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Database: PDB
Entry: 2R9L
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HEADER    TRANSFERASE/DNA                         13-SEP-07   2R9L              
TITLE     POLYMERASE DOMAIN FROM MYCOBACTERIUM TUBERCULOSIS LIGASE D IN COMPLEX 
TITLE    2 WITH DNA                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE DNA LIGASE-LIKE PROTEIN;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LIGD POLYMERASE DOMAIN RESIDUES 1-300;                     
COMPND   5 EC: 2.7.7.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-D(P*DGP*DCP*DGP*DGP*DC)-3');                       
COMPND   9 CHAIN: C, E;                                                         
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: DNA (5'-D(*DGP*DCP*DCP*DGP*DCP*DAP*DAP*DCP*DGP*DCP*DA)-3');
COMPND  13 CHAIN: D;                                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: DNA (5'-                                                   
COMPND  17 D(*DGP*DCP*DCP*DGP*DCP*DAP*DAP*DCP*DGP*DCP*DAP*DCP*DG)-3');          
COMPND  18 CHAIN: F;                                                            
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;               
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;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 MOL_ID: 4;                                                           
SOURCE  16 SYNTHETIC: YES                                                       
KEYWDS    TRANSFERASE, PROTEIN-DNA COMPLEX, ATP-BINDING, LIGASE, NUCLEOTIDE-    
KEYWDS   2 BINDING, TRANSFERASE-DNA COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.C.BRISSETT,G.C.FOX,R.S.PITCHER,A.J.DOHERTY                          
REVDAT   3   13-JUL-11 2R9L    1       VERSN                                    
REVDAT   2   24-FEB-09 2R9L    1       VERSN                                    
REVDAT   1   08-JAN-08 2R9L    0                                                
JRNL        AUTH   N.C.BRISSETT,R.S.PITCHER,R.JUAREZ,A.J.PICHER,A.J.GREEN,      
JRNL        AUTH 2 T.R.DAFFORN,G.C.FOX,L.BLANCO,A.J.DOHERTY                     
JRNL        TITL   STRUCTURE OF A NHEJ POLYMERASE-MEDIATED DNA SYNAPTIC COMPLEX 
JRNL        REF    SCIENCE                       V. 318   456 2007              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   17947582                                                     
JRNL        DOI    10.1126/SCIENCE.1145112                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 29486                          
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) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1502                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2037                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.56                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 124                          
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4348                                    
REMARK   3   NUCLEIC ACID ATOMS       : 693                                     
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 97                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 90.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.77000                                              
REMARK   3    B22 (A**2) : -7.02000                                             
REMARK   3    B33 (A**2) : 2.25000                                              
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): 0.471         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.289         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.231         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.383        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5249 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7286 ; 1.015 ; 2.138       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   567 ; 5.572 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   181 ;29.146 ;22.597       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   695 ;14.560 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;15.472 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   835 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3745 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2297 ; 0.220 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3475 ; 0.322 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   409 ; 0.213 ; 0.500       
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):    43 ; 0.223 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.472 ; 0.500       
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):  2899 ; 0.681 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4588 ; 1.048 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2910 ; 1.576 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2698 ; 2.173 ; 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 : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 8                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      9       A      81      1                      
REMARK   3           1     B      9       B      81      1                      
REMARK   3           2     A     82       A      87      6                      
REMARK   3           2     B     82       B      87      6                      
REMARK   3           3     A     88       A     118      1                      
REMARK   3           3     B     88       B     118      1                      
REMARK   3           4     A    126       A     140      1                      
REMARK   3           4     B    126       B     140      1                      
REMARK   3           5     A    153       A     183      1                      
REMARK   3           5     B    153       B     183      1                      
REMARK   3           6     A    186       A     202      1                      
REMARK   3           6     B    186       B     202      1                      
