GenomeNet

Database: PDB
Entry: 2UZ3
LinkDB: 2UZ3
Original site: 2UZ3 
HEADER    TRANSFERASE                             24-APR-07   2UZ3              
TITLE     CRYSTAL STRUCTURE OF THYMIDINE KINASE WITH DTTP FROM U. UREALYTICUM   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 2.7.1.21;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UREAPLASMA UREALYTICUM;                         
SOURCE   3 ORGANISM_TAXID: 2130;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: PLYSS;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-14B                                   
KEYWDS    DEOXYRIBONUCLEOSIDE KINASE, ZINC-BINDING DOMAIN, FEED-BACK INHIBITOR, 
KEYWDS   2 TK1, DTTP, UU-TK, KINASE, TRANSFERASE, ATP-BINDING, LASSO-DOMAIN,    
KEYWDS   3 DNA SYNTHESIS, NUCLEOTIDE-BINDING                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.WELIN,U.KOSINSKA,N.E.MIKKELSEN,C.CARNROT,C.ZHU,L.WANG,S.ERIKSSON,   
AUTHOR   2 B.MUNCH-PETERSEN,H.EKLUND                                            
REVDAT   4   06-FEB-19 2UZ3    1       REMARK                                   
REVDAT   3   30-JAN-19 2UZ3    1       REMARK                                   
REVDAT   2   24-FEB-09 2UZ3    1       VERSN                                    
REVDAT   1   29-MAY-07 2UZ3    0                                                
SPRSDE     29-MAY-07 2UZ3      1XMR                                             
JRNL        AUTH   M.WELIN,U.KOSINSKA,N.E.MIKKELSEN,C.CARNROT,C.ZHU,L.WANG,     
JRNL        AUTH 2 S.ERIKSSON,B.MUNCH-PETERSEN,H.EKLUND                         
JRNL        TITL   STRUCTURES OF THYMIDINE KINASE 1 OF HUMAN AND MYCOPLASMIC    
JRNL        TITL 2 ORIGIN                                                       
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 101 17970 2004              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   15611477                                                     
JRNL        DOI    10.1073/PNAS.0406332102                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 69.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 31345                          
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) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1672                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2304                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 130                          
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6385                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 144                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.87000                                             
REMARK   3    B22 (A**2) : -0.93000                                             
REMARK   3    B33 (A**2) : 2.39000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.61000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.664         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.322         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.242         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.900        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.877                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6646 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8990 ; 1.341 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   790 ; 5.614 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   316 ;36.614 ;24.304       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1159 ;19.559 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;23.166 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   974 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4974 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2896 ; 0.208 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4490 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   308 ; 0.162 ; 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):    23 ; 0.245 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.190 ; 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):  4055 ; 0.588 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6418 ; 1.062 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2890 ; 1.186 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2572 ; 1.923 ; 4.500       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     11       A      33      2                      
REMARK   3           1     B     11       B      33      2                      
REMARK   3           1     C     11       C      33      2                      
REMARK   3           1     D     11       D      33      2                      
