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Entry: 2IRY
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HEADER    TRANSFERASE                             16-OCT-06   2IRY              
TITLE     CRYSTAL STRUCTURE OF THE POLYMERASE DOMAIN FROM MYCOBACTERIUM         
TITLE    2 TUBERCULOSIS LIGASE D WITH DGTP AND MANGANESE.                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA LIGASE-LIKE PROTEIN RV0938/MT0965;                     
COMPND   3 CHAIN: A, B;                                                         
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, DGTP, TRANSFERASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.C.BRISSETT,R.S.PITCHER,A.J.DOHERTY                                  
REVDAT   4   13-JUL-11 2IRY    1       VERSN                                    
REVDAT   3   24-FEB-09 2IRY    1       VERSN                                    
REVDAT   2   30-OCT-07 2IRY    1       JRNL                                     
REVDAT   1   02-JAN-07 2IRY    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.    1.78 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) : 1.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 53660                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2868                            
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) : 1.78                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.83                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3931                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 188                          
REMARK   3   BIN FREE R VALUE                    : 0.3280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4362                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 53                                      
REMARK   3   SOLVENT ATOMS            : 659                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 20.26                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.40000                                              
REMARK   3    B22 (A**2) : -0.20000                                             
REMARK   3    B33 (A**2) : -0.22000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.17000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.129         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.128         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.806         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4526 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6194 ; 1.414 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   573 ; 5.987 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   183 ;34.396 ;22.678       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   703 ;13.432 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;19.010 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   709 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3420 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2213 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3065 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   483 ; 0.146 ; 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):    61 ; 0.206 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    52 ; 0.184 ; 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):  2930 ; 0.794 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4611 ; 1.254 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1830 ; 2.098 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1581 ; 3.191 ; 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  : 16                                         
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     5        A    63                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0590  46.3620  24.3950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0030 T22:   0.0040                                     
REMARK   3      T33:   0.0102 T12:  -0.0028                                     
REMARK   3      T13:  -0.0003 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8028 L22:   1.1621                                     
REMARK   3      L33:   0.9369 L12:   0.3077                                     
REMARK   3      L13:   0.3314 L23:   0.0294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0332 S12:   0.0163 S13:   0.0097                       
REMARK   3      S21:  -0.1345 S22:  -0.0144 S23:  -0.0796                       
REMARK   3      S31:  -0.0293 S32:  -0.0107 S33:   0.0477                       
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    64        A   115                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3350  39.9780  18.3730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0043 T22:  -0.0108                                     
REMARK   3      T33:   0.0039 T12:  -0.0156                                     
REMARK   3      T13:  -0.0160 T23:  -0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1864 L22:   1.3646                                     
REMARK   3      L33:   2.3512 L12:  -0.0610                                     
REMARK   3      L13:   0.3228 L23:   0.6124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0035 S12:   0.0484 S13:  -0.0874                       
REMARK   3      S21:  -0.0534 S22:  -0.0305 S23:   0.0752                       
REMARK   3      S31:   0.1117 S32:  -0.1806 S33:   0.0340                       
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   116        A   159                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.4200  24.9740  30.6520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0886 T22:  -0.0284                                     