REMARK   3           7     A    226       A     255      1                      
REMARK   3           7     B    226       B     255      1                      
REMARK   3           8     A    268       A     289      5                      
REMARK   3           8     B    268       B     289      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1510 ; 0.030 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):     88 ; 0.260 ; 0.500           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    132 ; 0.710 ; 5.000           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1510 ; 0.080 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):     88 ; 0.570 ; 2.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):    132 ; 2.000 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      1       C       5      1                      
REMARK   3           1     E      1       E       5      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    C    (A):    105 ; 0.030 ; 0.050           
REMARK   3   TIGHT THERMAL      2    C (A**2):    105 ; 0.050 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : D F                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D      1       D       5      4                      
REMARK   3           1     F      1       F       5      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    D    (A):     98 ; 0.250 ; 0.500           
REMARK   3   MEDIUM THERMAL     3    D (A**2):     98 ; 0.510 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
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     6        A   104                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0339 -11.8104 -13.8771              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2939 T22:  -0.2495                                     
REMARK   3      T33:  -0.3297 T12:  -0.0857                                     
REMARK   3      T13:  -0.0813 T23:   0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9635 L22:  10.7638                                     
REMARK   3      L33:   4.3118 L12:  -0.2897                                     
REMARK   3      L13:  -0.8570 L23:   1.3682                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0716 S12:  -0.0658 S13:   0.5187                       
REMARK   3      S21:   0.0992 S22:  -0.1229 S23:  -0.3499                       
REMARK   3      S31:  -0.6329 S32:   0.3137 S33:   0.0513                       
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 :   B     8        B   104                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.4047 -20.3539 -56.5617              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1279 T22:  -0.0889                                     
REMARK   3      T33:  -0.2107 T12:  -0.0944                                     
REMARK   3      T13:  -0.3089 T23:  -0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9609 L22:  10.0354                                     
REMARK   3      L33:   3.4649 L12:   1.8110                                     
REMARK   3      L13:  -0.2070 L23:   0.0352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2277 S12:   0.6817 S13:  -0.3046                       
REMARK   3      S21:  -1.2175 S22:   0.2945 S23:   0.7960                       
REMARK   3      S31:   0.5779 S32:  -0.0933 S33:  -0.0669                       
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 :   C     1        C     5                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.9965   4.0545 -18.4468              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3082 T22:  -0.2158                                     
REMARK   3      T33:  -0.0087 T12:  -0.1003                                     
REMARK   3      T13:  -0.0504 T23:  -0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3065 L22:  18.9171                                     
REMARK   3      L33:   9.4954 L12:  -2.7870                                     
REMARK   3      L13:   3.5106 L23:  -8.3908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3016 S12:   0.2152 S13:   0.6349                       
REMARK   3      S21:  -0.6782 S22:  -0.4069 S23:  -0.7085                       
REMARK   3      S31:  -1.2342 S32:   0.8317 S33:   0.1054                       
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 :   D     1        D     5                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7334   5.1346 -20.8041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4018 T22:  -0.1584                                     
REMARK   3      T33:   0.2128 T12:  -0.0438                                     
REMARK   3      T13:  -0.3446 T23:   0.0664                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6830 L22:  64.5998                                     
REMARK   3      L33:   3.8745 L12:  -4.6216                                     
REMARK   3      L13:  -0.3277 L23:  13.3478                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2583 S12:   0.1972 S13:   0.4480                       
REMARK   3      S21:  -0.8303 S22:  -1.0966 S23:   1.6984                       
REMARK   3      S31:  -1.0556 S32:  -0.5104 S33:   0.8383                       
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 :   E     1        E     5                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7992 -34.6475 -53.7896              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4412 T22:  -0.1897                                     
REMARK   3      T33:   0.3257 T12:  -0.0593                                     
REMARK   3      T13:  -0.1236 T23:  -0.0721                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.1830 L22:  12.8025                                     
REMARK   3      L33:   6.9118 L12: -13.2779                                     
REMARK   3      L13:   7.6925 L23:  -4.1245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7233 S12:   0.8576 S13:  -1.9864                       
