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Database: PDB
Entry: 2IRX
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Original site: 2IRX 
HEADER    TRANSFERASE                             16-OCT-06   2IRX              
TITLE     CRYSTAL STRUCTURE OF THE POLYMERASE DOMAIN FROM MYCOBACTERIUM         
TITLE    2 TUBERCULOSIS LIGASE D WITH GTP AND MANGANESE.                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA LIGASE-LIKE PROTEIN RV0938/MT0965;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGD POLYMERASE DOMAIN (RESIDUES 1-300);                   
COMPND   5 EC: 2.7.7.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: RV0938;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    POLYMERASE, PRIMASE, LIGASE, NHEJ, GTP, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.C.BRISSETT,R.S.PITCHER,A.J.DOHERTY                                  
REVDAT   4   13-JUL-11 2IRX    1       VERSN                                    
REVDAT   3   24-FEB-09 2IRX    1       VERSN                                    
REVDAT   2   30-OCT-07 2IRX    1       JRNL                                     
REVDAT   1   02-JAN-07 2IRX    0                                                
JRNL        AUTH   R.S.PITCHER,N.C.BRISSETT,A.J.PICHER,P.ANDRADE,R.JUAREZ,      
JRNL        AUTH 2 D.THOMPSON,G.C.FOX,L.BLANCO,A.J.DOHERTY                      
JRNL        TITL   STRUCTURE AND FUNCTION OF A MYCOBACTERIAL NHEJ DNA REPAIR    
JRNL        TITL 2 POLYMERASE.                                                  
JRNL        REF    J.MOL.BIOL.                   V. 366   391 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17174332                                                     
JRNL        DOI    10.1016/J.JMB.2006.10.046                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 25666                          
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1360                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1476                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.3940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2164                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 327                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 21.31                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.39000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : -0.38000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.122         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.121         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.075         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.321         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2248 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3078 ; 1.429 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   282 ; 6.007 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;33.435 ;22.556       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   347 ;14.203 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;21.390 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   353 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1696 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1115 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1500 ; 0.299 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   245 ; 0.155 ; 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):    36 ; 0.177 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    18 ; 0.176 ; 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):  1455 ; 0.795 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2281 ; 1.216 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   927 ; 1.996 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   797 ; 3.017 ; 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  : 9                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A    19                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6163  15.3522  -5.4902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0268 T22:   0.0740                                     
REMARK   3      T33:   0.0749 T12:  -0.0266                                     
REMARK   3      T13:  -0.0176 T23:  -0.0400                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7196 L22:   8.1576                                     
REMARK   3      L33:  12.7579 L12:   0.8714                                     
REMARK   3      L13:  -1.7429 L23:  -7.1104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1221 S12:   0.3110 S13:  -0.0320                       
REMARK   3      S21:  -0.5941 S22:   0.2582 S23:   0.2143                       
REMARK   3      S31:   0.2601 S32:  -0.1568 S33:  -0.1361                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    20        A    80                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3611  25.5495  -0.2749              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0324 T22:   0.0726                                     
REMARK   3      T33:   0.0557 T12:  -0.0010                                     
REMARK   3      T13:  -0.0081 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7237 L22:   0.9206                                     
REMARK   3      L33:   0.8030 L12:   0.2819                                     