REMARK   3           2     A     35       A      48      2                      
REMARK   3           2     B     35       B      48      2                      
REMARK   3           2     C     35       C      48      2                      
REMARK   3           2     D     35       D      48      2                      
REMARK   3           3     A     68       A      71      2                      
REMARK   3           3     B     68       B      71      2                      
REMARK   3           3     C     68       C      71      2                      
REMARK   3           3     D     68       D      71      2                      
REMARK   3           4     A     73       A     164      2                      
REMARK   3           4     B     73       B     164      2                      
REMARK   3           4     C     73       C     164      2                      
REMARK   3           4     D     73       D     164      2                      
REMARK   3           5     A    173       A     217      2                      
REMARK   3           5     B    173       B     217      2                      
REMARK   3           5     C    173       C     217      2                      
REMARK   3           5     D    173       D     217      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    712 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    712 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    712 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):    712 ;  0.06 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    715 ;  0.50 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    715 ;  0.36 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    715 ;  0.43 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):    715 ;  0.47 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    712 ;  0.14 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    712 ;  0.11 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):    712 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):    712 ;  0.12 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    715 ;  0.80 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    715 ;  0.74 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    715 ;  0.62 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):    715 ;  0.74 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     50       B      67      4                      
REMARK   3           1     D     50       D      67      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    140 ;  1.77 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    140 ;  1.40 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2UZ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-APR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290032341.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUL-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE (220)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33042                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 0.1400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.27000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000, LITHIUM CHLORIDE, DTT,         
REMARK 280  REMARK 280 MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 287.0 K, PH 6.00                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       55.37650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LEU 16 TO PHE                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, LEU 16 TO PHE                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, LEU 16 TO PHE                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, LEU 16 TO PHE                         
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     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     PHE A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     THR A    52                                                      
REMARK 465     ARG A    53                                                      
REMARK 465     SER A    54                                                      
REMARK 465     ILE A    55                                                      
REMARK 465     ARG A    56                                                      
REMARK 465     ASN A    57                                                      
REMARK 465     ILE A    58                                                      
REMARK 465     GLN A    59                                                      
REMARK 465     SER A    60                                                      
