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Database: PDB
Entry: 4MKY
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HEADER    TRANSFERASE/DNA                         05-SEP-13   4MKY              
TITLE     POLYMERASE DOMAIN FROM MYCOBACTERIUM TUBERCULOSIS LIGASE D IN COMPLEX 
TITLE    2 WITH AN ANNEALED DOUBLE-STRAND DNA BREAK.                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA LIGASE-LIKE PROTEIN RV0938/MT0965;                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: 5'-D(P*DGP*DCP*DGP*DGP*DC)-3';                             
COMPND   7 CHAIN: E, G, I, K;                                                   
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: 5'-D(*DGP*DCP*DCP*DGP*DCP*DAP*DGP*DTP*DAP*DC)-3';          
COMPND  11 CHAIN: F, H, J, L;                                                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: MT0965, MTCY08D9.01C, MTCY10D7.36C, RV0938;                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: SYNTHESISED DNA;                                      
SOURCE  14 MOL_ID: 3;                                                           
SOURCE  15 SYNTHETIC: YES;                                                      
SOURCE  16 OTHER_DETAILS: SYNTHESISED DNA                                       
KEYWDS    PROTEIN-DNA COMPLEX, TRANSFERASE-DNA COMPLEX, NUCLEOTIDE-BINDING,     
KEYWDS   2 POLYMERASE, PRIMASE, TRANSFERASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.C.BRISSETT,A.J.DOHERTY                                              
REVDAT   2   08-JAN-14 4MKY    1       JRNL                                     
REVDAT   1   11-DEC-13 4MKY    0                                                
JRNL        AUTH   N.C.BRISSETT,M.J.MARTIN,E.J.BARTLETT,J.BIANCHI,L.BLANCO,     
JRNL        AUTH 2 A.J.DOHERTY                                                  
JRNL        TITL   MOLECULAR BASIS FOR DNA DOUBLE-STRAND BREAK ANNEALING AND    
JRNL        TITL 2 PRIMER EXTENSION BY AN NHEJ DNA POLYMERASE.                  
JRNL        REF    CELL REP                      V.   5  1108 2013              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   24239356                                                     
JRNL        DOI    10.1016/J.CELREP.2013.10.016                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 37.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 55990                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2951                            
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) : 3833                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 202                          
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8680                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1060                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 196                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 19.02000                                             
REMARK   3    B22 (A**2) : 40.65000                                             
REMARK   3    B33 (A**2) : -59.67000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -6.55000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.080         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.054         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.140         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.616        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10064 ; 0.009 ; 0.018       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13945 ; 1.268 ; 1.862       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1131 ; 6.164 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   363 ;31.837 ;22.617       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1391 ;17.860 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;19.128 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1555 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7308 ; 0.018 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  4536 ; 0.908 ; 2.266       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5663 ; 1.400 ; 3.817       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5528 ; 1.113 ; 2.328       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1      A    10   291       B    10    291      330  0.25  0.05    
REMARK   3    2      A    10   293       C    10    293      337  0.26  0.05    
REMARK   3    3      A    10   293       D    10    293      347  0.25  0.05    
REMARK   3    4      B    10   291       C    10    291      331  0.27  0.05    
REMARK   3    5      B    10   291       D    10    291      327  0.25  0.05    
REMARK   3    6      C    10   293       D    10    293      336  0.26  0.05    
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.710                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : H, -K, -H-L                                     
REMARK   3      TWIN FRACTION : 0.290                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   446                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.5717 -41.1871  33.1511              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1402 T22:   0.1102                                     
REMARK   3      T33:   0.3521 T12:  -0.0072                                     
REMARK   3      T13:   0.0606 T23:   0.0462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5953 L22:   1.2905                                     
REMARK   3      L33:   1.9775 L12:   0.1093                                     
REMARK   3      L13:   0.4156 L23:  -0.1096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0189 S12:  -0.2010 S13:  -0.0818                       
REMARK   3      S21:   0.2235 S22:  -0.0815 S23:  -0.1835                       
REMARK   3      S31:   0.0138 S32:   0.2634 S33:   0.0626                       
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    10        B   292                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.0887 -40.5538  32.8619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2525 T22:   0.2566                                     
REMARK   3      T33:   0.4161 T12:  -0.0096                                     
REMARK   3      T13:   0.0647 T23:  -0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0054 L22:   1.2161                                     
REMARK   3      L33:   1.9353 L12:   0.1022                                     
REMARK   3      L13:  -0.3164 L23:   0.2086                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0194 S12:  -0.3887 S13:   0.0891                       