REMARK   3      T33:   0.0709 T12:  -0.0277                                     
REMARK   3      T13:  -0.0092 T23:   0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3698 L22:   2.3174                                     
REMARK   3      L33:   4.8356 L12:   0.0424                                     
REMARK   3      L13:   0.0153 L23:  -1.9193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0808 S12:  -0.0225 S13:  -0.0270                       
REMARK   3      S21:  -0.2029 S22:  -0.0217 S23:   0.0604                       
REMARK   3      S31:   0.2835 S32:   0.1018 S33:  -0.0591                       
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   160        A   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0450  21.7670  35.4570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0779 T22:  -0.0506                                     
REMARK   3      T33:   0.0451 T12:   0.0163                                     
REMARK   3      T13:  -0.0162 T23:   0.0411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7832 L22:   6.9690                                     
REMARK   3      L33:   1.6387 L12:  -0.0574                                     
REMARK   3      L13:   0.5810 L23:  -0.5529                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0812 S12:  -0.0831 S13:  -0.3566                       
REMARK   3      S21:   0.0035 S22:  -0.0456 S23:   0.0181                       
REMARK   3      S31:   0.4451 S32:   0.0958 S33:  -0.0356                       
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   189        A   215                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5400  16.1020  37.9580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0943 T22:  -0.0580                                     
REMARK   3      T33:  -0.0094 T12:  -0.1051                                     
REMARK   3      T13:  -0.0646 T23:   0.0423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6452 L22:   1.1316                                     
REMARK   3      L33:  20.3953 L12:  -0.3589                                     
REMARK   3      L13:   0.6881 L23:  -2.7858                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0805 S12:  -0.0316 S13:  -0.0855                       
REMARK   3      S21:  -0.3641 S22:   0.2496 S23:   0.0720                       
REMARK   3      S31:   1.1234 S32:  -0.4503 S33:  -0.3300                       
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   216        A   223                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6830  25.4940  45.0220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2041 T22:   0.2369                                     
REMARK   3      T33:   0.2694 T12:   0.1288                                     
REMARK   3      T13:   0.0101 T23:   0.0910                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.1759 L22:  39.3545                                     
REMARK   3      L33:  59.4614 L12:  -4.5345                                     
REMARK   3      L13:  10.8922 L23:  28.6358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1606 S12:   0.6149 S13:   1.0687                       
REMARK   3      S21:  -0.5170 S22:  -1.6412 S23:   3.0049                       
REMARK   3      S31:  -3.5184 S32:  -4.0035 S33:   1.8018                       
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   224        A   262                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1030  32.0720  36.4300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0117 T22:   0.0024                                     
REMARK   3      T33:  -0.0159 T12:  -0.0271                                     
REMARK   3      T13:  -0.0217 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1482 L22:   1.9397                                     
REMARK   3      L33:   1.3096 L12:   0.1989                                     
REMARK   3      L13:  -0.1992 L23:  -0.8023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0540 S12:  -0.1150 S13:   0.0120                       
REMARK   3      S21:   0.1098 S22:  -0.0654 S23:  -0.0017                       
REMARK   3      S31:   0.1749 S32:  -0.1168 S33:   0.0113                       
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   263        A   292                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.7780  34.0320  36.4380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0345 T22:  -0.0093                                     
REMARK   3      T33:   0.0243 T12:   0.0176                                     
REMARK   3      T13:  -0.0594 T23:   0.0566                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3236 L22:   4.0155                                     
REMARK   3      L33:   1.5477 L12:   1.4454                                     
REMARK   3      L13:   0.4524 L23:  -0.4899                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1202 S12:  -0.3063 S13:  -0.2670                       
REMARK   3      S21:   0.2542 S22:  -0.0926 S23:  -0.4968                       
REMARK   3      S31:   0.0787 S32:   0.2602 S33:  -0.0276                       
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 :   B     9        B    63                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3900 -19.5220  21.5240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0094 T22:   0.0205                                     
REMARK   3      T33:   0.0019 T12:  -0.0214                                     
REMARK   3      T13:  -0.0163 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8894 L22:   1.2833                                     
REMARK   3      L33:   0.8893 L12:  -0.2925                                     