REMARK   3      L13:  -0.3183 L23:   0.0088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0347 S12:   0.0846 S13:  -0.0478                       
REMARK   3      S21:  -0.0923 S22:   0.0384 S23:  -0.0046                       
REMARK   3      S31:  -0.0101 S32:   0.0044 S33:  -0.0036                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    81        A    90                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8658  37.9889 -10.6655              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0154 T22:   0.1210                                     
REMARK   3      T33:   0.1059 T12:  -0.0871                                     
REMARK   3      T13:  -0.0027 T23:   0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.0026 L22:  16.3843                                     
REMARK   3      L33:   8.1551 L12:   0.9563                                     
REMARK   3      L13:   1.2982 L23:   1.5752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8370 S12:  -0.2532 S13:   1.2743                       
REMARK   3      S21:  -0.0540 S22:   0.3870 S23:  -1.7506                       
REMARK   3      S31:  -0.7821 S32:   1.2091 S33:   0.4501                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    91        A   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.0047  31.7227  -5.0174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0447 T22:   0.0775                                     
REMARK   3      T33:   0.0468 T12:  -0.0066                                     
REMARK   3      T13:  -0.0007 T23:   0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2668 L22:   1.5219                                     
REMARK   3      L33:   0.7739 L12:   0.5369                                     
REMARK   3      L13:  -0.2127 L23:   0.0887                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0334 S12:   0.1600 S13:   0.0161                       
REMARK   3      S21:  -0.1401 S22:   0.0385 S23:   0.0462                       
REMARK   3      S31:  -0.1351 S32:  -0.0083 S33:  -0.0051                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   121        A   162                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7998  46.0639   6.7834              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1471 T22:   0.0442                                     
REMARK   3      T33:   0.1142 T12:   0.0021                                     
REMARK   3      T13:   0.0086 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6879 L22:   2.0604                                     
REMARK   3      L33:   2.8572 L12:   0.2032                                     
REMARK   3      L13:  -0.2058 L23:   0.7747                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1042 S12:  -0.0101 S13:   0.1782                       
REMARK   3      S21:  -0.2016 S22:   0.0091 S23:   0.0386                       
REMARK   3      S31:  -0.2703 S32:   0.0898 S33:  -0.1132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   163        A   192                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6967  48.0968   6.9439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1430 T22:   0.0142                                     
REMARK   3      T33:   0.0714 T12:   0.0334                                     
REMARK   3      T13:   0.0056 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3321 L22:   1.5144                                     
REMARK   3      L33:   1.8296 L12:   1.0275                                     
REMARK   3      L13:  -0.7171 L23:   0.7983                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1173 S12:   0.1331 S13:   0.3719                       
REMARK   3      S21:  -0.2016 S22:  -0.0001 S23:   0.2835                       
REMARK   3      S31:  -0.5610 S32:  -0.0646 S33:  -0.1171                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   193        A   227                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.7185  51.2897  15.9367              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0523 T22:   0.0462                                     
REMARK   3      T33:   0.0701 T12:  -0.0295                                     
REMARK   3      T13:   0.0201 T23:  -0.0328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7343 L22:   2.9191                                     
REMARK   3      L33:   9.8329 L12:   0.9637                                     
REMARK   3      L13:   0.8598 L23:   0.5047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0154 S12:  -0.0526 S13:   0.0540                       
REMARK   3      S21:  -0.2308 S22:   0.0809 S23:  -0.3250                       
REMARK   3      S31:   0.0701 S32:   0.5863 S33:  -0.0655                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   228        A   268                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3961  38.1440  11.2135              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0569 T22:   0.0617                                     
REMARK   3      T33:   0.0420 T12:   0.0012                                     
REMARK   3      T13:   0.0084 T23:  -0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7653 L22:   1.6990                                     
REMARK   3      L33:   0.7904 L12:   0.3325                                     