REMARK   3      S21:   0.2934 S22:   0.0070 S23:   0.0876                       
REMARK   3      S31:   0.0345 S32:  -0.2653 S33:  -0.0264                       
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    10        C   440                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.8753   0.9487  11.1152              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2303 T22:   0.1213                                     
REMARK   3      T33:   0.4038 T12:   0.0589                                     
REMARK   3      T13:   0.0709 T23:   0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4442 L22:   1.3960                                     
REMARK   3      L33:   1.7237 L12:   0.0812                                     
REMARK   3      L13:   0.2651 L23:   0.0898                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0974 S12:  -0.3663 S13:  -0.1535                       
REMARK   3      S21:   0.2969 S22:   0.0649 S23:  -0.1774                       
REMARK   3      S31:  -0.1428 S32:   0.0914 S33:   0.0325                       
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    10        D   456                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1990   0.0252  11.3345              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0718 T22:   0.0053                                     
REMARK   3      T33:   0.3126 T12:  -0.0094                                     
REMARK   3      T13:   0.0703 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2289 L22:   1.4938                                     
REMARK   3      L33:   2.0402 L12:  -0.0818                                     
REMARK   3      L13:  -0.4002 L23:   0.0222                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0522 S12:   0.0257 S13:   0.0661                       
REMARK   3      S21:   0.0707 S22:  -0.0279 S23:   0.0204                       
REMARK   3      S31:   0.0026 S32:  -0.0770 S33:  -0.0243                       
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     3                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1378 -40.9043  58.3955              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5097 T22:   0.4146                                     
REMARK   3      T33:   0.4352 T12:  -0.0340                                     
REMARK   3      T13:   0.0552 T23:  -0.1010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  20.1476 L22:   0.2867                                     
REMARK   3      L33:  11.3736 L12:  -2.2371                                     
REMARK   3      L13:   8.6692 L23:  -0.4307                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1213 S12:   0.0697 S13:  -0.2318                       
REMARK   3      S21:  -0.0103 S22:  -0.0112 S23:   0.0443                       
REMARK   3      S31:  -0.1246 S32:   0.2525 S33:  -0.1101                       
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 :   G     1        G   101                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3907 -38.1593  58.4494              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3339 T22:   0.3409                                     
REMARK   3      T33:   0.4105 T12:  -0.0254                                     
REMARK   3      T13:  -0.0508 T23:   0.0970                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.0722 L22:   0.3194                                     
REMARK   3      L33:   5.4752 L12:  -0.6219                                     
REMARK   3      L13:  -2.2394 L23:  -1.1573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0121 S12:  -0.0931 S13:   0.1086                       
REMARK   3      S21:   0.0811 S22:  -0.0899 S23:  -0.0478                       
REMARK   3      S31:  -0.3289 S32:   0.3580 S33:   0.1020                       
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 :   I     1        I     3                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.8849   2.9406  36.6194              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5794 T22:   0.5413                                     
REMARK   3      T33:   0.6561 T12:   0.0113                                     
REMARK   3      T13:  -0.1011 T23:   0.1121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8455 L22:  10.5433                                     
REMARK   3      L33:   2.0148 L12:   5.1658                                     
REMARK   3      L13:   1.3023 L23:   3.5440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0906 S12:  -0.4967 S13:  -0.1732                       
REMARK   3      S21:   0.1350 S22:  -0.3484 S23:  -0.4049                       
REMARK   3      S31:  -0.0290 S32:   0.3491 S33:   0.2577                       
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 :   K     1        K   102                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5642  -2.5353  36.5655              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6862 T22:   0.2141                                     
REMARK   3      T33:   0.3709 T12:  -0.1678                                     
REMARK   3      T13:   0.3988 T23:  -0.1375                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  27.7860 L22:  12.9684                                     
REMARK   3      L33:   0.2744 L12: -15.6384                                     
REMARK   3      L13:   1.9115 L23:  -1.8358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2846 S12:  -0.6051 S13:  -0.4231                       
REMARK   3      S21:   1.4920 S22:  -0.1353 S23:   1.2924                       
REMARK   3      S31:  -0.2778 S32:   0.0544 S33:  -0.1494                       
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 :   F     1        F   107                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1053 -41.1572  49.8860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5899 T22:   0.4764                                     
REMARK   3      T33:   0.5569 T12:   0.0086                                     
REMARK   3      T13:   0.0048 T23:   0.0516                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1603 L22:   0.3093                                     
REMARK   3      L33:   7.2871 L12:   0.5971                                     
REMARK   3      L13:  -3.8976 L23:  -1.4258                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1082 S12:  -0.2404 S13:  -0.5835                       
REMARK   3      S21:   0.0002 S22:  -0.0272 S23:  -0.0465                       