REMARK 465     ARG A    61                                                      
REMARK 465     THR A    62                                                      
REMARK 465     GLY A    63                                                      
REMARK 465     THR A    64                                                      
REMARK 465     SER A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     PRO A    67                                                      
REMARK 465     LYS A   218                                                      
REMARK 465     ARG A   219                                                      
REMARK 465     ASN A   220                                                      
REMARK 465     LYS A   221                                                      
REMARK 465     ASN A   222                                                      
REMARK 465     ILE A   223                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     PHE B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     LYS B    10                                                      
REMARK 465     LYS B   218                                                      
REMARK 465     ARG B   219                                                      
REMARK 465     ASN B   220                                                      
REMARK 465     LYS B   221                                                      
REMARK 465     ASN B   222                                                      
REMARK 465     ILE B   223                                                      
REMARK 465     MET C   -19                                                      
REMARK 465     GLY C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ASN C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     PHE C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     LYS C     9                                                      
REMARK 465     LYS C    10                                                      
REMARK 465     ILE C    50                                                      
REMARK 465     ASP C    51                                                      
REMARK 465     THR C    52                                                      
REMARK 465     ARG C    53                                                      
REMARK 465     SER C    54                                                      
REMARK 465     ILE C    55                                                      
REMARK 465     ARG C    56                                                      
REMARK 465     ASN C    57                                                      
REMARK 465     ILE C    58                                                      
REMARK 465     GLN C    59                                                      
REMARK 465     SER C    60                                                      
REMARK 465     ARG C    61                                                      
REMARK 465     THR C    62                                                      
REMARK 465     GLY C    63                                                      
REMARK 465     THR C    64                                                      
REMARK 465     LYS C   218                                                      
REMARK 465     ARG C   219                                                      
REMARK 465     ASN C   220                                                      
REMARK 465     LYS C   221                                                      
REMARK 465     ASN C   222                                                      
REMARK 465     ILE C   223                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     VAL D     4                                                      
REMARK 465     ASN D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     PHE D     7                                                      
REMARK 465     SER D     8                                                      
REMARK 465     LYS D     9                                                      
REMARK 465     LYS D    10                                                      
REMARK 465     LYS D   218                                                      
REMARK 465     ARG D   219                                                      
REMARK 465     ASN D   220                                                      
REMARK 465     LYS D   221                                                      
REMARK 465     ASN D   222                                                      
REMARK 465     ILE D   223                                                      