REMARK   3      L13:  -0.0048 L23:   0.3821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0373 S12:  -0.1518 S13:   0.0598                       
REMARK   3      S21:   0.1011 S22:  -0.0380 S23:   0.0772                       
REMARK   3      S31:  -0.1247 S32:   0.0311 S33:   0.0007                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   269        A   292                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.0192  34.8422   8.3037              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0226 T22:   0.0814                                     
REMARK   3      T33:   0.0806 T12:   0.0266                                     
REMARK   3      T13:   0.0041 T23:  -0.0383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2820 L22:   1.9387                                     
REMARK   3      L33:   1.8386 L12:   0.7145                                     
REMARK   3      L13:  -0.4728 L23:   0.1163                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0273 S12:  -0.0435 S13:   0.1956                       
REMARK   3      S21:  -0.0146 S22:  -0.0348 S23:   0.3134                       
REMARK   3      S31:  -0.1546 S32:  -0.3869 S33:   0.0621                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2IRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039940.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54180                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27079                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.700                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 9.000                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.47800                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA HEPES, 0.01M MNCL2, 10%(V/V)     
REMARK 280  ISO-PROPANOL, 20% PEG 4000, 0.01M GTP, PH 7.5, VAPOR DIFFUSION,     
REMARK 280  HANGING DROP, TEMPERATURE 285K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       21.27850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.75900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.76600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.75900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.27850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.76600            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     PRO A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     ALA A   297                                                      
REMARK 465     ASP A   298                                                      
REMARK 465     ARG A   299                                                      
REMARK 465     LEU A   300                                                      
REMARK 465     THR A   301                                                      
REMARK 465     ARG A   302                                                      
REMARK 465     TYR A   303                                                      
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    LYS A  69      -63.25   -103.69                                   
REMARK 500    ASP A  97       18.22   -143.86                                   
REMARK 500    SER A 177      -97.24   -118.10                                   
REMARK 500    THR A 219      119.43    -39.26                                   
REMARK 500    TYR A 244       -9.20     78.83                                   
REMARK 500    ALA A 255       86.50    -69.88                                   
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                              MN A 304  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 140   OD1                                                    
REMARK 620 2 ASP A 142   OD1  92.9                                              
REMARK 620 3 GTP A 305   O1B  89.3 177.0                                        
REMARK 620 4 GTP A 305   O2G 166.8  89.2  88.2                                  
REMARK 620 5 HOH A 583   O   102.2  86.1  95.4  90.9                            
REMARK 620 6 HOH A 584   O    77.4  87.4  91.1  89.8 173.5                      
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 MN A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 305                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2IRU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE POLYMERASE DOMAIN FROM                      
REMARK 900 MYCOBACTERIUM TUBERCULOSIS LIGASE D                                  
REMARK 900 RELATED ID: 2IRY   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DGTP                                 
DBREF  2IRX A    4   303  UNP    P71571   Y938_MYCTU       1    300             
SEQADV 2IRX GLY A    1  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRX SER A    2  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRX HIS A    3  UNP  P71571              EXPRESSION TAG                 
SEQRES   1 A  303  GLY SER HIS MET GLY SER ALA SER GLU GLN ARG VAL THR          
SEQRES   2 A  303  LEU THR ASN ALA ASP LYS VAL LEU TYR PRO ALA THR GLY          
SEQRES   3 A  303  THR THR LYS SER ASP ILE PHE ASP TYR TYR ALA GLY VAL          
SEQRES   4 A  303  ALA GLU VAL MET LEU GLY HIS ILE ALA GLY ARG PRO ALA          
SEQRES   5 A  303  THR ARG LYS ARG TRP PRO ASN GLY VAL ASP GLN PRO ALA          
SEQRES   6 A  303  PHE PHE GLU LYS GLN LEU ALA LEU SER ALA PRO PRO TRP          
SEQRES   7 A  303  LEU SER ARG ALA THR VAL ALA HIS ARG SER GLY THR THR          