REMARK   3      S31:   0.0623 S32:   0.0391 S33:  -0.0810                       
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 :   H     1        H   107                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2010 -38.8811  49.7550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5912 T22:   0.3384                                     
REMARK   3      T33:   0.4907 T12:   0.0113                                     
REMARK   3      T13:  -0.0048 T23:  -0.0183                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0087 L22:   1.7731                                     
REMARK   3      L33:   3.5540 L12:   1.9498                                     
REMARK   3      L13:   2.3461 L23:   2.4492                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0987 S12:   0.0034 S13:   0.4833                       
REMARK   3      S21:   0.0756 S22:  -0.2447 S23:   0.2562                       
REMARK   3      S31:   0.1343 S32:  -0.4084 S33:   0.1461                       
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 :   J     1        J   105                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.5534   1.9473  28.0542              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5707 T22:   0.5122                                     
REMARK   3      T33:   0.5284 T12:   0.0195                                     
REMARK   3      T13:   0.1206 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8121 L22:   1.8235                                     
REMARK   3      L33:   2.1086 L12:   1.8603                                     
REMARK   3      L13:   1.6858 L23:   1.9189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0536 S12:  -0.0873 S13:   0.3466                       
REMARK   3      S21:   0.0374 S22:  -0.0597 S23:   0.2218                       
REMARK   3      S31:   0.0268 S32:  -0.0359 S33:   0.1133                       
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 :   L     1        L   107                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.7413  -1.7414  27.7984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4932 T22:   0.2954                                     
REMARK   3      T33:   0.4580 T12:   0.0723                                     
REMARK   3      T13:  -0.0015 T23:   0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3833 L22:   2.1441                                     
REMARK   3      L33:   3.2146 L12:   2.2592                                     
REMARK   3      L13:  -2.3574 L23:  -2.5938                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0201 S12:   0.1310 S13:  -0.7644                       
REMARK   3      S21:  -0.0215 S22:  -0.1932 S23:  -0.2636                       
REMARK   3      S31:   0.0536 S32:   0.2774 S33:   0.1730                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.60                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4MKY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB082040.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-09                          
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 MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : VARIMAX HF                         
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58964                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 110.061                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3000                            
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) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.82500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.82500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2IRU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 200MM AMMONIUM CHLORIDE,   
REMARK 280  PH 7.5, VAPOR DIFFUSION, 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       40.05500            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F, H, G, E                      
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, L, J, K, I                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     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     GLU B     9                                                      
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 465     GLY C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     MET C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     GLU C     9                                                      
REMARK 465     ALA C   294                                                      
REMARK 465     PRO C   295                                                      
REMARK 465     VAL C   296                                                      
REMARK 465     ALA C   297                                                      
REMARK 465     ASP C   298                                                      
REMARK 465     ARG C   299                                                      
REMARK 465     LEU C   300                                                      
REMARK 465     THR C   301                                                      
REMARK 465     ARG C   302                                                      
REMARK 465     TYR C   303                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     MET D     4                                                      
REMARK 465     GLY D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     ALA D     7                                                      
REMARK 465     SER D     8                                                      
REMARK 465     GLU D     9                                                      
REMARK 465     ALA D   294                                                      
REMARK 465     PRO D   295                                                      
REMARK 465     VAL D   296                                                      
REMARK 465     ALA D   297                                                      
REMARK 465     ASP D   298                                                      
REMARK 465     ARG D   299                                                      
REMARK 465     LEU D   300                                                      
REMARK 465     THR D   301                                                      
REMARK 465     ARG D   302                                                      
REMARK 465     TYR D   303                                                      
REMARK 465      DG E     4                                                      
REMARK 465      DC E     5                                                      