REMARK   3      L13:   0.0983 L23:  -0.1122                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0445 S12:  -0.0472 S13:  -0.0759                       
REMARK   3      S21:   0.0585 S22:  -0.0524 S23:   0.0059                       
REMARK   3      S31:   0.0686 S32:   0.0182 S33:   0.0079                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    64        B    86                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2560 -13.6600  30.7560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0139 T22:   0.0218                                     
REMARK   3      T33:   0.0041 T12:  -0.0261                                     
REMARK   3      T13:   0.0110 T23:  -0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6099 L22:   2.1067                                     
REMARK   3      L33:   2.0293 L12:   0.8818                                     
REMARK   3      L13:   0.5088 L23:   1.5267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0106 S12:  -0.0581 S13:   0.1575                       
REMARK   3      S21:   0.0378 S22:  -0.0724 S23:   0.1338                       
REMARK   3      S31:  -0.2090 S32:  -0.0035 S33:   0.0830                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    87        B   120                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.3550 -10.1310  27.7550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0017 T22:   0.0268                                     
REMARK   3      T33:   0.0078 T12:  -0.0155                                     
REMARK   3      T13:  -0.0024 T23:  -0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4011 L22:   3.0113                                     
REMARK   3      L33:   1.8965 L12:   0.1942                                     
REMARK   3      L13:  -0.0723 L23:   0.5012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0218 S12:  -0.0687 S13:   0.0237                       
REMARK   3      S21:   0.0685 S22:  -0.0305 S23:   0.2388                       
REMARK   3      S31:  -0.2138 S32:  -0.1265 S33:   0.0087                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   121        B   159                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.7120   2.5950  16.8150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0806 T22:  -0.0424                                     
REMARK   3      T33:   0.0565 T12:  -0.0165                                     
REMARK   3      T13:  -0.0234 T23:  -0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9189 L22:   3.0539                                     
REMARK   3      L33:   7.7503 L12:  -0.0742                                     
REMARK   3      L13:   0.1660 L23:  -3.2639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0699 S12:   0.0638 S13:   0.0635                       
REMARK   3      S21:   0.1861 S22:   0.0042 S23:   0.0884                       
REMARK   3      S31:  -0.3133 S32:   0.0721 S33:  -0.0740                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   160        B   190                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.0750   5.9540  14.6670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0942 T22:  -0.0225                                     
REMARK   3      T33:   0.0151 T12:  -0.0812                                     
REMARK   3      T13:  -0.0213 T23:   0.0369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6803 L22:   6.8260                                     
REMARK   3      L33:   0.6124 L12:  -0.8554                                     
REMARK   3      L13:  -0.3761 L23:  -0.0518                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0598 S12:   0.0201 S13:   0.2383                       
REMARK   3      S21:   0.0989 S22:  -0.0290 S23:  -0.2775                       
REMARK   3      S31:  -0.3039 S32:   0.0355 S33:  -0.0308                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   191        B   236                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.9140   8.1340   8.6660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0492 T22:   0.0035                                     
REMARK   3      T33:  -0.0003 T12:   0.0222                                     
REMARK   3      T13:  -0.0081 T23:   0.0259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5557 L22:   2.0815                                     
REMARK   3      L33:  11.2350 L12:  -0.2202                                     
REMARK   3      L13:   0.0802 L23:  -3.0886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0589 S12:   0.0845 S13:   0.0894                       
REMARK   3      S21:   0.1249 S22:   0.2215 S23:   0.2344                       
REMARK   3      S31:  -0.1290 S32:  -0.4802 S33:  -0.2804                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   237        B   261                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.3940  -8.3990  13.3720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0006 T22:   0.0083                                     
REMARK   3      T33:   0.0187 T12:  -0.0153                                     
REMARK   3      T13:  -0.0076 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2131 L22:   1.4468                                     
REMARK   3      L33:   1.7956 L12:   0.1125                                     
REMARK   3      L13:   0.1494 L23:  -0.4483                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0624 S12:   0.1415 S13:   0.0764                       
REMARK   3      S21:  -0.0779 S22:  -0.0806 S23:  -0.0884                       
