GenomeNet

Database: PDB
Entry: 4ESJ
LinkDB: 4ESJ
Original site: 4ESJ 
HEADER    HYDROLASE/DNA                           23-APR-12   4ESJ              
TITLE     RESTRICTION ENDONUCLEASE DPNI IN COMPLEX WITH TARGET DNA              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYPE-2 RESTRICTION ENZYME DPNI;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: R.DPNI, ENDONUCLEASE DPNI, TYPE II RESTRICTION ENZYME DPNI; 
COMPND   5 EC: 3.1.21.4;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-D(*CP*TP*GP*GP*(6MA)P*TP*CP*CP*AP*G)-3');          
COMPND   9 CHAIN: C, D, E, F;                                                   
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 170187;                                              
SOURCE   4 STRAIN: TIGR4;                                                       
SOURCE   5 GENE: DPNC, SPR1665;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ER2925;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_TAXID: 32630;                                               
SOURCE  14 OTHER_DETAILS: SYNTHETIC OLIGONUCLEOTIDE                             
KEYWDS    RESTRICTION ENDONUCLEASE-DNA COMPLEX, TYPE IIM, TYPE IIE, RESTRICTION 
KEYWDS   2 ENZYME, DPNI, METHYLATION DEPENDENT, N6-METHYLADENINE, PD-(D/E)XK    
KEYWDS   3 TYPE ENDONUCLEASE, WINGED HELIX DOMAIN, RESTRICTION ENDONUCLEASE,    
KEYWDS   4 DNA BINDING, HYDROLASE-DNA COMPLEX                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.SIWEK,H.CZAPINSKA,M.BOCHTLER,J.M.BUJNICKI,K.SKOWRONEK               
REVDAT   2   17-OCT-12 4ESJ    1       JRNL                                     
REVDAT   1   13-JUN-12 4ESJ    0                                                
JRNL        AUTH   W.SIWEK,H.CZAPINSKA,M.BOCHTLER,J.M.BUJNICKI,K.SKOWRONEK      
JRNL        TITL   CRYSTAL STRUCTURE AND MECHANISM OF ACTION OF THE             
JRNL        TITL 2 N6-METHYLADENINE-DEPENDENT TYPE IIM RESTRICTION ENDONUCLEASE 
JRNL        TITL 3 R.DPNI.                                                      
JRNL        REF    NUCLEIC ACIDS RES.            V.  40  7563 2012              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   22610857                                                     
JRNL        DOI    10.1093/NAR/GKS428                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 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) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 60188                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3032                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4178                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 214                          
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4036                                    
REMARK   3   NUCLEIC ACID ATOMS       : 730                                     
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 197                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.45000                                              
REMARK   3    B22 (A**2) : -0.44000                                             
REMARK   3    B33 (A**2) : -0.62000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.81000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.156         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.137         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5183 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3449 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7150 ; 1.240 ; 2.134       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8425 ; 3.954 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   532 ; 6.112 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   228 ;37.568 ;24.518       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   831 ;14.768 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;19.503 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   753 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5311 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   997 ; 0.007 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   895 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3331 ; 0.246 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2423 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2225 ; 0.109 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   198 ; 0.123 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.249 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    18 ; 0.183 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    78 ; 0.283 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    25 ; 0.181 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     1 ; 0.239 ; 0.200       
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):  2581 ; 0.657 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1032 ; 0.000 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4215 ; 1.201 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2602 ; 1.736 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2935 ; 2.725 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -1        A   182                          
REMARK   3    RESIDUE RANGE :   A   301        A   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0960  20.6740  -5.2800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1902 T22:  -0.0816                                     
REMARK   3      T33:   0.0579 T12:  -0.0484                                     
REMARK   3      T13:  -0.0602 T23:   0.0631                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9433 L22:   2.2749                                     
REMARK   3      L33:   0.9341 L12:   1.4461                                     
REMARK   3      L13:   0.4369 L23:   0.2279                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0840 S12:  -0.0124 S13:  -0.0091                       
REMARK   3      S21:  -0.0852 S22:   0.0316 S23:  -0.0923                       
REMARK   3      S31:  -0.1435 S32:   0.2281 S33:   0.0525                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   183        A   254                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.6290  39.1120   9.0060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1977 T22:   0.0019                                     
REMARK   3      T33:  -0.0009 T12:  -0.1619                                     
REMARK   3      T13:  -0.0252 T23:   0.0255                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0298 L22:   5.2341                                     
REMARK   3      L33:   2.3816 L12:   1.7685                                     
REMARK   3      L13:   0.3665 L23:   0.3268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2369 S12:  -0.5374 S13:   0.0174                       
REMARK   3      S21:   0.3173 S22:  -0.1256 S23:   0.3042                       
REMARK   3      S31:   0.3152 S32:  -0.3396 S33:  -0.1113                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   182                          
REMARK   3    RESIDUE RANGE :   B   301        B   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.7920  10.7080  28.6810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1062 T22:  -0.0850                                     
