VAL A  31  GLU A  32  GLU A  86                    
SITE     1 BC1  4 PHE A 232  HIS A 234  ARG A 244  HOH A 513                    
SITE     1 BC2  5 VAL A 293  PRO A 295  LYS B 198  ASN B 238                    
SITE     2 BC2  5 HOH B 479                                                     
SITE     1 BC3  5 ASN A 238  HOH A 446  HOH A 575  HOH A 578                    
SITE     2 BC3  5 VAL B 293                                                     
SITE     1 BC4  2 LYS A 303  LEU A 313                                          
SITE     1 BC5  3 ARG A 306  TYR A 307  HOH A 592                               
SITE     1 BC6  3 THR A 251  TYR A 255  ARG A 275                               
SITE     1 BC7  4 ARG A 278  LYS A 279  ARG A 280  ARG A 283                    
SITE     1 BC8 12 GLY B  46  ARG B  47  GLY B  48  VAL B  53                    
SITE     2 BC8 12 ILE B  95  VAL B 116  ASN B 117  ASN B 118                    
SITE     3 BC8 12 ILE B 174  HOH B 473  HOH B 575  HOH B 640                    
SITE     1 BC9  2 HIS B 148  ALA B 315                                          
SITE     1 CC1  2 ARG B  80  ARG B 155                                          
SITE     1 CC2  3 ARG B 155  TYR B 188  ASN B 189                               
SITE     1 CC3  3 LYS B 122  PRO B 159  HIS B 160                               
SITE     1 CC4  3 LYS B  68  ASP B 175  HOH B 575                               
SITE     1 CC5  4 ARG A  19  HOH A 503  LYS B 170  HOH B 551                    
SITE     1 CC6  2 HOH B 415  HOH B 449                                          
SITE     1 CC7  3 LYS A 170  HOH A 544  ARG B  19                               
SITE     1 CC8  6 LYS B 229  PHE B 232  HIS B 234  ARG B 244                    
SITE     2 CC8  6 HOH B 384  HOH B 536                                          
SITE     1 CC9  4 HOH A 643  HIS B 321  PRO B 322  HOH B 556                    
SITE     1 DC1  3 ASP B 253  ARG B 278  HOH B 546                               
SITE     1 DC2  2 LYS A 329  HOH A 658                                          
SITE     1 DC3  4 HIS B  29  VAL B  31  GLU B  32  GLU B  86                    
SITE     1 DC4  2 GLN A  40  ARG B 333                                          
SITE     1 DC5  4 ARG B  19  PRO B  20  HOH B 616  HOH B 649                    
SITE     1 DC6  3 SER B 194  ARG B 195  HOH B 565                               
SITE     1 DC7  4 LYS B 303  HIS B 321  HOH B 366  HOH B 456                    
CRYST1   71.506   71.506  125.789  90.00  90.00  90.00 P 43          8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013985  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013985  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007950        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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