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    ASP C   176     O    HOH C  2024              2.19            
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    PRO A  20     -169.30    -76.83                                   
REMARK 500    CYS A 183     -131.27   -132.63                                   
REMARK 500    ASN A 199       33.08     71.18                                   
REMARK 500    ARG B  56       37.85     35.85                                   
REMARK 500    THR B  62     -176.63    171.37                                   
REMARK 500    THR B  64     -166.13   -162.15                                   
REMARK 500    CYS B 183     -130.15   -137.28                                   
REMARK 500    ASN B 199       30.92     70.97                                   
REMARK 500    SER C  68      144.52   -174.15                                   
REMARK 500    ASP C 168       57.30     37.70                                   
REMARK 500    CYS C 183     -139.23   -131.28                                   
REMARK 500    ASP D  51     -154.21   -107.27                                   
REMARK 500    CYS D 183     -134.25   -129.78                                   
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 A1218  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 156   SG                                                     
REMARK 620 2 CYS A 153   SG  112.7                                              
REMARK 620 3 HIS A 194   ND1 103.0 111.6                                        
REMARK 620 4 CYS A 191   SG  113.7 124.1  86.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2218  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 153   SG                                                     
REMARK 620 2 CYS B 156   SG  110.8                                              
REMARK 620 3 HIS B 194   ND1 113.5 109.6                                        
REMARK 620 4 CYS B 191   SG  117.0 112.5  92.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2219  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  26   OG1                                                    
REMARK 620 2 TTP B2220   O1A 130.9                                              
REMARK 620 3 TTP B2220   O3B 147.8  66.0                                        
REMARK 620 4 TTP B2220   O1G  94.2 120.0  57.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C3218  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 194   ND1                                                    
REMARK 620 2 CYS C 153   SG  106.1                                              
REMARK 620 3 CYS C 191   SG   96.6 118.3                                        
REMARK 620 4 CYS C 156   SG  107.5 110.1 116.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D4218  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 153   SG                                                     
REMARK 620 2 CYS D 191   SG  124.6                                              
REMARK 620 3 CYS D 156   SG  109.2 113.8                                        
REMARK 620 4 HIS D 194   ND1 109.5  93.0 103.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D4219  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TTP D4220   O1A                                                    
REMARK 620 2 TTP D4220   O1G  89.4                                              
REMARK 620 3 THR D  26   OG1 161.5  82.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1218                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B2218                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2219                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C3218                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D4218                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D4219                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A1220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP B2220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP C3220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP D4220                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XMR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THYMIDINE KINASE WITH DTTP FROM U.UREALYTICUM   
REMARK 900 RELATED ID: 2B8T   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM U .UREALYTICUM INCOMPLEX  
REMARK 900 WITH THYMIDINE                                                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE TWENTY FIRTS RESIDUES (-19 - 0) CORRESPOND TO THE HIS-TAG,       
REMARK 999 WHICH WAS NOT REMOVED PRIOR TO CRYSTALLIZATION                       