REMARK 465      DG G     4                                                      
REMARK 465      DC G     5                                                      
REMARK 465      DG I     4                                                      
REMARK 465      DC I     5                                                      
REMARK 465      DG K     4                                                      
REMARK 465      DC K     5                                                      
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   N2    DG F     7     N3    DC H    10              1.66            
REMARK 500   NZ   LYS C    29     OP1   DG I     1              1.74            
REMARK 500   O4    DT J     8     N6    DA L     9              1.83            
REMARK 500   NH2  ARG C   205     O    HOH C   406              1.96            
REMARK 500   NH1  ARG B    56     OE1  GLN B   108              1.97            
REMARK 500   O    ARG C   279     OD1  ASP C   283              1.99            
REMARK 500   OD2  ASP D   142     NH2  ARG D   223              2.04            
REMARK 500   NE2  HIS B    86     O3'   DG F     7              2.04            
REMARK 500   OG1  THR A   100     O    HOH A   409              2.13            
REMARK 500   N    ASP B   187     O    HOH B   410              2.13            
REMARK 500   N3    DT J     8     N1    DA L     9              2.14            
REMARK 500   O    HIS A    86     N    SER A    88              2.15            
REMARK 500   OE1  GLU C   207     OG   SER C   216              2.15            
REMARK 500   NZ   LYS B    29     OP1   DG E     1              2.15            
REMARK 500   NH1  ARG C    56     OE1  GLU C    68              2.15            
REMARK 500   O5'   DC J     3     O    HOH J   104              2.17            
REMARK 500   OG1  THR C   217     NZ   LYS D   200              2.17            
REMARK 500   OD2  ASP B   140     O    HOH B   419              2.19            
REMARK 500   NH2  ARG A   258     O    ARG A   269              2.19            
REMARK 500   NH2  ARG D   258     O    ARG D   269              2.19            
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   O    ARG C    87     O    HOH A   423     1565     1.94            
REMARK 500   O2    DC F     2     N2    DG J     1     2646     2.19            
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 E   1   P      DG E   1   OP3    -0.124                       
REMARK 500     DG G   1   P      DG G   1   OP3    -0.120                       
REMARK 500     DG I   1   P      DG I   1   OP3    -0.124                       
REMARK 500     DG K   1   P      DG K   1   OP3    -0.129                       
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    ALA A  17      151.62    -45.42                                   
REMARK 500    TRP A  57       67.73   -112.80                                   
REMARK 500    PRO A  64      142.91    -39.89                                   
REMARK 500    ARG A  87      -60.68     55.79                                   
REMARK 500    ASP A  97       15.34   -151.37                                   
REMARK 500    PRO A 124      -78.63    -49.07                                   
REMARK 500    SER A 177      -95.45   -117.23                                   
REMARK 500    THR A 219      112.09    -38.27                                   
REMARK 500    TYR A 244       -3.85     80.06                                   
REMARK 500    ALA B  17      170.39    -54.00                                   
REMARK 500    ASP B  18       20.55     38.11                                   
REMARK 500    TRP B  57       72.38   -111.44                                   
REMARK 500    PRO B  76      140.05    -39.02                                   
REMARK 500    ARG B  87      -74.99    -12.24                                   
REMARK 500    ASP B  97       22.11   -151.68                                   
REMARK 500    PRO B 124      -70.24    -58.00                                   
REMARK 500    SER B 177     -100.74   -109.02                                   
REMARK 500    THR B 219      106.63    -40.59                                   
REMARK 500    ALA B 224      120.57    -39.12                                   
REMARK 500    GLN B 233        0.68    -69.57                                   
REMARK 500    ASP C  18      -47.31    115.97                                   
REMARK 500    TRP C  57       60.11   -117.56                                   
REMARK 500    ALA C  82      147.08   -175.78                                   
REMARK 500    ARG C  87      -50.36    -16.47                                   
REMARK 500    SER C 177      -84.40   -127.47                                   
REMARK 500    GLN C 233        1.59    -67.82                                   
REMARK 500    TYR C 244        3.24     81.93                                   
REMARK 500    VAL D  61      -17.19    -48.16                                   
REMARK 500    PRO D  76      139.13    -37.16                                   
REMARK 500    ARG D  87      -65.78     17.21                                   
REMARK 500    ASP D  97       11.57   -144.25                                   
REMARK 500    GLU D 145      126.31    -36.73                                   
REMARK 500    ALA D 150      -55.71    100.59                                   
REMARK 500    SER D 177      -93.02   -104.96                                   
REMARK 500    THR D 219      131.59    -36.94                                   
REMARK 500    ILE D 241      134.25    -39.46                                   
REMARK 500    TYR D 244        0.35     81.90                                   
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 C 432        DISTANCE =  5.31 ANGSTROMS                       
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.          
REMARK 900 RELATED ID: 2IRY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE POLYMERASE DOMAIN FROM                      
REMARK 900 MYCOBACTERIUM TUBERCULOSIS LIGASE D WITH DGTP AND MANGANESE.         
REMARK 900 RELATED ID: 2R9L   RELATED DB: PDB                                   
REMARK 900 POLYMERASE DOMAIN FROM MYCOBACTERIUM TUBERCULOSIS LIGASE D           
REMARK 900 IN COMPLEX WITH DNA                                                  
REMARK 900 RELATED ID: 3PKY   RELATED DB: PDB                                   
REMARK 900 POLYMERASE DOMAIN FROM MYCOBACTERIUM TUBERCULOSIS LIGASE D           
REMARK 900 IN COMPLEX WITH DNA, UTP AND MANGANESE.                              
