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Database: PDB
Entry: 2ORW
LinkDB: 2ORW
Original site: 2ORW 
HEADER    TRANSFERASE                             04-FEB-07   2ORW              
TITLE     THERMOTOGA MARITIMA THYMIDINE KINASE 1 LIKE ENZYME IN                 
TITLE    2 COMPLEX WITH TP4A                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.1.21;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;                            
SOURCE   3 ORGANISM_TAXID: 2336;                                                
SOURCE   4 GENE: TDK;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    TMTK, TP4A, TRANSFERASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.SEGURA-PENA,S.LUTZ,C.MONNERJAHN,M.KONRAD,A.LAVIE                    
REVDAT   3   24-FEB-09 2ORW    1       VERSN                                    
REVDAT   2   22-MAY-07 2ORW    1       JRNL                                     
REVDAT   1   27-MAR-07 2ORW    0                                                
JRNL        AUTH   D.SEGURA-PENA,S.LUTZ,C.MONNERJAHN,M.KONRAD,A.LAVIE           
JRNL        TITL   BINDING OF ATP TO TK1-LIKE ENZYMES IS ASSOCIATED             
JRNL        TITL 2 WITH A CONFORMATIONAL CHANGE IN THE QUATERNARY               
JRNL        TITL 3 STRUCTURE.                                                   
JRNL        REF    J.MOL.BIOL.                   V. 369   129 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17407781                                                     
JRNL        DOI    10.1016/J.JMB.2007.02.104                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 55418                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5566                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2964                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 336                          
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2694                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 106                                     
REMARK   3   SOLVENT ATOMS            : 370                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.77                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.50000                                             
REMARK   3    B22 (A**2) : 1.09000                                              
REMARK   3    B33 (A**2) : -0.62000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.06000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.078         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.083         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.054         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.444         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2843 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3847 ; 1.778 ; 2.029       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   338 ; 5.857 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   112 ;33.642 ;24.732       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   521 ;13.195 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;16.042 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   445 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2004 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1430 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1954 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   324 ; 0.175 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.086 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    43 ; 0.184 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    28 ; 0.149 ; 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):  1737 ; 1.070 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2748 ; 1.723 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1238 ; 2.764 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1099 ; 4.386 ; 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2ORW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041509.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SI (111) SAGITTAL FOCUSING         
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55419                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.39500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 65% 2-METHYL-2,4-PENTANEDIOL (MPD),      
REMARK 280  0.1 M NA-ACETATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       51.27500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.81500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.27500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.81500            
REMARK 290   SMTRY3   4  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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      102.55000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ILE A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     TYR A    45                                                      