REMARK   3      S21:  -1.7531 S22:  -0.6473 S23:  -0.1737                       
REMARK   3      S31:   0.9203 S32:   0.2769 S33:  -0.0760                       
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 :   F     1        F     7                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0872 -29.1904 -45.3880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2831 T22:  -0.1729                                     
REMARK   3      T33:  -0.1319 T12:   0.0766                                     
REMARK   3      T13:  -0.2915 T23:  -0.0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6570 L22:  38.1132                                     
REMARK   3      L33:   3.0213 L12:  -4.0490                                     
REMARK   3      L13:  -4.1339 L23:   2.8238                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2855 S12:  -0.2589 S13:  -0.3745                       
REMARK   3      S21:   1.8461 S22:  -0.3175 S23:  -1.9801                       
REMARK   3      S31:   0.7842 S32:   0.1691 S33:   0.6030                       
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 :   B   105        B   173                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.0044  -1.5714 -49.4339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2437 T22:  -0.1865                                     
REMARK   3      T33:   0.1114 T12:  -0.0255                                     
REMARK   3      T13:  -0.2965 T23:   0.1635                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4183 L22:  12.7765                                     
REMARK   3      L33:   2.6386 L12:   0.7287                                     
REMARK   3      L13:   0.6235 L23:   2.6807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2077 S12:   0.2941 S13:   0.8550                       
REMARK   3      S21:  -0.6979 S22:   0.2121 S23:   1.9824                       
REMARK   3      S31:   0.0325 S32:  -0.2765 S33:  -0.0044                       
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 :   B   174        B   216                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.3168   4.3106 -42.1757              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2693 T22:  -0.2927                                     
REMARK   3      T33:   0.1387 T12:   0.0169                                     
REMARK   3      T13:  -0.0243 T23:   0.0771                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.6664 L22:  14.0631                                     
REMARK   3      L33:   6.3835 L12:   2.2682                                     
REMARK   3      L13:  -2.3403 L23:   1.4935                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1980 S12:  -0.4707 S13:   0.4632                       
REMARK   3      S21:   0.3502 S22:  -0.0863 S23:   2.2706                       
REMARK   3      S31:  -0.3526 S32:  -0.0976 S33:  -0.1117                       
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   217        B   289                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.4927  -6.5164 -48.4460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2147 T22:  -0.0569                                     
REMARK   3      T33:   0.5706 T12:  -0.0614                                     
REMARK   3      T13:  -0.2505 T23:   0.0993                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4538 L22:   8.9819                                     
REMARK   3      L33:   3.2152 L12:   2.4767                                     
REMARK   3      L13:   1.6017 L23:   1.6203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0291 S12:   0.0258 S13:   0.6531                       
REMARK   3      S21:  -0.1873 S22:  -0.0525 S23:   2.6091                       
REMARK   3      S31:   0.2535 S32:  -0.6926 S33:   0.0234                       
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 :   D     6        D    11                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8491 -16.5133 -31.8618              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2260 T22:   0.0697                                     
REMARK   3      T33:  -0.0360 T12:   0.0656                                     
REMARK   3      T13:  -0.4005 T23:   0.0309                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3330 L22:   2.5695                                     
REMARK   3      L33:   4.1559 L12:   1.3871                                     
REMARK   3      L13:   2.1147 L23:  -0.9244                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3554 S12:  -0.3061 S13:   0.5544                       
REMARK   3      S21:  -1.1257 S22:   0.0344 S23:   1.1889                       
REMARK   3      S31:  -0.4446 S32:  -0.8871 S33:   0.3210                       
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 :   F     8        F    13                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1885 -12.1801 -34.2900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0439 T22:   0.1125                                     
REMARK   3      T33:   0.1021 T12:   0.0988                                     
REMARK   3      T13:  -0.4262 T23:   0.0777                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8902 L22:  14.5290                                     
REMARK   3      L33:   8.1284 L12:  -0.9967                                     
REMARK   3      L13:   3.4013 L23:   7.5048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4052 S12:  -0.8985 S13:   1.1070                       
REMARK   3      S21:  -0.1477 S22:   0.2422 S23:   1.1699                       
REMARK   3      S31:  -0.2506 S32:  -0.4867 S33:  -0.6475                       
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 :   A   105        A   173                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8224 -30.1594 -20.0025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4436 T22:  -0.2354                                     