DBREF  4MKY A    4   303  UNP    P71571   Y938_MYCTU       1    300             
DBREF  4MKY B    4   303  UNP    P71571   Y938_MYCTU       1    300             
DBREF  4MKY C    4   303  UNP    P71571   Y938_MYCTU       1    300             
DBREF  4MKY D    4   303  UNP    P71571   Y938_MYCTU       1    300             
DBREF  4MKY E    1     5  PDB    4MKY     4MKY             1      5             
DBREF  4MKY G    1     5  PDB    4MKY     4MKY             1      5             
DBREF  4MKY I    1     5  PDB    4MKY     4MKY             1      5             
DBREF  4MKY K    1     5  PDB    4MKY     4MKY             1      5             
DBREF  4MKY F    1    10  PDB    4MKY     4MKY             1     10             
DBREF  4MKY H    1    10  PDB    4MKY     4MKY             1     10             
DBREF  4MKY J    1    10  PDB    4MKY     4MKY             1     10             
DBREF  4MKY L    1    10  PDB    4MKY     4MKY             1     10             
SEQADV 4MKY GLY A    1  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY SER A    2  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY HIS A    3  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY GLY B    1  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY SER B    2  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY HIS B    3  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY GLY C    1  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY SER C    2  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY HIS C    3  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY GLY D    1  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY SER D    2  UNP  P71571              EXPRESSION TAG                 
SEQADV 4MKY HIS D    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                                              
SEQRES   1 C  303  GLY SER HIS MET GLY SER ALA SER GLU GLN ARG VAL THR          
SEQRES   2 C  303  LEU THR ASN ALA ASP LYS VAL LEU TYR PRO ALA THR GLY          
SEQRES   3 C  303  THR THR LYS SER ASP ILE PHE ASP TYR TYR ALA GLY VAL          
SEQRES   4 C  303  ALA GLU VAL MET LEU GLY HIS ILE ALA GLY ARG PRO ALA          
SEQRES   5 C  303  THR ARG LYS ARG TRP PRO ASN GLY VAL ASP GLN PRO ALA          
SEQRES   6 C  303  PHE PHE GLU LYS GLN LEU ALA LEU SER ALA PRO PRO TRP          
SEQRES   7 C  303  LEU SER ARG ALA THR VAL ALA HIS ARG SER GLY THR THR          
SEQRES   8 C  303  THR TYR PRO ILE ILE ASP SER ALA THR GLY LEU ALA TRP          
SEQRES   9 C  303  ILE ALA GLN GLN ALA ALA LEU GLU VAL HIS VAL PRO GLN          
SEQRES  10 C  303  TRP ARG PHE VAL ALA GLU PRO GLY SER GLY GLU LEU ASN          
SEQRES  11 C  303  PRO GLY PRO ALA THR ARG LEU VAL PHE ASP LEU ASP PRO          
SEQRES  12 C  303  GLY GLU GLY VAL MET MET ALA GLN LEU ALA GLU VAL ALA          
SEQRES  13 C  303  ARG ALA VAL ARG ASP LEU LEU ALA ASP ILE GLY LEU VAL          
SEQRES  14 C  303  THR PHE PRO VAL THR SER GLY SER LYS GLY LEU HIS LEU          
SEQRES  15 C  303  TYR THR PRO LEU ASP GLU PRO VAL SER SER ARG GLY ALA          
SEQRES  16 C  303  THR VAL LEU ALA LYS ARG VAL ALA GLN ARG LEU GLU GLN          
SEQRES  17 C  303  ALA MET PRO ALA LEU VAL THR SER THR MET THR LYS SER          
SEQRES  18 C  303  LEU ARG ALA GLY LYS VAL PHE VAL ASP TRP SER GLN ASN          
SEQRES  19 C  303  SER GLY SER LYS THR THR ILE ALA PRO TYR SER LEU ARG          
SEQRES  20 C  303  GLY ARG THR HIS PRO THR VAL ALA ALA PRO ARG THR TRP          
SEQRES  21 C  303  ALA GLU LEU ASP ASP PRO ALA LEU ARG GLN LEU SER TYR          
SEQRES  22 C  303  ASP GLU VAL LEU THR ARG ILE ALA ARG ASP GLY ASP LEU          
SEQRES  23 C  303  LEU GLU ARG LEU ASP ALA ASP ALA PRO VAL ALA ASP ARG          
SEQRES  24 C  303  LEU THR ARG TYR                                              
SEQRES   1 D  303  GLY SER HIS MET GLY SER ALA SER GLU GLN ARG VAL THR          