REMARK   3      S31:  -0.1312 S32:   0.0256 S33:   0.0181                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   262        B   291                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5360  -7.0210  12.1450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0570 T22:   0.0426                                     
REMARK   3      T33:   0.0139 T12:  -0.0637                                     
REMARK   3      T13:   0.0173 T23:   0.0390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9971 L22:   3.0919                                     
REMARK   3      L33:   2.7918 L12:  -1.3353                                     
REMARK   3      L13:  -0.0612 L23:   0.0781                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1105 S12:   0.2235 S13:   0.2497                       
REMARK   3      S21:  -0.2763 S22:  -0.1508 S23:  -0.3452                       
REMARK   3      S31:  -0.1859 S32:   0.4848 S33:   0.0404                       
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 2IRY 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 RCSB039941.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUL-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   : 56549                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.490                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.700                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : 0.09500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.23700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
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   (%): 46.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
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 DGTP, 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 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       37.93500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
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 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     ALA B   292                                                      
REMARK 465     ASP B   293                                                      
REMARK 465     ALA B   294                                                      
REMARK 465     PRO B   295                                                      
REMARK 465     VAL B   296                                                      
REMARK 465     ALA B   297                                                      
REMARK 465     ASP B   298                                                      
REMARK 465     ARG B   299                                                      
REMARK 465     LEU B   300                                                      
REMARK 465     THR B   301                                                      
REMARK 465     ARG B   302                                                      
REMARK 465     TYR B   303                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1179     O    HOH A  1425              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A    34     O    HOH B  1408     1665     2.16            
REMARK 500   O    HOH A  1245     O    HOH B  1289     1565     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  97       21.19   -141.17                                   
REMARK 500    SER A 177     -103.65   -112.13                                   
REMARK 500    THR A 219      120.51    -37.25                                   
REMARK 500    TYR A 244       -6.83     79.98                                   
REMARK 500    ASP A 291     -161.34   -125.48                                   
REMARK 500    LYS B  69      -65.84   -109.55                                   
REMARK 500    ASP B  97       21.06   -145.15                                   
REMARK 500    SER B 177     -113.84   -109.25                                   
REMARK 500    TYR B 244       -5.11     73.25                                   
REMARK 500    LEU B 268      128.64    -37.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1230        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH B1311        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH B1341        DISTANCE =  5.17 ANGSTROMS                       
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     DGT B 1103                                                       
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 A1100  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 140   OD1                                                    
REMARK 620 2 HOH A1397   O   109.7                                              
REMARK 620 3 DGT A1102   O2G 148.4  87.0                                        
REMARK 620 4 HOH A1412   O    60.4 145.8  90.5                                  
REMARK 620 5 ASP A 140   OD2  50.4  59.6 140.8 105.6                            
REMARK 620 6 DGT A1102   O2B  83.3  67.2  78.7  78.8  70.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B1101  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 140   OD1                                                    
REMARK 620 2 DGT B1103   O3G 131.5                                              
REMARK 620 3 HOH B1394   O   105.2  68.0                                        
REMARK 620 4 ASP B 142   OD1 143.4  71.9 110.5                                  
REMARK 620 5 HOH B1387   O    61.1  82.0 122.6 104.2                            
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 MN A 1100                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGT A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGT B 1103                
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: 2IRX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE POLYMERASE DOMAIN FROM                      
REMARK 900 MYCOBACTERIUM TUBERCULOSIS LIGASE D WITH GTP AND MANGANESE.          