REMARK   3      T33:  -0.3862 T12:   0.0482                                     
REMARK   3      T13:  -0.0557 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2545 L22:  11.0391                                     
REMARK   3      L33:   2.8639 L12:  -0.2709                                     
REMARK   3      L13:   0.7253 L23:   0.6683                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0459 S12:   0.0323 S13:  -0.1141                       
REMARK   3      S21:   0.0138 S22:  -0.0922 S23:   0.6790                       
REMARK   3      S31:  -0.0492 S32:  -0.0832 S33:   0.0463                       
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 :   A   174        A   216                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3721 -35.2255 -25.4391              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2215 T22:  -0.1899                                     
REMARK   3      T33:  -0.0394 T12:   0.0243                                     
REMARK   3      T13:  -0.2244 T23:  -0.0417                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9156 L22:   8.9231                                     
REMARK   3      L33:   6.4238 L12:   0.7542                                     
REMARK   3      L13:   0.0117 L23:   0.6918                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4015 S12:   0.4766 S13:  -0.5138                       
REMARK   3      S21:  -1.0823 S22:  -0.1941 S23:   1.6501                       
REMARK   3      S31:   0.0797 S32:  -0.7813 S33:  -0.2074                       
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 :   A   217        A   292                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7795 -28.1014 -11.3980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3261 T22:  -0.1825                                     
REMARK   3      T33:  -0.3098 T12:  -0.0706                                     
REMARK   3      T13:   0.1130 T23:  -0.0689                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2938 L22:  11.0962                                     
REMARK   3      L33:   5.9778 L12:   1.4341                                     
REMARK   3      L13:   0.3272 L23:   2.7629                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1765 S12:  -0.1615 S13:   0.0176                       
REMARK   3      S21:   1.1910 S22:  -0.6398 S23:   1.0188                       
REMARK   3      S31:   0.5004 S32:  -0.5053 S33:   0.4633                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.60                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2R9L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044596.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-SEP-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) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM16                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98400                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29540                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: PDB ENTRY 2IRU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V)PEG 3350, 0.2 M AMMONIUM         
REMARK 280  CHLORIDE, 10MM MNCL2, PH 7.5, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  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       24.26550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.77100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.89400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.77100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.26550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.89400            
REMARK 290   SMTRY3   4  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2680 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     VAL A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     ASP A   295                                                      
REMARK 465     ARG A   296                                                      
REMARK 465     LEU A   297                                                      
REMARK 465     THR A   298                                                      
REMARK 465     ARG A   299                                                      
REMARK 465     TYR A   300                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     ASP B   290                                                      
REMARK 465     ALA B   291                                                      
REMARK 465     PRO B   292                                                      
REMARK 465     VAL B   293                                                      
REMARK 465     ALA B   294                                                      
REMARK 465     ASP B   295                                                      
REMARK 465     ARG B   296                                                      
REMARK 465     LEU B   297                                                      
REMARK 465     THR B   298                                                      
REMARK 465     ARG B   299                                                      
REMARK 465     TYR B   300                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A    8   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     SER A  123   CB   OG                                             
REMARK 480     GLU A  142   CB   CG   CD   OE1  OE2                             
REMARK 480     ALA A  147   CB                                                  
REMARK 480     ALA A  209   CB                                                  
REMARK 480     LEU A  219   CB   CG   CD1  CD2                                  
REMARK 480     VAL B   17   CG2                                                 
REMARK 480     GLU B   38   CG   CD   OE1  OE2                                  
REMARK 480     PRO B   74   CB   CG                                             