SEQRES   2 D  303  LEU THR ASN ALA ASP LYS VAL LEU TYR PRO ALA THR GLY          
SEQRES   3 D  303  THR THR LYS SER ASP ILE PHE ASP TYR TYR ALA GLY VAL          
SEQRES   4 D  303  ALA GLU VAL MET LEU GLY HIS ILE ALA GLY ARG PRO ALA          
SEQRES   5 D  303  THR ARG LYS ARG TRP PRO ASN GLY VAL ASP GLN PRO ALA          
SEQRES   6 D  303  PHE PHE GLU LYS GLN LEU ALA LEU SER ALA PRO PRO TRP          
SEQRES   7 D  303  LEU SER ARG ALA THR VAL ALA HIS ARG SER GLY THR THR          
SEQRES   8 D  303  THR TYR PRO ILE ILE ASP SER ALA THR GLY LEU ALA TRP          
SEQRES   9 D  303  ILE ALA GLN GLN ALA ALA LEU GLU VAL HIS VAL PRO GLN          
SEQRES  10 D  303  TRP ARG PHE VAL ALA GLU PRO GLY SER GLY GLU LEU ASN          
SEQRES  11 D  303  PRO GLY PRO ALA THR ARG LEU VAL PHE ASP LEU ASP PRO          
SEQRES  12 D  303  GLY GLU GLY VAL MET MET ALA GLN LEU ALA GLU VAL ALA          
SEQRES  13 D  303  ARG ALA VAL ARG ASP LEU LEU ALA ASP ILE GLY LEU VAL          
SEQRES  14 D  303  THR PHE PRO VAL THR SER GLY SER LYS GLY LEU HIS LEU          
SEQRES  15 D  303  TYR THR PRO LEU ASP GLU PRO VAL SER SER ARG GLY ALA          
SEQRES  16 D  303  THR VAL LEU ALA LYS ARG VAL ALA GLN ARG LEU GLU GLN          
SEQRES  17 D  303  ALA MET PRO ALA LEU VAL THR SER THR MET THR LYS SER          
SEQRES  18 D  303  LEU ARG ALA GLY LYS VAL PHE VAL ASP TRP SER GLN ASN          
SEQRES  19 D  303  SER GLY SER LYS THR THR ILE ALA PRO TYR SER LEU ARG          
SEQRES  20 D  303  GLY ARG THR HIS PRO THR VAL ALA ALA PRO ARG THR TRP          
SEQRES  21 D  303  ALA GLU LEU ASP ASP PRO ALA LEU ARG GLN LEU SER TYR          
SEQRES  22 D  303  ASP GLU VAL LEU THR ARG ILE ALA ARG ASP GLY ASP LEU          
SEQRES  23 D  303  LEU GLU ARG LEU ASP ALA ASP ALA PRO VAL ALA ASP ARG          
SEQRES  24 D  303  LEU THR ARG TYR                                              
SEQRES   1 E    5   DG  DC  DG  DG  DC                                          
SEQRES   1 F   10   DG  DC  DC  DG  DC  DA  DG  DT  DA  DC                      
SEQRES   1 G    5   DG  DC  DG  DG  DC                                          
SEQRES   1 H   10   DG  DC  DC  DG  DC  DA  DG  DT  DA  DC                      
SEQRES   1 I    5   DG  DC  DG  DG  DC                                          
SEQRES   1 J   10   DG  DC  DC  DG  DC  DA  DG  DT  DA  DC                      
SEQRES   1 K    5   DG  DC  DG  DG  DC                                          
SEQRES   1 L   10   DG  DC  DC  DG  DC  DA  DG  DT  DA  DC                      
FORMUL  13  HOH   *196(H2 O)                                                    
HELIX    1   1 LYS A   29  GLY A   45  1                                  17    
HELIX    2   2 SER A   98  ALA A  109  1                                  12    
HELIX    3   3 MET A  148  ASP A  165  1                                  18    
HELIX    4   4 SER A  191  MET A  210  1                                  20    
HELIX    5   5 THR A  219  ARG A  223  5                                   5    
HELIX    6   6 TRP A  231  SER A  235  5                                   5    
HELIX    7   7 ALA A  261  ASP A  265  5                                   5    
HELIX    8   8 SER A  272  GLY A  284  1                                  13    
HELIX    9   9 LEU A  287  ALA A  292  5                                   6    
HELIX   10  10 THR B   28  VAL B   39  1                                  12    
HELIX   11  11 VAL B   39  LEU B   44  1                                   6    
HELIX   12  12 GLY B   45  ILE B   47  5                                   3    
HELIX   13  13 SER B   98  ALA B  109  1                                  12    
HELIX   14  14 MET B  148  ASP B  165  1                                  18    
HELIX   15  15 SER B  191  MET B  210  1                                  20    
