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Database: PDB
Entry: 2J9R
LinkDB: 2J9R
Original site: 2J9R 
HEADER    TRANSFERASE                             15-NOV-06   2J9R              
TITLE     THYMIDINE KINASE FROM B. ANTHRACIS IN COMPLEX WITH DT.                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.1.21;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_TAXID: 260799;                                              
SOURCE   4 STRAIN: STERNE;                                                      
SOURCE   5 VARIANT: 34F2;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: PLYSS;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET-14B                                    
KEYWDS    TK1, DNK, LASSO, KINASE, TRANSFERASE, ATP-BINDING,                    
KEYWDS   2 DEOXYRIBONUCLEOSIDE KINASE, DNA SYNTHESIS, PHOSPHATE ACCEPTOR,       
KEYWDS   3 NUCLEOTIDE-BINDING                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.KOSINSKA,C.CARNROT,M.P.B.SANDRINI,A.R.CLAUSEN,L.WANG,J.PISKUR,      
AUTHOR   2 S.ERIKSSON,H.EKLUND                                                  
REVDAT   3   13-JUL-11 2J9R    1       VERSN                                    
REVDAT   2   24-FEB-09 2J9R    1       VERSN                                    
REVDAT   1   23-JAN-07 2J9R    0                                                
JRNL        AUTH   U.KOSINSKA,C.CARNROT,M.P.B.SANDRINI,A.R.CLAUSEN,L.WANG,      
JRNL        AUTH 2 J.PISKUR,S.ERIKSSON,H.EKLUND                                 
JRNL        TITL   STRUCTURAL STUDIES OF THYMIDINE KINASES FROM BACILLUS        
JRNL        TITL 2 ANTHRACIS AND BACILLUS CEREUS PROVIDE INSIGHTS INTO          
JRNL        TITL 3 QUATERNARY STRUCTURE AND CONFORMATIONAL CHANGES UPON         
JRNL        TITL 4 SUBSTRATE BINDING                                            
JRNL        REF    FEBS J.                       V. 274   727 2007              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   17288553                                                     
JRNL        DOI    10.1111/J.1742-4658.2006.05617.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.7  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 8366                           
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 415                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 598                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 31                           
REMARK   3   BIN FREE R VALUE                    : 0.4200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1385                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 19                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.51000                                              
REMARK   3    B22 (A**2) : 2.51000                                              
REMARK   3    B33 (A**2) : -5.02000                                             
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): 0.409         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.276         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.179         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.998        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1435 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1943 ; 1.343 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   176 ; 5.927 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    65 ;33.099 ;23.692       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   242 ;17.524 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;16.842 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   218 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1082 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   600 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   974 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    55 ; 0.128 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    44 ; 0.188 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.212 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   908 ; 0.456 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1437 ; 0.841 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   583 ; 1.132 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   506 ; 1.880 ; 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  : 1                                          
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    -1        A   193                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.1328  18.4702  -1.5512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0593 T22:  -0.1821                                     
REMARK   3      T33:  -0.0890 T12:  -0.0006                                     
REMARK   3      T13:   0.0516 T23:   0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9790 L22:   1.8095                                     
REMARK   3      L33:   3.3625 L12:   0.0031                                     
REMARK   3      L13:  -0.3139 L23:   0.0878                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0295 S12:   0.0318 S13:  -0.4261                       
REMARK   3      S21:  -0.0859 S22:  -0.0307 S23:   0.0450                       
REMARK   3      S31:   0.9255 S32:   0.0935 S33:   0.0602                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2J9R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-NOV-06.                  
REMARK 100 THE PDBE ID CODE IS EBI-30510.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8799                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.870                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 14.100                             
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.50                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDP ENTRY 1XMR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.6                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.1                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% 1,2-PROPANEDIOL 0.1M NA/K             
REMARK 280  PHOSPHATE PH 6 10% GLYCEROL                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.58550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       36.58550            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      111.86700            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       36.58550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       55.93350            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       36.58550            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      167.80050            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       36.58550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      167.80050            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       36.58550            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       55.93350            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       36.58550            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       36.58550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      111.86700            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       36.58550            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       36.58550            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      111.86700            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       36.58550            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      167.80050            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       36.58550            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       55.93350            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       36.58550            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       55.93350            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       36.58550            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      167.80050            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       36.58550            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       36.58550            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      111.86700            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