REMARK 480     ALA B   96   CB                                                  
REMARK 480     THR B   97   CG2                                                 
REMARK 480     ALA B  100   CB                                                  
REMARK 480     PRO B  121   CG   CD                                             
REMARK 480     ALA B  147   CB                                                  
REMARK 480     ALA B  209   CB                                                  
REMARK 480     LEU B  210   CD1  CD2                                            
REMARK 480     THR B  216   CG2                                                 
REMARK 480     LEU B  219   CD1  CD2                                            
REMARK 480     ALA B  258   CB                                                  
REMARK 480     ASP B  261   OD2                                                 
REMARK 480     PRO B  263   CG                                                  
REMARK 480     LEU B  283   CD2                                                 
REMARK 480     GLU B  285   OE2                                                 
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   NH2  ARG A   198     O1   PEG A   297              2.00            
REMARK 500   OP2   DG C     3     O    HOH C    16              2.05            
REMARK 500   O    ALA B   278     O    HOH B   315              2.14            
REMARK 500   O6    DG E     3     O    HOH E    31              2.15            
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   184     NH1  ARG B   198     3544     2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DG C   1   P      DG C   1   OP3    -0.121                       
REMARK 500     DG E   1   P      DG E   1   OP3    -0.134                       
REMARK 500    ALA B 278   C     ALA B 278   O       0.125                       
REMARK 500    ARG B 279   CZ    ARG B 279   NH1     0.098                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DG C   1   OP1 -  P   -  OP2 ANGL. DEV. = -11.5 DEGREES          
REMARK 500     DG C   1   O4' -  C1' -  N9  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DC D   5   O4' -  C1' -  N1  ANGL. DEV. =   4.7 DEGREES          
REMARK 500     DC D   8   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DG E   1   OP1 -  P   -  OP2 ANGL. DEV. = -11.7 DEGREES          
REMARK 500     DG E   1   O4' -  C1' -  N9  ANGL. DEV. =  -4.2 DEGREES          
REMARK 500     DC F   5   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DA F   6   C3' -  C2' -  C1' ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DG F   9   O4' -  C1' -  N9  ANGL. DEV. =  -4.6 DEGREES          
REMARK 500     DC F  12   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500    ARG B 279   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
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    LYS A  66      -52.67   -123.47                                   
REMARK 500    ASP A  94       18.68   -147.31                                   
REMARK 500    PRO A 121      108.28    -57.75                                   
REMARK 500    SER A 123       55.63   -158.43                                   
REMARK 500    SER A 174     -105.08   -110.45                                   
REMARK 500    THR A 216      111.83    -15.68                                   
REMARK 500    LEU A 219       52.47    -97.61                                   
REMARK 500    ARG A 220       49.18   -140.74                                   
REMARK 500    TYR A 241       -8.23     83.07                                   
REMARK 500    ALA A 252       87.39    -68.88                                   
REMARK 500    ALA A 264       41.20    -89.33                                   
REMARK 500    LYS B  66      -52.12   -121.21                                   
REMARK 500    ASP B  94       17.19   -145.51                                   
REMARK 500    SER B 174     -105.40   -111.44                                   
REMARK 500    MET B 215      -71.39    -39.78                                   
REMARK 500    THR B 216       92.10      4.42                                   
REMARK 500    TYR B 241       -8.41     84.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 293                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 293                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 297                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2IRU   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN                                                     
REMARK 900 RELATED ID: 2IRX   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND GTP AND MANGANESE                        
REMARK 900 RELATED ID: 2IRY   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH BOUND DGTP AND MANGANESE                       
DBREF  2R9L C    1     5  PDB    2R9L     2R9L             1      5             
DBREF  2R9L D    1    11  PDB    2R9L     2R9L             1     11             
DBREF  2R9L E    1     5  PDB    2R9L     2R9L             1      5             
DBREF  2R9L F    1    13  PDB    2R9L     2R9L             1     13             
DBREF  2R9L A    1   300  UNP    P71571   Y938_MYCTU       1    300             
DBREF  2R9L B    1   300  UNP    P71571   Y938_MYCTU       1    300             
SEQADV 2R9L GLY A   -2  UNP  P71571              EXPRESSION TAG                 
SEQADV 2R9L SER A   -1  UNP  P71571              EXPRESSION TAG                 
SEQADV 2R9L HIS A    0  UNP  P71571              EXPRESSION TAG                 
SEQADV 2R9L GLY B   -2  UNP  P71571              EXPRESSION TAG                 
SEQADV 2R9L SER B   -1  UNP  P71571              EXPRESSION TAG                 
SEQADV 2R9L HIS B    0  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                                              
SEQRES   1 C    5   DG  DC  DG  DG  DC                                          
SEQRES   1 D   11   DG  DC  DC  DG  DC  DA  DA  DC  DG  DC  DA                  