HELIX   16  16 THR B  219  ARG B  223  5                                   5    
HELIX   17  17 TRP B  231  SER B  235  5                                   5    
HELIX   18  18 THR B  259  ASP B  264  1                                   6    
HELIX   19  19 TYR B  273  GLY B  284  1                                  12    
HELIX   20  20 ASP B  285  ALA B  292  5                                   8    
HELIX   21  21 THR C   28  ALA C   48  1                                  21    
HELIX   22  22 SER C   98  GLN C  108  1                                  11    
HELIX   23  23 MET C  148  ASP C  165  1                                  18    
HELIX   24  24 SER C  191  MET C  210  1                                  20    
HELIX   25  25 THR C  219  ARG C  223  5                                   5    
HELIX   26  26 TRP C  231  SER C  235  5                                   5    
HELIX   27  27 THR C  259  ASP C  264  1                                   6    
HELIX   28  28 SER C  272  GLY C  284  1                                  13    
HELIX   29  29 LYS D   29  LEU D   44  1                                  16    
HELIX   30  30 GLY D   45  ILE D   47  5                                   3    
HELIX   31  31 SER D   98  GLN D  108  1                                  11    
HELIX   32  32 ALA D  150  ASP D  165  1                                  16    
HELIX   33  33 SER D  191  MET D  210  1                                  20    
HELIX   34  34 THR D  219  ARG D  223  5                                   5    
HELIX   35  35 TRP D  231  SER D  235  5                                   5    
HELIX   36  36 THR D  259  ASP D  264  1                                   6    
HELIX   37  37 TYR D  273  GLY D  284  1                                  12    
HELIX   38  38 LEU D  287  ASP D  291  5                                   5    
SHEET    1   A 2 VAL A  20  TYR A  22  0                                        
SHEET    2   A 2 THR A  27  THR A  28 -1  O  THR A  27   N  LEU A  21           
SHEET    1   B 4 PHE A  66  GLU A  68  0                                        
SHEET    2   B 4 THR A  53  ARG A  56 -1  N  ARG A  54   O  GLU A  68           
SHEET    3   B 4 GLU A 112  VAL A 115 -1  O  HIS A 114   N  THR A  53           
SHEET    4   B 4 THR A 240  ILE A 241 -1  O  THR A 240   N  VAL A 115           
SHEET    1   C 2 SER A  80  HIS A  86  0                                        
SHEET    2   C 2 GLY A  89A ILE A  95 -1  O  THR A  91   N  VAL A  84           
SHEET    1   D 4 TRP A 118  ALA A 122  0                                        
SHEET    2   D 4 LEU A 129  PRO A 143 -1  O  ASN A 130   N  VAL A 121           
SHEET    3   D 4 VAL A 227  ASP A 230 -1  O  ASP A 230   N  ASP A 140           
SHEET    4   D 4 VAL A 214  THR A 215  1  N  THR A 215   O  VAL A 227           
SHEET    1   E 5 TRP A 118  ALA A 122  0                                        
SHEET    2   E 5 LEU A 129  PRO A 143 -1  O  ASN A 130   N  VAL A 121           
SHEET    3   E 5 LEU A 180  VAL A 190 -1  O  LEU A 180   N  LEU A 141           
SHEET    4   E 5 PHE A 171  THR A 174 -1  N  VAL A 173   O  HIS A 181           
SHEET    5   E 5 ALA A 256  PRO A 257 -1  O  ALA A 256   N  THR A 174           
SHEET    1   F 4 PHE B  66  GLU B  68  0                                        
SHEET    2   F 4 THR B  53  ARG B  56 -1  N  ARG B  54   O  GLU B  68           
SHEET    3   F 4 GLU B 112  VAL B 115 -1  O  HIS B 114   N  THR B  53           
SHEET    4   F 4 THR B 240  ILE B 241 -1  O  THR B 240   N  VAL B 115           
SHEET    1   G 2 SER B  80  HIS B  86  0                                        
SHEET    2   G 2 GLY B  89  ILE B  95 -1  O  TYR B  93   N  ALA B  82           
SHEET    1   H 4 TRP B 118  ALA B 122  0                                        
SHEET    2   H 4 LEU B 129  PRO B 143 -1  O  ASN B 130   N  VAL B 121           
