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Database: PDB
Entry: 1N5L
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HEADER    TRANSFERASE                             06-NOV-02   1N5L              
TITLE     CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS THYMIDYLATE KINASE    
TITLE    2 CRYSTALLIZED IN SODIUM MALONATE, AFTER CATALYSIS IN THE CRYSTAL (2.3 
TITLE    3 A RESOLUTION)                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDYLATE KINASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.4.9;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    TRANSFERASE (ATP:TMP PHOSPHOTRANSFERASE), KINASE, TRANSFERASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.FIORAVANTI,A.HAOUZ,T.URSBY,H.MUNIER-LEHMANN,M.DELARUE,D.BOURGEOIS   
REVDAT   4   14-FEB-24 1N5L    1       REMARK                                   
REVDAT   3   31-JAN-18 1N5L    1       REMARK                                   
REVDAT   2   24-FEB-09 1N5L    1       VERSN                                    
REVDAT   1   15-APR-03 1N5L    0                                                
JRNL        AUTH   E.FIORAVANTI,A.HAOUZ,T.URSBY,H.MUNIER-LEHMANN,M.DELARUE,     
JRNL        AUTH 2 D.BOURGEOIS                                                  
JRNL        TITL   MYCOBACTERIUM TUBERCULOSIS THYMIDYLATE KINASE: STRUCTURAL    
JRNL        TITL 2 STUDIES OF INTERMEDIATES ALONG THE REACTION PATHWAY          
JRNL        REF    J.MOL.BIOL.                   V. 375  1077 2003              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12662932                                                     
JRNL        DOI    10.1016/S0022-2836(03)00202-X                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.URSBY,M.WEIK,E.FIORAVANTI,M.DELARUE,M.GOELDNER,D.BOURGEOIS 
REMARK   1  TITL   CRYO-PHOTOLYSIS OF CAGED COMPOUNDS: A TECHNIQUE FOR TRAPPING 
REMARK   1  TITL 2 INTERMEDIATE STATES IN PROTEIN CRYSTALS                      
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  58   607 2002              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444902002135                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   I.LI DE LA SIERRA,H.MUNIER-LEHMANN,A.M.GILLES,O.BARZU,       
REMARK   1  AUTH 2 M.DELARUE                                                    
REMARK   1  TITL   X-RAY STRUCTURE OF TMP KINASE FROM MYCOBACTERIUM             
REMARK   1  TITL 2 TUBERCULOSIS COMPLEXED WITH TMP AT 1.95 A RESOLUTION         
REMARK   1  REF    J.MOL.BIOL.                   V. 311    87 2001              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.2001.4843                                       
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   I.LI DE LA SIERRA,H.MUNIER-LEHMANN,A.M.GILLES,O.BARZU,       
REMARK   1  AUTH 2 M.DELARUE                                                    
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF THE        
REMARK   1  TITL 2 THYMIDYLATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS           
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  56   226 2000              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444999016212                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1848944.310                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 21577                          
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 SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1054                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3345                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 165                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.024                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2905                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 205                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.08000                                              
REMARK   3    B22 (A**2) : 6.08000                                              
REMARK   3    B33 (A**2) : -12.17000                                            
REMARK   3    B12 (A**2) : 4.70000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : -0.0                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.090                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.410 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.310 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.060 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.320 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 63.18                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : TMP+TDP+ACT+DPO.PAR                            
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : TMP+TDP+ACT+DPO.TOP                            
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MONOMER A CONTAINS THE APO-STRUCTURE.     
REMARK   3  MONOMER B CONTAINS THE TDP-MG++-ADP COMPLEX.                        
REMARK   4                                                                      
REMARK   4 1N5L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000017546.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.936                              
REMARK 200  MONOCHROMATOR                  : SILICON                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21648                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.760                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: CNS 1.0                                               
REMARK 200 STARTING MODEL: PDB ENTRY 1N5K                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM MALONATE, 2% PEG 2000,      
REMARK 280  0.1 M MES PH 6.0, 2 MM B-MERCAPTOETHANOL, 25 MM MAGNESIUM           
REMARK 280  ACETATE, SOAKING IN 30 MM ATP, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  STREAK SEEDING, SOAKING, TEMPERATURE 293.0K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.29967            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      130.59933            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      130.59933            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       65.29967            
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS THE FUNCTIONAL DIMER.           