DBREF  2IRY A    4   303  UNP    P71571   Y938_MYCTU       1    300             
DBREF  2IRY B    4   303  UNP    P71571   Y938_MYCTU       1    300             
SEQADV 2IRY GLY A    1  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRY SER A    2  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRY HIS A    3  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRY GLY B    1  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRY SER B    2  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRY HIS B    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                                              
SEQRES   1 B  303  GLY SER HIS MET GLY SER ALA SER GLU GLN ARG VAL THR          
SEQRES   2 B  303  LEU THR ASN ALA ASP LYS VAL LEU TYR PRO ALA THR GLY          
SEQRES   3 B  303  THR THR LYS SER ASP ILE PHE ASP TYR TYR ALA GLY VAL          
SEQRES   4 B  303  ALA GLU VAL MET LEU GLY HIS ILE ALA GLY ARG PRO ALA          
SEQRES   5 B  303  THR ARG LYS ARG TRP PRO ASN GLY VAL ASP GLN PRO ALA          
SEQRES   6 B  303  PHE PHE GLU LYS GLN LEU ALA LEU SER ALA PRO PRO TRP          
SEQRES   7 B  303  LEU SER ARG ALA THR VAL ALA HIS ARG SER GLY THR THR          
SEQRES   8 B  303  THR TYR PRO ILE ILE ASP SER ALA THR GLY LEU ALA TRP          
SEQRES   9 B  303  ILE ALA GLN GLN ALA ALA LEU GLU VAL HIS VAL PRO GLN          
SEQRES  10 B  303  TRP ARG PHE VAL ALA GLU PRO GLY SER GLY GLU LEU ASN          
SEQRES  11 B  303  PRO GLY PRO ALA THR ARG LEU VAL PHE ASP LEU ASP PRO          
SEQRES  12 B  303  GLY GLU GLY VAL MET MET ALA GLN LEU ALA GLU VAL ALA          
SEQRES  13 B  303  ARG ALA VAL ARG ASP LEU LEU ALA ASP ILE GLY LEU VAL          
SEQRES  14 B  303  THR PHE PRO VAL THR SER GLY SER LYS GLY LEU HIS LEU          
SEQRES  15 B  303  TYR THR PRO LEU ASP GLU PRO VAL SER SER ARG GLY ALA          
SEQRES  16 B  303  THR VAL LEU ALA LYS ARG VAL ALA GLN ARG LEU GLU GLN          
SEQRES  17 B  303  ALA MET PRO ALA LEU VAL THR SER THR MET THR LYS SER          
SEQRES  18 B  303  LEU ARG ALA GLY LYS VAL PHE VAL ASP TRP SER GLN ASN          
SEQRES  19 B  303  SER GLY SER LYS THR THR ILE ALA PRO TYR SER LEU ARG          
SEQRES  20 B  303  GLY ARG THR HIS PRO THR VAL ALA ALA PRO ARG THR TRP          
SEQRES  21 B  303  ALA GLU LEU ASP ASP PRO ALA LEU ARG GLN LEU SER TYR          
SEQRES  22 B  303  ASP GLU VAL LEU THR ARG ILE ALA ARG ASP GLY ASP LEU          
SEQRES  23 B  303  LEU GLU ARG LEU ASP ALA ASP ALA PRO VAL ALA ASP ARG          
SEQRES  24 B  303  LEU THR ARG TYR                                              
HET     MN  A1100       1                                                       
HET     MN  B1101       1                                                       
HET    DGT  A1102      31                                                       
HET    DGT  B1103      20                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     DGT 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE                                
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  DGT    2(C10 H16 N5 O13 P3)                                         
FORMUL   7  HOH   *659(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 THR A  259  ASP A  264  1                                   6    
HELIX    8   8 SER A  272  GLY A  284  1                                  13    
HELIX    9   9 THR B   28  ALA B   48  1                                  21    
HELIX   10  10 SER B   98  GLN B  108  1                                  11    
HELIX   11  11 MET B  148  ASP B  165  1                                  18    
HELIX   12  12 SER B  191  MET B  210  1                                  20    
HELIX   13  13 THR B  219  ARG B  223  5                                   5    
HELIX   14  14 TRP B  231  SER B  235  5                                   5    
HELIX   15  15 THR B  259  ASP B  264  1                                   6    