SHEET    3   H 4 VAL B 227  ASP B 230 -1  O  ASP B 230   N  ASP B 140           
SHEET    4   H 4 VAL B 214  THR B 215  1  N  THR B 215   O  VAL B 229           
SHEET    1   I 5 TRP B 118  ALA B 122  0                                        
SHEET    2   I 5 LEU B 129  PRO B 143 -1  O  ASN B 130   N  VAL B 121           
SHEET    3   I 5 LEU B 180  VAL B 190 -1  O  LEU B 186   N  THR B 135           
SHEET    4   I 5 PHE B 171  THR B 174 -1  N  VAL B 173   O  HIS B 181           
SHEET    5   I 5 ALA B 256  PRO B 257 -1  O  ALA B 256   N  THR B 174           
SHEET    1   J 2 THR B 253  VAL B 254  0                                        
SHEET    2   J 2 LEU B 271  SER B 272 -1  O  LEU B 271   N  VAL B 254           
SHEET    1   K 4 PHE C  66  GLU C  68  0                                        
SHEET    2   K 4 THR C  53  ARG C  56 -1  N  ARG C  54   O  GLU C  68           
SHEET    3   K 4 GLU C 112  VAL C 115 -1  O  HIS C 114   N  THR C  53           
SHEET    4   K 4 THR C 240  ILE C 241 -1  O  THR C 240   N  VAL C 115           
SHEET    1   L 2 SER C  80  HIS C  86  0                                        
SHEET    2   L 2 GLY C  89  ILE C  95 -1  O  ILE C  95   N  SER C  80           
SHEET    1   M 4 TRP C 118  ALA C 122  0                                        
SHEET    2   M 4 LEU C 129  PRO C 143 -1  O  ASN C 130   N  VAL C 121           
SHEET    3   M 4 VAL C 227  ASP C 230 -1  O  PHE C 228   N  ASP C 142           
SHEET    4   M 4 VAL C 214  THR C 215  1  N  THR C 215   O  VAL C 229           
SHEET    1   N 5 TRP C 118  ALA C 122  0                                        
SHEET    2   N 5 LEU C 129  PRO C 143 -1  O  ASN C 130   N  VAL C 121           
SHEET    3   N 5 LEU C 180  VAL C 190 -1  O  LEU C 180   N  LEU C 141           
SHEET    4   N 5 PHE C 171  THR C 174 -1  N  VAL C 173   O  HIS C 181           
SHEET    5   N 5 ALA C 256  PRO C 257 -1  O  ALA C 256   N  THR C 174           
SHEET    1   O 2 VAL D  20  TYR D  22  0                                        
SHEET    2   O 2 THR D  27  THR D  28 -1  O  THR D  27   N  LEU D  21           
SHEET    1   P 4 PHE D  66  GLU D  68  0                                        
SHEET    2   P 4 THR D  53  ARG D  56 -1  N  ARG D  56   O  PHE D  66           
SHEET    3   P 4 GLU D 112  VAL D 115 -1  O  HIS D 114   N  THR D  53           
SHEET    4   P 4 THR D 240  ILE D 241 -1  O  THR D 240   N  VAL D 115           
SHEET    1   Q 2 ARG D  81  HIS D  86  0                                        
SHEET    2   Q 2 GLY D  89  PRO D  94 -1  O  GLY D  89   N  HIS D  86           
SHEET    1   R 4 TRP D 118  ALA D 122  0                                        
SHEET    2   R 4 LEU D 129  PRO D 143 -1  O  ASN D 130   N  VAL D 121           
SHEET    3   R 4 VAL D 227  ASP D 230 -1  O  ASP D 230   N  ASP D 140           
SHEET    4   R 4 VAL D 214  THR D 215  1  N  THR D 215   O  VAL D 227           
SHEET    1   S 5 TRP D 118  ALA D 122  0                                        
SHEET    2   S 5 LEU D 129  PRO D 143 -1  O  ASN D 130   N  VAL D 121           
SHEET    3   S 5 LEU D 180  VAL D 190 -1  O  VAL D 190   N  ALA D 134           
SHEET    4   S 5 PHE D 171  THR D 174 -1  N  VAL D 173   O  HIS D 181           
SHEET    5   S 5 ALA D 256  PRO D 257 -1  O  ALA D 256   N  THR D 174           
SHEET    1   T 2 THR D 253  VAL D 254  0                                        
SHEET    2   T 2 LEU D 271  SER D 272 -1  O  LEU D 271   N  VAL D 254           
CRYST1   87.580   80.110  118.390  90.00 111.62  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011418  0.000000  0.004525        0.00000                         
SCALE2      0.000000  0.012483  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009086        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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