DBREF  2UZ3 A  -19     0  PDB    2UZ3     2UZ3           -19      0             
DBREF  2UZ3 A    1   223  UNP    Q9PPP5   KITH_UREPA       1    223             
DBREF  2UZ3 B  -19     0  PDB    2UZ3     2UZ3           -19      0             
DBREF  2UZ3 B    1   223  UNP    Q9PPP5   KITH_UREPA       1    223             
DBREF  2UZ3 C  -19     0  PDB    2UZ3     2UZ3           -19      0             
DBREF  2UZ3 C    1   223  UNP    Q9PPP5   KITH_UREPA       1    223             
DBREF  2UZ3 D  -19     0  PDB    2UZ3     2UZ3           -19      0             
DBREF  2UZ3 D    1   223  UNP    Q9PPP5   KITH_UREPA       1    223             
SEQADV 2UZ3 PHE A   16  UNP  Q9PPP5    LEU    16 ENGINEERED MUTATION            
SEQADV 2UZ3 PHE B   16  UNP  Q9PPP5    LEU    16 ENGINEERED MUTATION            
SEQADV 2UZ3 PHE C   16  UNP  Q9PPP5    LEU    16 ENGINEERED MUTATION            
SEQADV 2UZ3 PHE D   16  UNP  Q9PPP5    LEU    16 ENGINEERED MUTATION            
SEQRES   1 A  243  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  243  LEU VAL PRO ARG GLY SER HIS MET ALA LYS VAL ASN ALA          
SEQRES   3 A  243  PHE SER LYS LYS ILE GLY TRP ILE GLU PHE ILE THR GLY          
SEQRES   4 A  243  PRO MET PHE ALA GLY LYS THR ALA GLU LEU ILE ARG ARG          
SEQRES   5 A  243  LEU HIS ARG LEU GLU TYR ALA ASP VAL LYS TYR LEU VAL          
SEQRES   6 A  243  PHE LYS PRO LYS ILE ASP THR ARG SER ILE ARG ASN ILE          
SEQRES   7 A  243  GLN SER ARG THR GLY THR SER LEU PRO SER VAL GLU VAL          
SEQRES   8 A  243  GLU SER ALA PRO GLU ILE LEU ASN TYR ILE MET SER ASN          
SEQRES   9 A  243  SER PHE ASN ASP GLU THR LYS VAL ILE GLY ILE ASP GLU          
SEQRES  10 A  243  VAL GLN PHE PHE ASP ASP ARG ILE CYS GLU VAL ALA ASN          
SEQRES  11 A  243  ILE LEU ALA GLU ASN GLY PHE VAL VAL ILE ILE SER GLY          
SEQRES  12 A  243  LEU ASP LYS ASN PHE LYS GLY GLU PRO PHE GLY PRO ILE          
SEQRES  13 A  243  ALA LYS LEU PHE THR TYR ALA ASP LYS ILE THR LYS LEU          
SEQRES  14 A  243  THR ALA ILE CYS ASN GLU CYS GLY ALA GLU ALA THR HIS          
SEQRES  15 A  243  SER LEU ARG LYS ILE ASP GLY LYS HIS ALA ASP TYR ASN          
SEQRES  16 A  243  ASP ASP ILE VAL LYS ILE GLY CYS GLN GLU PHE TYR SER          
SEQRES  17 A  243  ALA VAL CYS ARG HIS HIS HIS LYS VAL PRO ASN ARG PRO          
SEQRES  18 A  243  TYR LEU ASN SER ASN SER GLU GLU PHE ILE LYS PHE PHE          
SEQRES  19 A  243  LYS ASN LYS LYS ARG ASN LYS ASN ILE                          
SEQRES   1 B  243  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  243  LEU VAL PRO ARG GLY SER HIS MET ALA LYS VAL ASN ALA          
SEQRES   3 B  243  PHE SER LYS LYS ILE GLY TRP ILE GLU PHE ILE THR GLY          
SEQRES   4 B  243  PRO MET PHE ALA GLY LYS THR ALA GLU LEU ILE ARG ARG          
SEQRES   5 B  243  LEU HIS ARG LEU GLU TYR ALA ASP VAL LYS TYR LEU VAL          
SEQRES   6 B  243  PHE LYS PRO LYS ILE ASP THR ARG SER ILE ARG ASN ILE          
SEQRES   7 B  243  GLN SER ARG THR GLY THR SER LEU PRO SER VAL GLU VAL          
SEQRES   8 B  243  GLU SER ALA PRO GLU ILE LEU ASN TYR ILE MET SER ASN          
SEQRES   9 B  243  SER PHE ASN ASP GLU THR LYS VAL ILE GLY ILE ASP GLU          
SEQRES  10 B  243  VAL GLN PHE PHE ASP ASP ARG ILE CYS GLU VAL ALA ASN          
SEQRES  11 B  243  ILE LEU ALA GLU ASN GLY PHE VAL VAL ILE ILE SER GLY          
SEQRES  12 B  243  LEU ASP LYS ASN PHE LYS GLY GLU PRO PHE GLY PRO ILE          
SEQRES  13 B  243  ALA LYS LEU PHE THR TYR ALA ASP LYS ILE THR LYS LEU          
SEQRES  14 B  243  THR ALA ILE CYS ASN GLU CYS GLY ALA GLU ALA THR HIS          
SEQRES  15 B  243  SER LEU ARG LYS ILE ASP GLY LYS HIS ALA ASP TYR ASN          
SEQRES  16 B  243  ASP ASP ILE VAL LYS ILE GLY CYS GLN GLU PHE TYR SER          
SEQRES  17 B  243  ALA VAL CYS ARG HIS HIS HIS LYS VAL PRO ASN ARG PRO          
SEQRES  18 B  243  TYR LEU ASN SER ASN SER GLU GLU PHE ILE LYS PHE PHE          
SEQRES  19 B  243  LYS ASN LYS LYS ARG ASN LYS ASN ILE                          
SEQRES   1 C  243  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  243  LEU VAL PRO ARG GLY SER HIS MET ALA LYS VAL ASN ALA          
SEQRES   3 C  243  PHE SER LYS LYS ILE GLY TRP ILE GLU PHE ILE THR GLY          
SEQRES   4 C  243  PRO MET PHE ALA GLY LYS THR ALA GLU LEU ILE ARG ARG          
SEQRES   5 C  243  LEU HIS ARG LEU GLU TYR ALA ASP VAL LYS TYR LEU VAL          
SEQRES   6 C  243  PHE LYS PRO LYS ILE ASP THR ARG SER ILE ARG ASN ILE          
SEQRES   7 C  243  GLN SER ARG THR GLY THR SER LEU PRO SER VAL GLU VAL          
SEQRES   8 C  243  GLU SER ALA PRO GLU ILE LEU ASN TYR ILE MET SER ASN          