SEQRES   1 E    5   DG  DC  DG  DG  DC                                          
SEQRES   1 F   13   DG  DC  DC  DG  DC  DA  DA  DC  DG  DC  DA  DC  DG          
HET    EDO  A 293       4                                                       
HET    EDO  A 294       4                                                       
HET    EDO  B 293       4                                                       
HET    EDO  B 294       4                                                       
HET    EDO  A 295       4                                                       
HET    EDO  A 296       4                                                       
HET    PEG  A 297       7                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   7  EDO    6(C2 H6 O2)                                                  
FORMUL  13  PEG    C4 H10 O3                                                    
FORMUL  14  HOH   *97(H2 O)                                                     
HELIX    1   1 THR A   25  ALA A   45  1                                  21    
HELIX    2   2 SER A   95  GLN A  105  1                                  11    
HELIX    3   3 MET A  145  ILE A  163  1                                  19    
HELIX    4   4 SER A  188  MET A  207  1                                  20    
HELIX    5   5 THR A  216  ARG A  220  5                                   5    
HELIX    6   6 TRP A  228  SER A  232  5                                   5    
HELIX    7   7 THR A  256  ASP A  261  1                                   6    
HELIX    8   8 SER A  269  GLY A  281  1                                  13    
HELIX    9   9 THR B   25  ALA B   45  1                                  21    
HELIX   10  10 SER B   95  GLN B  105  1                                  11    
HELIX   11  11 MET B  145  ILE B  163  1                                  19    
HELIX   12  12 SER B  188  MET B  207  1                                  20    
HELIX   13  13 THR B  216  ARG B  220  5                                   5    
HELIX   14  14 TRP B  228  SER B  232  5                                   5    
HELIX   15  15 THR B  256  ASP B  261  1                                   6    
HELIX   16  16 TYR B  270  GLY B  281  1                                  12    
SHEET    1   A 4 PHE A  63  GLU A  65  0                                        
SHEET    2   A 4 THR A  50  ARG A  53 -1  N  ARG A  51   O  GLU A  65           
SHEET    3   A 4 GLU A 109  VAL A 112 -1  O  HIS A 111   N  THR A  50           
SHEET    4   A 4 THR A 237  ILE A 238 -1  O  THR A 237   N  VAL A 112           
SHEET    1   B 2 SER A  77  HIS A  83  0                                        
SHEET    2   B 2 GLY A  86  ILE A  92 -1  O  THR A  88   N  VAL A  81           
SHEET    1   C 4 TRP A 115  ALA A 119  0                                        
SHEET    2   C 4 LEU A 126  PRO A 140 -1  O  ASN A 127   N  VAL A 118           
SHEET    3   C 4 VAL A 224  ASP A 227 -1  O  ASP A 227   N  ASP A 137           
SHEET    4   C 4 VAL A 211  THR A 212  1  N  THR A 212   O  VAL A 224           
SHEET    1   D 5 TRP A 115  ALA A 119  0                                        
SHEET    2   D 5 LEU A 126  PRO A 140 -1  O  ASN A 127   N  VAL A 118           
SHEET    3   D 5 LEU A 177  VAL A 187 -1  O  LEU A 177   N  LEU A 138           
SHEET    4   D 5 PHE A 168  THR A 171 -1  N  VAL A 170   O  HIS A 178           
SHEET    5   D 5 ALA A 253  PRO A 254 -1  O  ALA A 253   N  THR A 171           
SHEET    1   E 4 PHE B  63  GLU B  65  0                                        
SHEET    2   E 4 THR B  50  ARG B  53 -1  N  ARG B  51   O  GLU B  65           
SHEET    3   E 4 GLU B 109  VAL B 112 -1  O  HIS B 111   N  THR B  50           
SHEET    4   E 4 THR B 237  ILE B 238 -1  O  THR B 237   N  VAL B 112           
SHEET    1   F 2 SER B  77  HIS B  83  0                                        
SHEET    2   F 2 GLY B  86  ILE B  92 -1  O  THR B  88   N  VAL B  81           
SHEET    1   G 4 TRP B 115  ALA B 119  0                                        
SHEET    2   G 4 LEU B 126  PRO B 140 -1  O  ASN B 127   N  VAL B 118           
SHEET    3   G 4 VAL B 224  ASP B 227 -1  O  ASP B 227   N  ASP B 137           
SHEET    4   G 4 VAL B 211  THR B 212  1  N  THR B 212   O  VAL B 226           
SHEET    1   H 5 TRP B 115  ALA B 119  0                                        
SHEET    2   H 5 LEU B 126  PRO B 140 -1  O  ASN B 127   N  VAL B 118           
SHEET    3   H 5 LEU B 177  VAL B 187 -1  O  LEU B 177   N  LEU B 138           
SHEET    4   H 5 PHE B 168  THR B 171 -1  N  VAL B 170   O  HIS B 178           
SHEET    5   H 5 ALA B 253  PRO B 254 -1  O  ALA B 253   N  THR B 171           
SHEET    1   I 2 THR B 250  VAL B 251  0                                        
SHEET    2   I 2 LEU B 268  SER B 269 -1  O  LEU B 268   N  VAL B 251           
SITE     1 AC1  5 LEU A 183  LEU A 195  PEG A 297  HOH A 347                    
SITE     2 AC1  5 ARG B 198                                                     
SITE     1 AC2  3 HOH A 344  ILE B 163  LEU B 195                               
SITE     1 AC3  2 LYS B 235  THR B 236                                          
SITE     1 AC4  5 LYS B  52  TRP B  54  GLU B 109  GLY B 245                    
SITE     2 AC4  5 ARG B 246                                                     
SITE     1 AC5  4 HIS A 111  THR A 236  THR A 237  ILE A 238                    
SITE     1 AC6  6 LYS A  52  TRP A  54  GLU A 109  ARG A 244                    
SITE     2 AC6  6 GLY A 245  ARG A 246                                          
SITE     1 AC7  4 ILE A 163  LEU A 195  ARG A 198  EDO A 293                    
CRYST1   48.531  111.788  139.542  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020605  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008946  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007166        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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