REMARK 465     HIS A    53                                                      
REMARK 465     SER A    54                                                      
REMARK 465     GLY A    55                                                      
REMARK 465     ASN A    56                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     ARG A   183                                                      
REMARK 465     VAL A   184                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B    43                                                      
REMARK 465     ARG B    44                                                      
REMARK 465     TYR B    45                                                      
REMARK 465     HIS B    46                                                      
REMARK 465     SER B    47                                                      
REMARK 465     SER B    54                                                      
REMARK 465     GLY B    55                                                      
REMARK 465     ASN B    56                                                      
REMARK 465     ARG B   183                                                      
REMARK 465     VAL B   184                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS B  53    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   821     O    HOH B  1003              1.75            
REMARK 500   O    HOH A   504     O    HOH B   990              1.94            
REMARK 500   O1C  4TA B   802     O    HOH B   992              2.06            
REMARK 500   O    HOH A   537     O    HOH A   652              2.10            
REMARK 500   O3'  4TA B   801     O    HOH B   986              2.13            
REMARK 500   NE2  HIS B    61     O    HOH B   926              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 147       14.56   -147.19                                   
REMARK 500    ASP A 162       96.63   -164.18                                   
REMARK 500    ILE B  41       54.04    178.44                                   
REMARK 500    GLU B  64      -61.11    -94.42                                   
REMARK 500    ASN B 147       15.23   -148.81                                   
REMARK 500    ASP B 162       95.47   -161.92                                   
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 A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 140   SG                                                     
REMARK 620 2 CYS A 143   SG  104.2                                              
REMARK 620 3 CYS A 176   SG  102.0 117.7                                        
REMARK 620 4 CYS A 173   SG  115.4 119.9  96.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 983   O                                                      
REMARK 620 2 HOH B 911   O    87.4                                              
REMARK 620 3 THR A  17   OG1  88.8  92.7                                        
REMARK 620 4 HOH A 643   O    91.9 176.0  83.4                                  
REMARK 620 5 4TA B 801   O2D  85.3  93.5 171.3  90.3                            
REMARK 620 6 4TA B 801   O2B 173.1  87.6  86.6  92.8  99.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 140   SG                                                     
REMARK 620 2 CYS B 173   SG  113.8                                              
REMARK 620 3 CYS B 143   SG  104.3 120.7                                        
REMARK 620 4 CYS B 176   SG  104.6  95.7 117.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 4TA B 802   O2D                                                    
REMARK 620 2 HOH B 834   O    87.5                                              
REMARK 620 3 THR B  17   OG1 165.0  80.6                                        
REMARK 620 4 HOH B 992   O    98.3 173.9  94.0                                  
REMARK 620 5 HOH B 984   O    83.9  94.6  88.0  87.9                            
REMARK 620 6 4TA B 802   O2B 104.5  90.5  84.8  86.3 170.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 502                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4TA B 801                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4TA B 802                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ORV   RELATED DB: PDB                                   
REMARK 900 HUMAN THYMIDINE KINASE 1 IN COMPLEX WITH TP4A                        
DBREF  2ORW A    1   184  UNP    Q9WYN2   KITH_THEMA       1    184             
DBREF  2ORW B    1   184  UNP    Q9WYN2   KITH_THEMA       1    184             
SEQRES   1 A  184  MET SER GLY LYS LEU THR VAL ILE THR GLY PRO MET TYR          
SEQRES   2 A  184  SER GLY LYS THR THR GLU LEU LEU SER PHE VAL GLU ILE          
SEQRES   3 A  184  TYR LYS LEU GLY LYS LYS LYS VAL ALA VAL PHE LYS PRO          