SEQRES   9 C  243  SER PHE ASN ASP GLU THR LYS VAL ILE GLY ILE ASP GLU          
SEQRES  10 C  243  VAL GLN PHE PHE ASP ASP ARG ILE CYS GLU VAL ALA ASN          
SEQRES  11 C  243  ILE LEU ALA GLU ASN GLY PHE VAL VAL ILE ILE SER GLY          
SEQRES  12 C  243  LEU ASP LYS ASN PHE LYS GLY GLU PRO PHE GLY PRO ILE          
SEQRES  13 C  243  ALA LYS LEU PHE THR TYR ALA ASP LYS ILE THR LYS LEU          
SEQRES  14 C  243  THR ALA ILE CYS ASN GLU CYS GLY ALA GLU ALA THR HIS          
SEQRES  15 C  243  SER LEU ARG LYS ILE ASP GLY LYS HIS ALA ASP TYR ASN          
SEQRES  16 C  243  ASP ASP ILE VAL LYS ILE GLY CYS GLN GLU PHE TYR SER          
SEQRES  17 C  243  ALA VAL CYS ARG HIS HIS HIS LYS VAL PRO ASN ARG PRO          
SEQRES  18 C  243  TYR LEU ASN SER ASN SER GLU GLU PHE ILE LYS PHE PHE          
SEQRES  19 C  243  LYS ASN LYS LYS ARG ASN LYS ASN ILE                          
SEQRES   1 D  243  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  243  LEU VAL PRO ARG GLY SER HIS MET ALA LYS VAL ASN ALA          
SEQRES   3 D  243  PHE SER LYS LYS ILE GLY TRP ILE GLU PHE ILE THR GLY          
SEQRES   4 D  243  PRO MET PHE ALA GLY LYS THR ALA GLU LEU ILE ARG ARG          
SEQRES   5 D  243  LEU HIS ARG LEU GLU TYR ALA ASP VAL LYS TYR LEU VAL          
SEQRES   6 D  243  PHE LYS PRO LYS ILE ASP THR ARG SER ILE ARG ASN ILE          
SEQRES   7 D  243  GLN SER ARG THR GLY THR SER LEU PRO SER VAL GLU VAL          
SEQRES   8 D  243  GLU SER ALA PRO GLU ILE LEU ASN TYR ILE MET SER ASN          
SEQRES   9 D  243  SER PHE ASN ASP GLU THR LYS VAL ILE GLY ILE ASP GLU          
SEQRES  10 D  243  VAL GLN PHE PHE ASP ASP ARG ILE CYS GLU VAL ALA ASN          
SEQRES  11 D  243  ILE LEU ALA GLU ASN GLY PHE VAL VAL ILE ILE SER GLY          
SEQRES  12 D  243  LEU ASP LYS ASN PHE LYS GLY GLU PRO PHE GLY PRO ILE          
SEQRES  13 D  243  ALA LYS LEU PHE THR TYR ALA ASP LYS ILE THR LYS LEU          
SEQRES  14 D  243  THR ALA ILE CYS ASN GLU CYS GLY ALA GLU ALA THR HIS          
SEQRES  15 D  243  SER LEU ARG LYS ILE ASP GLY LYS HIS ALA ASP TYR ASN          
SEQRES  16 D  243  ASP ASP ILE VAL LYS ILE GLY CYS GLN GLU PHE TYR SER          
SEQRES  17 D  243  ALA VAL CYS ARG HIS HIS HIS LYS VAL PRO ASN ARG PRO          
SEQRES  18 D  243  TYR LEU ASN SER ASN SER GLU GLU PHE ILE LYS PHE PHE          
SEQRES  19 D  243  LYS ASN LYS LYS ARG ASN LYS ASN ILE                          
HET     ZN  A1218       1                                                       
HET    TTP  A1220      29                                                       
HET     ZN  B2218       1                                                       
HET     MG  B2219       1                                                       
HET    TTP  B2220      29                                                       
HET     ZN  C3218       1                                                       
HET    TTP  C3220      29                                                       
HET     ZN  D4218       1                                                       
HET     MG  D4219       1                                                       
HET    TTP  D4220      29                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     TTP THYMIDINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6  TTP    4(C10 H17 N2 O14 P3)                                         
FORMUL   8   MG    2(MG 2+)                                                     
FORMUL  15  HOH   *144(H2 O)                                                    
HELIX    1   1 GLY A   24  TYR A   38  1                                  15    
HELIX    2   2 ALA A   74  SER A   83  1                                  10    
HELIX    3   3 GLU A   97  PHE A  101  5                                   5    
HELIX    4   4 ASP A  103  ASN A  115  1                                  13    
HELIX    5   5 PRO A  135  ALA A  143  1                                   9    
HELIX    6   6 ASN A  206  ASN A  216  1                                  11    
HELIX    7   7 GLY B   24  TYR B   38  1                                  15    
HELIX    8   8 ALA B   74  SER B   83  1                                  10    
HELIX    9   9 GLU B   97  PHE B  101  5                                   5    
HELIX   10  10 ASP B  103  ASN B  115  1                                  13    
HELIX   11  11 PRO B  135  ALA B  143  1                                   9    
HELIX   12  12 ASN B  206  ASN B  216  1                                  11    
HELIX   13  13 GLY C   24  TYR C   38  1                                  15    
HELIX   14  14 ALA C   74  SER C   83  1                                  10    