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   150                                                      
REMARK 465     ARG A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     ARG A   153                                                      
REMARK 465     ALA A   154                                                      
REMARK 465     GLN A   155                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     ASP A   157                                                      
REMARK 465     PRO A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     ARG A   160                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     ARG A   162                                                      
REMARK 465     PRO A   209                                                      
REMARK 465     PRO A   210                                                      
REMARK 465     ASP A   211                                                      
REMARK 465     VAL A   212                                                      
REMARK 465     PRO A   213                                                      
REMARK 465     SER A   214                                                      
REMARK 465     GLN B   155                                                      
REMARK 465     ARG B   156                                                      
REMARK 465     ASP B   157                                                      
REMARK 465     PRO B   158                                                      
REMARK 465     GLY B   159                                                      
REMARK 465     PRO B   209                                                      
REMARK 465     PRO B   210                                                      
REMARK 465     ASP B   211                                                      
REMARK 465     VAL B   212                                                      
REMARK 465     PRO B   213                                                      
REMARK 465     SER B   214                                                      
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     ASP A   9    CG   OD1  OD2                                       
REMARK 470     ARG A  14    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A  55    OE1  OE2                                            
REMARK 470     GLU A 144    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 148    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 164    CG   OD1  ND2                                       
REMARK 470     GLU A 166    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 167    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 171    CG   CD1  CD2                                       
REMARK 470     ARG A 190    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 167    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 190    CG   CD   NE   CZ   NH1  NH2                        
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   NH1  ARG B   151     O    HOH B   455              2.06            
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    ARG A  95      128.97     79.02                                   
REMARK 500    TYR A  96     -153.06   -142.54                                   
REMARK 500    ALA A 196        0.79    -64.45                                   
REMARK 500    ARG B  95      145.43     78.56                                   
REMARK 500    TYR B  96     -158.24   -160.06                                   
REMARK 500    ASN B 111     -165.24   -111.95                                   
REMARK 500    ASP B 197       35.32    -91.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN HOH MOLECULES 140 AND 141 WERE BOTH NAMED 140 IN THE       
REMARK 600 PAPER BECAUSE THEY OCCUPY THE SAME SITE IN THE 2 MONOMERS (A AND     
REMARK 600 B), IN ORDER TO MAKE AN EASIER COMPARISON OF THE ACTIVE SITES.       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     DPO B  414                                                       
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                              MG B 215  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B   9   OD1                                                    
REMARK 620 2 TYD B 216   O2B 163.4                                              
REMARK 620 3 TYD B 216   O2A  89.1  83.9                                        
REMARK 620 4 HOH B 469   O    72.6  92.3  89.7                                  
REMARK 620 5 HOH B 502   O    88.8 102.2  67.7 151.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 215                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TYD B 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPO B 414                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1N5K   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS THYMIDYLATE KINASE   