HELIX   16  16 SER B  272  GLY B  284  1                                  13    
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  PHE A 228   N  ASP A 142           
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  LEU A 180   N  LEU A 141           
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 4 PHE B  66  GLU B  68  0                                        
SHEET    2   E 4 THR B  53  ARG B  56 -1  N  ARG B  56   O  PHE B  66           
SHEET    3   E 4 GLU B 112  VAL B 115 -1  O  HIS B 114   N  THR B  53           
SHEET    4   E 4 THR B 240  ILE B 241 -1  O  THR B 240   N  VAL B 115           
SHEET    1   F 2 SER B  80  HIS B  86  0                                        
SHEET    2   F 2 GLY B  89  ILE B  95 -1  O  TYR B  93   N  ALA B  82           
SHEET    1   G 4 TRP B 118  ALA B 122  0                                        
SHEET    2   G 4 LEU B 129  PRO B 143 -1  O  ASN B 130   N  VAL B 121           
SHEET    3   G 4 VAL B 227  ASP B 230 -1  O  PHE B 228   N  ASP B 142           
SHEET    4   G 4 VAL B 214  THR B 215  1  N  THR B 215   O  VAL B 229           
SHEET    1   H 5 TRP B 118  ALA B 122  0                                        
SHEET    2   H 5 LEU B 129  PRO B 143 -1  O  ASN B 130   N  VAL B 121           
SHEET    3   H 5 LEU B 180  VAL B 190 -1  O  LEU B 180   N  LEU B 141           
SHEET    4   H 5 PHE B 171  THR B 174 -1  N  VAL B 173   O  HIS B 181           
SHEET    5   H 5 ALA B 256  PRO B 257 -1  O  ALA B 256   N  THR B 174           
LINK         OD1 ASP A 140                MN    MN A1100     1555   1555  2.48  
LINK         OD1 ASP B 140                MN    MN B1101     1555   1555  2.45  
LINK        MN    MN A1100                 O   HOH A1397     1555   1555  2.20  
LINK        MN    MN A1100                 O2G DGT A1102     1555   1555  2.08  
LINK        MN    MN A1100                 O   HOH A1412     1555   1555  2.45  
LINK        MN    MN B1101                 O3G DGT B1103     1555   1555  2.27  
LINK        MN    MN B1101                 O   HOH B1394     1555   1555  2.15  
LINK        MN    MN A1100                 OD2 ASP A 140     1555   1555  2.66  
LINK        MN    MN A1100                 O2B DGT A1102     1555   1555  2.74  
LINK        MN    MN B1101                 OD1 ASP B 142     1555   1555  2.67  
LINK        MN    MN B1101                 O   HOH B1387     1555   1555  2.66  
SITE     1 AC1  5 ASP A 140  ASP A 142  DGT A1102  HOH A1397                    
SITE     2 AC1  5 HOH A1412                                                     
SITE     1 AC2  5 ASP B 140  ASP B 142  DGT B1103  HOH B1387                    
SITE     2 AC2  5 HOH B1394                                                     
SITE     1 AC3 21 PHE A  67  LYS A  69  ASP A 140  ASP A 142                    
SITE     2 AC3 21 SER A 175  SER A 177  LYS A 178  GLY A 179                    
SITE     3 AC3 21 HIS A 181  GLN A 233  THR A 239  ARG A 247                    
SITE     4 AC3 21  MN A1100  HOH A1396  HOH A1397  HOH A1400                    
SITE     5 AC3 21 HOH A1401  HOH A1404  HOH A1412  HOH A1420                    
SITE     6 AC3 21 HOH A1426                                                     
SITE     1 AC4 13 ASP B 140  ASP B 142  SER B 175  SER B 177                    
SITE     2 AC4 13 LYS B 178  GLY B 179  HIS B 181  ILE B 241                    
SITE     3 AC4 13 ARG B 247   MN B1101  HOH B1387  HOH B1391                    
SITE     4 AC4 13 HOH B1394                                                     
CRYST1   41.221   75.870   95.809  90.00  92.59  90.00 P 1 21 1      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      0.024260  0.000000  0.001098        0.00000                         
SCALE2      0.000000  0.013180  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010448        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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