HELIX   15  15 GLU C   97  PHE C  101  5                                   5    
HELIX   16  16 ASP C  103  ASN C  115  1                                  13    
HELIX   17  17 PRO C  135  ALA C  143  1                                   9    
HELIX   18  18 ASN C  206  ASN C  216  1                                  11    
HELIX   19  19 GLY D   24  TYR D   38  1                                  15    
HELIX   20  20 ALA D   74  SER D   83  1                                  10    
HELIX   21  21 GLU D   97  PHE D  101  5                                   5    
HELIX   22  22 ASP D  103  ASN D  115  1                                  13    
HELIX   23  23 PRO D  135  ALA D  143  1                                   9    
HELIX   24  24 ASN D  206  ASN D  216  1                                  11    
SHEET    1  AA 6 VAL A  69  VAL A  71  0                                        
SHEET    2  AA 6 TYR A  43  PRO A  48  1  O  VAL A  45   N  VAL A  69           
SHEET    3  AA 6 VAL A  92  ILE A  95  1  O  VAL A  92   N  LEU A  44           
SHEET    4  AA 6 VAL A 118  LEU A 124  1  O  VAL A 118   N  ILE A  93           
SHEET    5  AA 6 TRP A  13  GLY A  19  1  O  TRP A  13   N  VAL A 119           
SHEET    6  AA 6 LYS A 145  LYS A 148  1  O  LYS A 145   N  PHE A  16           
SHEET    1  AB 2 ALA A 151  ILE A 152  0                                        
SHEET    2  AB 2 GLU A 159  ALA A 160 -1  O  ALA A 160   N  ALA A 151           
SHEET    1  AC 3 LYS A 170  HIS A 171  0                                        
SHEET    2  AC 3 HIS A 162  ILE A 167 -1  O  ILE A 167   N  LYS A 170           
SHEET    3  AC 3 TYR A 187  VAL A 190 -1  O  SER A 188   N  LEU A 164           
SHEET    1  BA 6 VAL B  69  VAL B  71  0                                        
SHEET    2  BA 6 TYR B  43  PRO B  48  1  O  VAL B  45   N  VAL B  69           
SHEET    3  BA 6 VAL B  92  ILE B  95  1  O  VAL B  92   N  LEU B  44           
SHEET    4  BA 6 VAL B 118  SER B 122  1  O  VAL B 118   N  ILE B  93           
SHEET    5  BA 6 TRP B  13  THR B  18  1  O  TRP B  13   N  VAL B 119           
SHEET    6  BA 6 LYS B 145  LYS B 148  1  O  LYS B 145   N  PHE B  16           
SHEET    1  BB 2 ASN B  57  GLN B  59  0                                        
SHEET    2  BB 2 SER B  65  PRO B  67 -1  O  LEU B  66   N  ILE B  58           
SHEET    1  BC 2 ALA B 151  ILE B 152  0                                        
SHEET    2  BC 2 GLU B 159  ALA B 160 -1  O  ALA B 160   N  ALA B 151           
SHEET    1  BD 3 LYS B 170  HIS B 171  0                                        
SHEET    2  BD 3 HIS B 162  ILE B 167 -1  O  ILE B 167   N  LYS B 170           
SHEET    3  BD 3 TYR B 187  VAL B 190 -1  O  SER B 188   N  LEU B 164           
SHEET    1  CA 6 VAL C  69  VAL C  71  0                                        
SHEET    2  CA 6 TYR C  43  PRO C  48  1  O  VAL C  45   N  VAL C  69           
SHEET    3  CA 6 VAL C  92  ILE C  95  1  O  VAL C  92   N  LEU C  44           
SHEET    4  CA 6 VAL C 118  LEU C 124  1  O  VAL C 118   N  ILE C  93           
SHEET    5  CA 6 TRP C  13  GLY C  19  1  O  TRP C  13   N  VAL C 119           
SHEET    6  CA 6 LYS C 145  LYS C 148  1  O  LYS C 145   N  PHE C  16           
SHEET    1  CB 2 ALA C 151  ILE C 152  0                                        
SHEET    2  CB 2 GLU C 159  ALA C 160 -1  O  ALA C 160   N  ALA C 151           
SHEET    1  CC 3 LYS C 170  HIS C 171  0                                        
SHEET    2  CC 3 HIS C 162  ILE C 167 -1  O  ILE C 167   N  LYS C 170           
SHEET    3  CC 3 TYR C 187  VAL C 190 -1  O  SER C 188   N  LEU C 164           
SHEET    1  DA 6 VAL D  69  VAL D  71  0                                        
SHEET    2  DA 6 TYR D  43  PRO D  48  1  O  VAL D  45   N  VAL D  69           
SHEET    3  DA 6 VAL D  92  ILE D  95  1  O  VAL D  92   N  LEU D  44           
SHEET    4  DA 6 VAL D 118  SER D 122  1  O  VAL D 118   N  ILE D  93           
SHEET    5  DA 6 TRP D  13  THR D  18  1  O  TRP D  13   N  VAL D 119           
SHEET    6  DA 6 LYS D 145  LYS D 148  1  O  LYS D 145   N  PHE D  16           
SHEET    1  DB 2 ASN D  57  GLN D  59  0                                        
SHEET    2  DB 2 SER D  65  PRO D  67 -1  O  LEU D  66   N  ILE D  58           
SHEET    1  DC 2 ALA D 151  ILE D 152  0                                        
SHEET    2  DC 2 GLU D 159  ALA D 160 -1  O  ALA D 160   N  ALA D 151           
SHEET    1  DD 3 LYS D 170  HIS D 171  0                                        
SHEET    2  DD 3 HIS D 162  ILE D 167 -1  O  ILE D 167   N  LYS D 170           