REMARK 900 CRYSTALLIZED IN SODIUM MALONATE (2.1 A RESOLUTION)                   
REMARK 900 RELATED ID: 1GTV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS THYMIDYLATE KINASE   
REMARK 900 COMPLEXED WITH THYMIDINE-5'-DIPHOSPHATE (TDP)                        
REMARK 900 RELATED ID: 1N5I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF INACTIVE MYCOBACTERIUM TUBERCULOSIS             
REMARK 900 THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE (TMP) AT   
REMARK 900 PH 4.6 (RESOLUTION 1.85 A)                                           
REMARK 900 RELATED ID: 1N5J   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS THYMIDYLATE KINASE   
REMARK 900 COMPLEXED WITH THYMIDINE DIPHOSPHATE (TDP) AND THYMIDINE             
REMARK 900 TRIPHOSPHATE (TTP) AT PH 5.4 (RESOLUTION 1.85 A)                     
DBREF  1N5L A    1   214  UNP    O05891   KTHY_MYCTU       1    214             
DBREF  1N5L B    1   214  PDB    1N5L     1N5L             1    214             
SEQRES   1 A  214  MET LEU ILE ALA ILE GLU GLY VAL ASP GLY ALA GLY LYS          
SEQRES   2 A  214  ARG THR LEU VAL GLU LYS LEU SER GLY ALA PHE ARG ALA          
SEQRES   3 A  214  ALA GLY ARG SER VAL ALA THR LEU ALA PHE PRO ARG TYR          
SEQRES   4 A  214  GLY GLN SER VAL ALA ALA ASP ILE ALA ALA GLU ALA LEU          
SEQRES   5 A  214  HIS GLY GLU HIS GLY ASP LEU ALA SER SER VAL TYR ALA          
SEQRES   6 A  214  MET ALA THR LEU PHE ALA LEU ASP ARG ALA GLY ALA VAL          
SEQRES   7 A  214  HIS THR ILE GLN GLY LEU CYS ARG GLY TYR ASP VAL VAL          
SEQRES   8 A  214  ILE LEU ASP ARG TYR VAL ALA SER ASN ALA ALA TYR SER          
SEQRES   9 A  214  ALA ALA ARG LEU HIS GLU ASN ALA ALA GLY LYS ALA ALA          
SEQRES  10 A  214  ALA TRP VAL GLN ARG ILE GLU PHE ALA ARG LEU GLY LEU          
SEQRES  11 A  214  PRO LYS PRO ASP TRP GLN VAL LEU LEU ALA VAL SER ALA          
SEQRES  12 A  214  GLU LEU ALA GLY GLU ARG SER ARG GLY ARG ALA GLN ARG          
SEQRES  13 A  214  ASP PRO GLY ARG ALA ARG ASP ASN TYR GLU ARG ASP ALA          
SEQRES  14 A  214  GLU LEU GLN GLN ARG THR GLY ALA VAL TYR ALA GLU LEU          
SEQRES  15 A  214  ALA ALA GLN GLY TRP GLY GLY ARG TRP LEU VAL VAL GLY          
SEQRES  16 A  214  ALA ASP VAL ASP PRO GLY ARG LEU ALA ALA THR LEU ALA          
SEQRES  17 A  214  PRO PRO ASP VAL PRO SER                                      
SEQRES   1 B  214  MET LEU ILE ALA ILE GLU GLY VAL ASP GLY ALA GLY LYS          
SEQRES   2 B  214  ARG THR LEU VAL GLU LYS LEU SER GLY ALA PHE ARG ALA          
SEQRES   3 B  214  ALA GLY ARG SER VAL ALA THR LEU ALA PHE PRO ARG TYR          
SEQRES   4 B  214  GLY GLN SER VAL ALA ALA ASP ILE ALA ALA GLU ALA LEU          
SEQRES   5 B  214  HIS GLY GLU HIS GLY ASP LEU ALA SER SER VAL TYR ALA          
SEQRES   6 B  214  MET ALA THR LEU PHE ALA LEU ASP ARG ALA GLY ALA VAL          
SEQRES   7 B  214  HIS THR ILE GLN GLY LEU CYS ARG GLY TYR ASP VAL VAL          
SEQRES   8 B  214  ILE LEU ASP ARG TYR VAL ALA SER ASN ALA ALA TYR SER          
SEQRES   9 B  214  ALA ALA ARG LEU HIS GLU ASN ALA ALA GLY LYS ALA ALA          
SEQRES  10 B  214  ALA TRP VAL GLN ARG ILE GLU PHE ALA ARG LEU GLY LEU          
SEQRES  11 B  214  PRO LYS PRO ASP TRP GLN VAL LEU LEU ALA VAL SER ALA          
SEQRES  12 B  214  GLU LEU ALA GLY GLU ARG SER ARG GLY ARG ALA GLN ARG          
SEQRES  13 B  214  ASP PRO GLY ARG ALA ARG ASP ASN TYR GLU ARG ASP ALA          
SEQRES  14 B  214  GLU LEU GLN GLN ARG THR GLY ALA VAL TYR ALA GLU LEU          
SEQRES  15 B  214  ALA ALA GLN GLY TRP GLY GLY ARG TRP LEU VAL VAL GLY          
SEQRES  16 B  214  ALA ASP VAL ASP PRO GLY ARG LEU ALA ALA THR LEU ALA          
SEQRES  17 B  214  PRO PRO ASP VAL PRO SER                                      
HET    ACT  A 412       4                                                       
HET    ACT  A 413       4                                                       
HET    TMP  A 409      21                                                       
HET     MG  B 215       1                                                       
HET    TYD  B 216      25                                                       
HET    DPO  B 414       8                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     TMP THYMIDINE-5'-PHOSPHATE                                           
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     TYD THYMIDINE-5'-DIPHOSPHATE                                         
HETNAM     DPO DIPHOSPHATE                                                      
FORMUL   3  ACT    2(C2 H3 O2 1-)                                               
FORMUL   5  TMP    C10 H15 N2 O8 P                                              