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   BIOMT1   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000      -73.17100            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000       73.17100            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      -73.17100            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       73.17100            
REMARK 350   BIOMT3   4  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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     ILE A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     ASN A    48                                                      
REMARK 465     ARG A    49                                                      
REMARK 465     TYR A    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     GLU A    52                                                      
REMARK 465     GLU A    53                                                      
REMARK 465     ASP A    54                                                      
REMARK 465     VAL A    55                                                      
REMARK 465     VAL A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     HIS A    58                                                      
REMARK 465     ASN A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     LEU A    61                                                      
REMARK 465     LYS A    62                                                      
REMARK 465     ARG A   194                                                      
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   7       49.12    -88.36                                   
REMARK 500    ASP A  94     -178.87    -68.62                                   
REMARK 500    SER A 153       12.25   -145.02                                   
REMARK 500    ALA A 175     -137.71   -137.04                                   
REMARK 500    SER A 178      -12.90   -153.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1194  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 145   SG                                                     
REMARK 620 2 CYS A 148   SG  100.8                                              
REMARK 620 3 CYS A 186   SG  109.1 112.6                                        
REMARK 620 4 CYS A 183   SG  121.9 114.5  98.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1194                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1196                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THM A1195                 
DBREF  2J9R A  -19     0  PDB    2J9R     2J9R           -19      0             
DBREF  2J9R A    1   194  UNP    Q81JX0   KITH_BACAN       1    194             
SEQRES   1 A  214  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  214  LEU VAL PRO ARG GLY SER HIS MET TYR LEU ILE ASN GLN          
SEQRES   3 A  214  ASN GLY TRP ILE GLU VAL ILE CYS GLY SER MET PHE SER          
SEQRES   4 A  214  GLY LYS SER GLU GLU LEU ILE ARG ARG VAL ARG ARG THR          
SEQRES   5 A  214  GLN PHE ALA LYS GLN HIS ALA ILE VAL PHE LYS PRO CYS          
SEQRES   6 A  214  ILE ASP ASN ARG TYR SER GLU GLU ASP VAL VAL SER HIS          
SEQRES   7 A  214  ASN GLY LEU LYS VAL LYS ALA VAL PRO VAL SER ALA SER          
SEQRES   8 A  214  LYS ASP ILE PHE LYS HIS ILE THR GLU GLU MET ASP VAL          
SEQRES   9 A  214  ILE ALA ILE ASP GLU VAL GLN PHE PHE ASP GLY ASP ILE          
SEQRES  10 A  214  VAL GLU VAL VAL GLN VAL LEU ALA ASN ARG GLY TYR ARG          
SEQRES  11 A  214  VAL ILE VAL ALA GLY LEU ASP GLN ASP PHE ARG GLY LEU          
SEQRES  12 A  214  PRO PHE GLY GLN VAL PRO GLN LEU MET ALA ILE ALA GLU          
SEQRES  13 A  214  HIS VAL THR LYS LEU GLN ALA VAL CYS SER ALA CYS GLY          
SEQRES  14 A  214  SER PRO ALA SER ARG THR GLN ARG LEU ILE ASP GLY GLU          
SEQRES  15 A  214  PRO ALA ALA PHE ASP ASP PRO ILE ILE LEU VAL GLY ALA          
SEQRES  16 A  214  SER GLU SER TYR GLU PRO ARG CYS ARG HIS CYS HIS ALA          
SEQRES  17 A  214  VAL PRO THR LYS GLN ARG                                      
HET     ZN  A1194       1                                                       
HET    PO4  A1196       5                                                       
HET    THM  A1195      17                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     THM THYMIDINE                                                        
HETSYN     THM DEOXYTHYMIDINE                                                   
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  THM    C10 H14 N2 O5                                                
FORMUL   5  HOH   *19(H2 O)                                                     
HELIX    1   1 GLY A   20  ALA A   35  1                                  16    
HELIX    2   2 ALA A   70  ILE A   78  5                                   9    
HELIX    3   3 GLU A   89  PHE A   93  5                                   5    
HELIX    4   4 ASP A   96  ARG A  107  1                                  12    
HELIX    5   5 GLN A  127  ALA A  135  1                                   9    
SHEET    1  AA 6 ALA A  65  PRO A  67  0                                        
SHEET    2  AA 6 ALA A  39  LYS A  43  1  O  VAL A  41   N  VAL A  66           
SHEET    3  AA 6 VAL A  84  ILE A  87  1  O  VAL A  84   N  ILE A  40           
SHEET    4  AA 6 ARG A 110  GLY A 115  1  O  ARG A 110   N  ILE A  85           
SHEET    5  AA 6 TRP A   9  CYS A  14  1  O  TRP A   9   N  VAL A 111           
SHEET    6  AA 6 HIS A 137  LYS A 140  1  O  HIS A 137   N  VAL A  12           
SHEET    1  AB 2 ALA A 143  CYS A 145  0                                        
SHEET    2  AB 2 GLY A 149  ALA A 152 -1  O  SER A 150   N  CYS A 145           
SHEET    1  AC 3 GLU A 162  PRO A 163  0                                        
SHEET    2  AC 3 ARG A 154  ILE A 159 -1  O  ILE A 159   N  GLU A 162           
SHEET    3  AC 3 TYR A 179  ARG A 182 -1  O  GLU A 180   N  GLN A 156           
LINK        ZN    ZN A1194                 SG  CYS A 145     1555   1555  2.33  
LINK        ZN    ZN A1194                 SG  CYS A 148     1555   1555  2.40  
LINK        ZN    ZN A1194                 SG  CYS A 186     1555   1555  2.34  
LINK        ZN    ZN A1194                 SG  CYS A 183     1555   1555  2.31  
SITE     1 AC1  4 CYS A 145  CYS A 148  CYS A 183  CYS A 186                    
SITE     1 AC2  8 SER A  16  PHE A  18  SER A  19  GLY A  20                    
SITE     2 AC2  8 LYS A  21  SER A  22  HOH A2001  HOH A2019                    
SITE     1 AC3 13 GLU A  89  PHE A  92  LEU A 116  ASP A 119                    
SITE     2 AC3 13 PHE A 120  PHE A 125  THR A 155  ILE A 170                    
SITE     3 AC3 13 ILE A 171  LEU A 172  VAL A 173  GLY A 174                    
SITE     4 AC3 13 TYR A 179                                                     
CRYST1   73.171   73.171  223.734  90.00  90.00  90.00 I 41 2 2     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013667  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013667  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004470        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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