SEQRES   4 A  184  LYS ILE ASP SER ARG TYR HIS SER THR MET ILE VAL SER          
SEQRES   5 A  184  HIS SER GLY ASN GLY VAL GLU ALA HIS VAL ILE GLU ARG          
SEQRES   6 A  184  PRO GLU GLU MET ARG LYS TYR ILE GLU GLU ASP THR ARG          
SEQRES   7 A  184  GLY VAL PHE ILE ASP GLU VAL GLN PHE PHE ASN PRO SER          
SEQRES   8 A  184  LEU PHE GLU VAL VAL LYS ASP LEU LEU ASP ARG GLY ILE          
SEQRES   9 A  184  ASP VAL PHE CYS ALA GLY LEU ASP LEU THR HIS LYS GLN          
SEQRES  10 A  184  ASN PRO PHE GLU THR THR ALA LEU LEU LEU SER LEU ALA          
SEQRES  11 A  184  ASP THR VAL ILE LYS LYS LYS ALA VAL CYS HIS ARG CYS          
SEQRES  12 A  184  GLY GLU TYR ASN ALA THR LEU THR LEU LYS VAL ALA GLY          
SEQRES  13 A  184  GLY GLU GLU GLU ILE ASP VAL GLY GLY GLN GLU LYS TYR          
SEQRES  14 A  184  ILE ALA VAL CYS ARG ASP CYS TYR ASN THR LEU LYS LYS          
SEQRES  15 A  184  ARG VAL                                                      
SEQRES   1 B  184  MET SER GLY LYS LEU THR VAL ILE THR GLY PRO MET TYR          
SEQRES   2 B  184  SER GLY LYS THR THR GLU LEU LEU SER PHE VAL GLU ILE          
SEQRES   3 B  184  TYR LYS LEU GLY LYS LYS LYS VAL ALA VAL PHE LYS PRO          
SEQRES   4 B  184  LYS ILE ASP SER ARG TYR HIS SER THR MET ILE VAL SER          
SEQRES   5 B  184  HIS SER GLY ASN GLY VAL GLU ALA HIS VAL ILE GLU ARG          
SEQRES   6 B  184  PRO GLU GLU MET ARG LYS TYR ILE GLU GLU ASP THR ARG          
SEQRES   7 B  184  GLY VAL PHE ILE ASP GLU VAL GLN PHE PHE ASN PRO SER          
SEQRES   8 B  184  LEU PHE GLU VAL VAL LYS ASP LEU LEU ASP ARG GLY ILE          
SEQRES   9 B  184  ASP VAL PHE CYS ALA GLY LEU ASP LEU THR HIS LYS GLN          
SEQRES  10 B  184  ASN PRO PHE GLU THR THR ALA LEU LEU LEU SER LEU ALA          
SEQRES  11 B  184  ASP THR VAL ILE LYS LYS LYS ALA VAL CYS HIS ARG CYS          
SEQRES  12 B  184  GLY GLU TYR ASN ALA THR LEU THR LEU LYS VAL ALA GLY          
SEQRES  13 B  184  GLY GLU GLU GLU ILE ASP VAL GLY GLY GLN GLU LYS TYR          
SEQRES  14 B  184  ILE ALA VAL CYS ARG ASP CYS TYR ASN THR LEU LYS LYS          
SEQRES  15 B  184  ARG VAL                                                      
HET     ZN  A 401       1                                                       
HET     ZN  B 402       1                                                       
HET     MG  A 501       1                                                       
HET     MG  B 502       1                                                       
HET    4TA  B 801      51                                                       
HET    4TA  B 802      51                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     4TA P1-(5'-ADENOSYL)P4-(5'-(2'-DEOXY-THYMIDYL))                      
HETNAM   2 4TA  TETRAPHOSPHATE                                                  
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  4TA    2(C20 H25 N7 O20 P4 4-)                                      
FORMUL   8  HOH   *370(H2 O)                                                    
HELIX    1   1 GLY A   15  GLY A   30  1                                  16    
HELIX    2   2 ARG A   65  ILE A   73  5                                   9    
HELIX    3   3 GLU A   84  PHE A   88  5                                   5    
HELIX    4   4 ASN A   89  PRO A   90  5                                   2    
HELIX    5   5 SER A   91  ARG A  102  1                                  12    
HELIX    6   6 PHE A  120  ALA A  130  1                                  11    
HELIX    7   7 CYS A  173  LYS A  181  1                                   9    
HELIX    8   8 GLY B   15  GLY B   30  1                                  16    
HELIX    9   9 ARG B   65  ILE B   73  5                                   9    
HELIX   10  10 GLU B   84  PHE B   88  5                                   5    
HELIX   11  11 ASN B   89  PRO B   90  5                                   2    
HELIX   12  12 SER B   91  ARG B  102  1                                  12    
HELIX   13  13 PHE B  120  ALA B  130  1                                  11    
HELIX   14  14 CYS B  173  LYS B  182  1                                  10    
SHEET    1   A 6 HIS A  61  ILE A  63  0                                        
SHEET    2   A 6 LYS A  33  PRO A  39  1  N  VAL A  36   O  HIS A  61           
SHEET    3   A 6 THR A  77  ILE A  82  1  O  PHE A  81   N  PHE A  37           
SHEET    4   A 6 ASP A 105  LEU A 111  1  O  PHE A 107   N  ILE A  82           
SHEET    5   A 6 LEU A   5  GLY A  10  1  N  ILE A   8   O  CYS A 108           
SHEET    6   A 6 THR A 132  LYS A 135  1  O  ILE A 134   N  VAL A   7           
SHEET    1   B 2 MET A  49  ILE A  50  0                                        
SHEET    2   B 2 VAL A  58  GLU A  59 -1  O  VAL A  58   N  ILE A  50           
SHEET    1   C 2 LEU A 150  LYS A 153  0                                        