FORMUL   6   MG    MG 2+                                                        
FORMUL   7  TYD    C10 H16 N2 O11 P2                                            
FORMUL   8  DPO    O7 P2 4-                                                     
FORMUL   9  HOH   *205(H2 O)                                                    
HELIX    1   1 GLY A   12  ALA A   27  1                                  16    
HELIX    2   2 SER A   42  HIS A   53  1                                  12    
HELIX    3   3 ASP A   58  SER A   61  5                                   4    
HELIX    4   4 SER A   62  GLY A   76  1                                  15    
HELIX    5   5 ALA A   77  TYR A   88  1                                  12    
HELIX    6   6 TYR A   96  HIS A  109  1                                  14    
HELIX    7   7 GLY A  114  PHE A  125  1                                  12    
HELIX    8   8 SER A  142  ARG A  149  1                                   8    
HELIX    9   9 ASP A  168  GLY A  186  1                                  19    
HELIX   10  10 ASP A  199  ALA A  208  1                                  10    
HELIX   11  11 GLY B   12  ALA B   27  1                                  16    
HELIX   12  12 SER B   42  HIS B   53  1                                  12    
HELIX   13  13 ASP B   58  SER B   61  5                                   4    
HELIX   14  14 SER B   62  GLY B   76  1                                  15    
HELIX   15  15 ALA B   77  TYR B   88  1                                  12    
HELIX   16  16 TYR B   96  LEU B  108  1                                  13    
HELIX   17  17 GLY B  114  ALA B  126  1                                  13    
HELIX   18  18 SER B  142  ARG B  153  1                                  12    
HELIX   19  19 ASP B  168  GLN B  185  1                                  18    
HELIX   20  20 ASP B  199  ALA B  208  1                                  10    
SHEET    1   A 5 VAL A  31  ALA A  35  0                                        
SHEET    2   A 5 VAL A  90  ASP A  94  1  O  ILE A  92   N  ALA A  32           
SHEET    3   A 5 LEU A   2  GLU A   6  1  N  ILE A   3   O  LEU A  93           
SHEET    4   A 5 TRP A 135  LEU A 139  1  O  VAL A 137   N  ALA A   4           
SHEET    5   A 5 ARG A 190  VAL A 194  1  O  VAL A 194   N  LEU A 138           
SHEET    1   B 5 VAL B  31  ALA B  35  0                                        
SHEET    2   B 5 VAL B  90  ASP B  94  1  O  ILE B  92   N  ALA B  32           
SHEET    3   B 5 LEU B   2  GLU B   6  1  N  ILE B   5   O  LEU B  93           
SHEET    4   B 5 TRP B 135  LEU B 139  1  O  TRP B 135   N  ALA B   4           
SHEET    5   B 5 TRP B 191  VAL B 194  1  O  VAL B 194   N  LEU B 138           
LINK         OD1 ASP B   9                MG    MG B 215     1555   1555  2.32  
LINK        MG    MG B 215                 O2B TYD B 216     1555   1555  2.24  
LINK        MG    MG B 215                 O2A TYD B 216     1555   1555  1.96  
LINK        MG    MG B 215                 O   HOH B 469     1555   1555  2.80  
LINK        MG    MG B 215                 O   HOH B 502     1555   1555  2.99  
CISPEP   1 PHE A   36    PRO A   37          0        -0.15                     
CISPEP   2 PHE B   36    PRO B   37          0         0.08                     
SITE     1 AC1  5 ASP B   9  GLU B 166  TYD B 216  HOH B 469                    
SITE     2 AC1  5 HOH B 502                                                     
SITE     1 AC2  3 ARG A 122  ARG A 127  ASN B 111                               
SITE     1 AC3  4 GLY A  10  ALA A  11  GLY A  12  LYS A  13                    
SITE     1 AC4 10 PRO A  37  TYR A  39  PHE A  70  ARG A  74                    
SITE     2 AC4 10 ARG A  95  ASN A 100  TYR A 103  TYR A 165                    
SITE     3 AC4 10 HOH A 434  HOH A 492                                          
SITE     1 AC5 17 ASP B   9  PHE B  36  PRO B  37  TYR B  39                    
SITE     2 AC5 17 LEU B  52  PHE B  70  ARG B  74  ARG B  95                    
SITE     3 AC5 17 SER B  99  ASN B 100  TYR B 103  TYR B 165                    
SITE     4 AC5 17  MG B 215  HOH B 415  HOH B 427  HOH B 469                    
SITE     5 AC5 17 HOH B 502                                                     
SITE     1 AC6  7 GLY B  10  ALA B  11  GLY B  12  LYS B  13                    
SITE     2 AC6  7 ARG B  14  THR B  15  HOH B 502                               
CRYST1   64.454   64.454  195.899  90.00  90.00 120.00 P 31 2 1     12          
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      0.015515  0.008958  0.000000        0.00000                         
SCALE2      0.000000  0.017915  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005105        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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