SHEET    3  DD 3 TYR D 187  VAL D 190 -1  O  SER D 188   N  LEU D 164           
LINK        ZN    ZN A1218                 SG  CYS A 156     1555   1555  2.19  
LINK        ZN    ZN A1218                 SG  CYS A 153     1555   1555  2.24  
LINK        ZN    ZN A1218                 ND1 HIS A 194     1555   1555  2.18  
LINK        ZN    ZN A1218                 SG  CYS A 191     1555   1555  2.25  
LINK        ZN    ZN B2218                 SG  CYS B 153     1555   1555  2.29  
LINK        ZN    ZN B2218                 SG  CYS B 156     1555   1555  2.25  
LINK        ZN    ZN B2218                 ND1 HIS B 194     1555   1555  2.08  
LINK        ZN    ZN B2218                 SG  CYS B 191     1555   1555  2.35  
LINK        MG    MG B2219                 OG1 THR B  26     1555   1555  2.81  
LINK        MG    MG B2219                 O1A TTP B2220     1555   1555  2.16  
LINK        MG    MG B2219                 O3B TTP B2220     1555   1555  2.81  
LINK        MG    MG B2219                 O1G TTP B2220     1555   1555  2.29  
LINK        ZN    ZN C3218                 ND1 HIS C 194     1555   1555  2.25  
LINK        ZN    ZN C3218                 SG  CYS C 153     1555   1555  2.25  
LINK        ZN    ZN C3218                 SG  CYS C 191     1555   1555  2.05  
LINK        ZN    ZN C3218                 SG  CYS C 156     1555   1555  2.33  
LINK        ZN    ZN D4218                 SG  CYS D 153     1555   1555  2.26  
LINK        ZN    ZN D4218                 SG  CYS D 191     1555   1555  2.27  
LINK        ZN    ZN D4218                 SG  CYS D 156     1555   1555  2.23  
LINK        ZN    ZN D4218                 ND1 HIS D 194     1555   1555  2.33  
LINK        MG    MG D4219                 O1A TTP D4220     1555   1555  1.98  
LINK        MG    MG D4219                 O1G TTP D4220     1555   1555  2.55  
LINK        MG    MG D4219                 OG1 THR D  26     1555   1555  2.20  
SITE     1 AC1  4 CYS A 153  CYS A 156  CYS A 191  HIS A 194                    
SITE     1 AC2  4 CYS B 153  CYS B 156  CYS B 191  HIS B 194                    
SITE     1 AC3  2 THR B  26  TTP B2220                                          
SITE     1 AC4  4 CYS C 153  CYS C 156  CYS C 191  HIS C 194                    
SITE     1 AC5  4 CYS D 153  CYS D 156  CYS D 191  HIS D 194                    
SITE     1 AC6  2 THR D  26  TTP D4220                                          
SITE     1 AC7 19 MET A  21  PHE A  22  ALA A  23  GLY A  24                    
SITE     2 AC7 19 LYS A  25  THR A  26  GLN A  99  PHE A 100                    
SITE     3 AC7 19 ASN A 127  PHE A 128  PHE A 133  SER A 163                    
SITE     4 AC7 19 ILE A 178  VAL A 179  LYS A 180  ILE A 181                    
SITE     5 AC7 19 GLY A 182  TYR A 187  HOH A2018                               
SITE     1 AC8 26 MET B  21  PHE B  22  ALA B  23  GLY B  24                    
SITE     2 AC8 26 LYS B  25  THR B  26  ASP B  51  ARG B  53                    
SITE     3 AC8 26 ARG B  61  GLU B  97  PHE B 100  LEU B 124                    
SITE     4 AC8 26 ASN B 127  PHE B 128  PHE B 133  SER B 163                    
SITE     5 AC8 26 ARG B 165  ILE B 178  VAL B 179  LYS B 180                    
SITE     6 AC8 26 ILE B 181  GLY B 182  TYR B 187  HOH B2003                    
SITE     7 AC8 26 HOH B2052   MG B2219                                          
SITE     1 AC9 20 MET C  21  PHE C  22  ALA C  23  GLY C  24                    
SITE     2 AC9 20 LYS C  25  THR C  26  PHE C 100  LEU C 124                    
SITE     3 AC9 20 ASN C 127  PHE C 128  PHE C 133  SER C 163                    
SITE     4 AC9 20 ARG C 165  ILE C 178  VAL C 179  LYS C 180                    
SITE     5 AC9 20 GLY C 182  TYR C 187  HOH C2029  HOH C2030                    
SITE     1 BC1 21 MET D  21  PHE D  22  ALA D  23  GLY D  24                    
SITE     2 BC1 21 LYS D  25  THR D  26  PHE D 100  LEU D 124                    
SITE     3 BC1 21 ASN D 127  PHE D 128  PHE D 133  SER D 163                    
SITE     4 BC1 21 ILE D 178  VAL D 179  LYS D 180  ILE D 181                    
SITE     5 BC1 21 GLY D 182  TYR D 187  HOH D2004  HOH D2043                    
SITE     6 BC1 21  MG D4219                                                     
CRYST1   63.789  110.753   73.034  90.00 109.86  90.00 P 1 21 1      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      0.015677  0.000000  0.005663        0.00000                         
SCALE2      0.000000  0.009029  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014558        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system