SHEET    2   C 2 TYR A 169  VAL A 172 -1  O  ILE A 170   N  LEU A 152           
SHEET    1   D 6 HIS B  61  ILE B  63  0                                        
SHEET    2   D 6 LYS B  33  PRO B  39  1  N  VAL B  36   O  HIS B  61           
SHEET    3   D 6 THR B  77  ILE B  82  1  O  PHE B  81   N  PHE B  37           
SHEET    4   D 6 ASP B 105  LEU B 111  1  O  PHE B 107   N  VAL B  80           
SHEET    5   D 6 LEU B   5  GLY B  10  1  N  ILE B   8   O  CYS B 108           
SHEET    6   D 6 THR B 132  LYS B 135  1  O  ILE B 134   N  VAL B   7           
SHEET    1   E 2 MET B  49  ILE B  50  0                                        
SHEET    2   E 2 VAL B  58  GLU B  59 -1  O  VAL B  58   N  ILE B  50           
SHEET    1   F 2 LEU B 150  LYS B 153  0                                        
SHEET    2   F 2 TYR B 169  VAL B 172 -1  O  ILE B 170   N  LEU B 152           
LINK        ZN    ZN A 401                 SG  CYS A 140     1555   1555  2.32  
LINK        ZN    ZN A 401                 SG  CYS A 143     1555   1555  2.36  
LINK        ZN    ZN A 401                 SG  CYS A 176     1555   1555  2.36  
LINK        ZN    ZN A 401                 SG  CYS A 173     1555   1555  2.40  
LINK        MG    MG A 501                 O   HOH B 983     1555   1555  2.06  
LINK        MG    MG A 501                 O   HOH B 911     1555   1555  2.11  
LINK        MG    MG A 501                 OG1 THR A  17     1555   1555  2.09  
LINK        MG    MG A 501                 O   HOH A 643     1555   1555  2.22  
LINK        MG    MG A 501                 O2D 4TA B 801     1555   1555  1.95  
LINK        MG    MG A 501                 O2B 4TA B 801     1555   1555  2.05  
LINK        ZN    ZN B 402                 SG  CYS B 140     1555   1555  2.39  
LINK        ZN    ZN B 402                 SG  CYS B 173     1555   1555  2.37  
LINK        ZN    ZN B 402                 SG  CYS B 143     1555   1555  2.35  
LINK        ZN    ZN B 402                 SG  CYS B 176     1555   1555  2.37  
LINK        MG    MG B 502                 O2D 4TA B 802     1555   1555  1.95  
LINK        MG    MG B 502                 O   HOH B 834     1555   1555  2.43  
LINK        MG    MG B 502                 OG1 THR B  17     1555   1555  2.08  
LINK        MG    MG B 502                 O   HOH B 992     1555   1555  1.85  
LINK        MG    MG B 502                 O   HOH B 984     1555   1555  2.08  
LINK        MG    MG B 502                 O2B 4TA B 802     1555   1555  2.11  
SITE     1 AC1  4 CYS A 140  CYS A 143  CYS A 173  CYS A 176                    
SITE     1 AC2  4 CYS B 140  CYS B 143  CYS B 173  CYS B 176                    
SITE     1 AC3  5 THR A  17  HOH A 643  4TA B 801  HOH B 911                    
SITE     2 AC3  5 HOH B 983                                                     
SITE     1 AC4  5 THR B  17  4TA B 802  HOH B 834  HOH B 984                    
SITE     2 AC4  5 HOH B 992                                                     
SITE     1 AC5 38 MET A  12  TYR A  13  SER A  14  GLY A  15                    
SITE     2 AC5 38 LYS A  16  THR A  17  THR A  18  GLU A  84                    
SITE     3 AC5 38 PHE A  87  LEU A 111  THR A 114  HIS A 115                    
SITE     4 AC5 38 ALA A 138  VAL A 139  THR A 151  GLU A 160                    
SITE     5 AC5 38 ASP A 162  VAL A 163  GLY A 164  TYR A 169                    
SITE     6 AC5 38  MG A 501  HOH A 535  HOH A 545  HOH A 643                    
SITE     7 AC5 38 GLU B  25  LEU B  29  HOH B 807  HOH B 810                    
SITE     8 AC5 38 HOH B 833  HOH B 911  HOH B 921  HOH B 935                    
SITE     9 AC5 38 HOH B 955  HOH B 961  HOH B 983  HOH B 986                    
SITE    10 AC5 38 HOH B 998  HOH B1001                                          
SITE     1 AC6 35 GLU A  25  LEU A  29  MET B  12  TYR B  13                    
SITE     2 AC6 35 SER B  14  GLY B  15  LYS B  16  THR B  17                    
SITE     3 AC6 35 THR B  18  SER B  52  GLU B  84  GLN B  86                    
SITE     4 AC6 35 PHE B  87  LEU B 111  THR B 114  HIS B 115                    
SITE     5 AC6 35 ALA B 138  VAL B 139  THR B 151  GLU B 160                    
SITE     6 AC6 35 ASP B 162  VAL B 163  GLY B 164  TYR B 169                    
SITE     7 AC6 35  MG B 502  HOH B 827  HOH B 834  HOH B 838                    
SITE     8 AC6 35 HOH B 919  HOH B 934  HOH B 965  HOH B 974                    
SITE     9 AC6 35 HOH B 984  HOH B 992  HOH B 995                               
CRYST1  102.550   59.630   61.440  90.00 103.11  90.00 C 1 2 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      0.009751  0.000000  0.002271        0.00000                         
SCALE2      0.000000  0.016770  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016712        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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