SEQRES   8 A  303  THR TYR PRO ILE ILE ASP SER ALA THR GLY LEU ALA TRP          
SEQRES   9 A  303  ILE ALA GLN GLN ALA ALA LEU GLU VAL HIS VAL PRO GLN          
SEQRES  10 A  303  TRP ARG PHE VAL ALA GLU PRO GLY SER GLY GLU LEU ASN          
SEQRES  11 A  303  PRO GLY PRO ALA THR ARG LEU VAL PHE ASP LEU ASP PRO          
SEQRES  12 A  303  GLY GLU GLY VAL MET MET ALA GLN LEU ALA GLU VAL ALA          
SEQRES  13 A  303  ARG ALA VAL ARG ASP LEU LEU ALA ASP ILE GLY LEU VAL          
SEQRES  14 A  303  THR PHE PRO VAL THR SER GLY SER LYS GLY LEU HIS LEU          
SEQRES  15 A  303  TYR THR PRO LEU ASP GLU PRO VAL SER SER ARG GLY ALA          
SEQRES  16 A  303  THR VAL LEU ALA LYS ARG VAL ALA GLN ARG LEU GLU GLN          
SEQRES  17 A  303  ALA MET PRO ALA LEU VAL THR SER THR MET THR LYS SER          
SEQRES  18 A  303  LEU ARG ALA GLY LYS VAL PHE VAL ASP TRP SER GLN ASN          
SEQRES  19 A  303  SER GLY SER LYS THR THR ILE ALA PRO TYR SER LEU ARG          
SEQRES  20 A  303  GLY ARG THR HIS PRO THR VAL ALA ALA PRO ARG THR TRP          
SEQRES  21 A  303  ALA GLU LEU ASP ASP PRO ALA LEU ARG GLN LEU SER TYR          
SEQRES  22 A  303  ASP GLU VAL LEU THR ARG ILE ALA ARG ASP GLY ASP LEU          
SEQRES  23 A  303  LEU GLU ARG LEU ASP ALA ASP ALA PRO VAL ALA ASP ARG          
SEQRES  24 A  303  LEU THR ARG TYR                                              
HET     MN  A 304       1                                                       
HET    GTP  A 305      32                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
FORMUL   2   MN    MN 2+                                                        
FORMUL   3  GTP    C10 H16 N5 O14 P3                                            
FORMUL   4  HOH   *327(H2 O)                                                    
HELIX    1   1 THR A   28  ALA A   48  1                                  21    
HELIX    2   2 SER A   98  GLN A  108  1                                  11    
HELIX    3   3 MET A  148  ASP A  165  1                                  18    
HELIX    4   4 SER A  191  MET A  210  1                                  20    
HELIX    5   5 THR A  219  ARG A  223  5                                   5    
HELIX    6   6 TRP A  231  SER A  235  5                                   5    
HELIX    7   7 ALA A  261  ASP A  265  5                                   5    
HELIX    8   8 TYR A  273  GLY A  284  1                                  12    
SHEET    1   A 4 PHE A  66  GLU A  68  0                                        
SHEET    2   A 4 THR A  53  ARG A  56 -1  N  ARG A  54   O  GLU A  68           
SHEET    3   A 4 GLU A 112  VAL A 115 -1  O  HIS A 114   N  THR A  53           
SHEET    4   A 4 THR A 240  ILE A 241 -1  O  THR A 240   N  VAL A 115           
SHEET    1   B 2 SER A  80  ALA A  85  0                                        
SHEET    2   B 2 THR A  90  ILE A  95 -1  O  THR A  91   N  VAL A  84           
SHEET    1   C 4 TRP A 118  ALA A 122  0                                        
SHEET    2   C 4 LEU A 129  PRO A 143 -1  O  ASN A 130   N  VAL A 121           
SHEET    3   C 4 VAL A 227  ASP A 230 -1  O  ASP A 230   N  ASP A 140           
SHEET    4   C 4 VAL A 214  THR A 215  1  N  THR A 215   O  VAL A 229           
SHEET    1   D 5 TRP A 118  ALA A 122  0                                        
SHEET    2   D 5 LEU A 129  PRO A 143 -1  O  ASN A 130   N  VAL A 121           
SHEET    3   D 5 LEU A 180  VAL A 190 -1  O  VAL A 190   N  ALA A 134           
SHEET    4   D 5 PHE A 171  THR A 174 -1  N  VAL A 173   O  HIS A 181           
SHEET    5   D 5 ALA A 256  PRO A 257 -1  O  ALA A 256   N  THR A 174           
SHEET    1   E 2 THR A 253  VAL A 254  0                                        
SHEET    2   E 2 LEU A 271  SER A 272 -1  O  LEU A 271   N  VAL A 254           
LINK         OD1 ASP A 140                MN    MN A 304     1555   1555  2.20  
LINK         OD1 ASP A 142                MN    MN A 304     1555   1555  2.16  
LINK        MN    MN A 304                 O1B GTP A 305     1555   1555  2.26  
LINK        MN    MN A 304                 O2G GTP A 305     1555   1555  2.20  
LINK        MN    MN A 304                 O   HOH A 583     1555   1555  2.17  
LINK        MN    MN A 304                 O   HOH A 584     1555   1555  2.51  
SITE     1 AC1  5 ASP A 140  ASP A 142  GTP A 305  HOH A 583                    
SITE     2 AC1  5 HOH A 584                                                     
SITE     1 AC2 28 LYS A  55  PHE A  67  HIS A 114  ASP A 140                    
SITE     2 AC2 28 ASP A 142  SER A 175  SER A 177  LYS A 178                    
SITE     3 AC2 28 GLY A 179  HIS A 181  GLN A 233  THR A 239                    
SITE     4 AC2 28 ARG A 247  ARG A 249   MN A 304  HOH A 431                    
SITE     5 AC2 28 HOH A 475  HOH A 481  HOH A 580  HOH A 581                    
SITE     6 AC2 28 HOH A 582  HOH A 584  HOH A 585  HOH A 586                    
SITE     7 AC2 28 HOH A 591  HOH A 593  HOH A 597  HOH A 617                    
CRYST1   42.557   75.532   89.518  90.00  90.00  90.00 P 21 21 21    4          
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      0.023498  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013239  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011171        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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