REMARK   3      T33:   0.0492 T12:  -0.0012                                     
REMARK   3      T13:  -0.1000 T23:  -0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6100 L22:   2.7522                                     
REMARK   3      L33:   3.3425 L12:   1.3296                                     
REMARK   3      L13:   1.6435 L23:   0.9852                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1889 S12:  -0.0567 S13:  -0.2138                       
REMARK   3      S21:   0.4516 S22:   0.0526 S23:  -0.2363                       
REMARK   3      S31:   0.1956 S32:   0.1590 S33:  -0.2415                       
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 :   B   183        B   254                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.0310  25.9510  50.0800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0147 T22:  -0.0616                                     
REMARK   3      T33:  -0.1684 T12:  -0.2056                                     
REMARK   3      T13:  -0.0573 T23:  -0.0990                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7732 L22:   7.2877                                     
REMARK   3      L33:   8.0794 L12:   1.9756                                     
REMARK   3      L13:   0.1882 L23:   2.8860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6462 S12:  -0.5814 S13:  -0.1607                       
REMARK   3      S21:   0.1442 S22:  -0.1996 S23:  -0.1701                       
REMARK   3      S31:   0.3043 S32:   0.2283 S33:  -0.4466                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C    10                          
REMARK   3    RESIDUE RANGE :   D     1        D    10                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.3000  48.5330   2.7710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1827 T22:  -0.0440                                     
REMARK   3      T33:   0.0037 T12:  -0.0619                                     
REMARK   3      T13:  -0.0312 T23:  -0.0615                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6037 L22:   3.0645                                     
REMARK   3      L33:   1.7288 L12:   0.7838                                     
REMARK   3      L13:   0.1852 L23:   0.1169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0307 S12:   0.0909 S13:   0.0505                       
REMARK   3      S21:   0.0308 S22:   0.0806 S23:  -0.0919                       
REMARK   3      S31:   0.1248 S32:  -0.1587 S33:  -0.1113                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     3        E    10                          
REMARK   3    RESIDUE RANGE :   F     1        F     8                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.2700  39.1410  52.2130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0709 T22:   0.0876                                     
REMARK   3      T33:  -0.0764 T12:  -0.3151                                     
REMARK   3      T13:   0.1144 T23:  -0.1897                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7575 L22:   7.6548                                     
REMARK   3      L33:   9.8561 L12:  -0.1684                                     
REMARK   3      L13:  -1.5812 L23:   6.3896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1073 S12:  -0.0045 S13:   0.3431                       
REMARK   3      S21:  -0.6290 S22:   0.6961 S23:  -0.7602                       
REMARK   3      S31:  -0.3177 S32:   0.3384 S33:  -0.5888                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: PROGRAM CNS HAS BEEN USED FOR DNA         
REMARK   3  REFINEMENT. NO SUGAR PUCKER CONSTRAINTS HAVE BEEN APPLIED.          
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. TLS REFINEMENT   
REMARK   3  HAS BEEN USED.                                                      
REMARK   4                                                                      
REMARK   4 4ESJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072015.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949,1.2833,1.2835              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : BENT MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC Q315                          
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60190                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.02800                            
REMARK 200  R SYM                      (I) : 0.02800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.30000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXD/E, DM, ARP/WARP                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM POTASSIUM SULFATE, 100 MM         
REMARK 280  BETAINE, 20 % W/V PEG 3350, PH 6.8. FOR CRYOCOOLING THE             
REMARK 280  CRYSTALLIZATION BUFFER WAS MIXED IN 3:1 RATIO WITH 100% GLYCEROL,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       65.25900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.20550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       65.25900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.20550            
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 300 REMARK: BIOLOGICAL UNIT CONTAINS A MONOMERIC PROTEIN AND DOUBLE      
REMARK 300 STRANDED DNA FRAGMENT BOUND TO ITS C-TERMINAL WINGED HELIX DOMAIN    
REMARK 300 (ASSEMBLY 1 COMPRISES CHAINS A,C,D; ASSEMBLY 2 COMPRISES CHAINS B,   
REMARK 300 E,F). TO THE BEST OF OUR KNOWLEDGE ADDITIONAL COPY OF DOUBLE         
REMARK 300 STRANDED TARGET DNA BINDS TO THE N-TERMINAL CATALYTIC DOMAIN OF THE  
REMARK 300 ENZYME IN SOLUTION. THE TRIMER (ACCORDING TO PDB CONVENTIONS) IS A   
REMARK 300 COMPLEX OF THE MONOMERIC ENZYME WITH DOUBLE STRANDED DNA FRAGMENT    
REMARK 300 PRESENT IN THE CRYSTAL                                               
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D                               
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, F                               
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 ZN    ZN A 302  LIES ON A SPECIAL POSITION.                          
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     GLU A    46                                                      
REMARK 465     ASN A    47                                                      
REMARK 465     ASN A    48                                                      
REMARK 465     ARG A    49                                                      
REMARK 465     PRO A   131                                                      
REMARK 465     THR A   132                                                      
REMARK 465     ALA A   133                                                      
REMARK 465     ASN A   134                                                      
REMARK 465     ARG A   135                                                      
REMARK 465     ALA A   136                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     PRO B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     ASN B    47                                                      
REMARK 465     ASN B    48                                                      
REMARK 465     ARG B    49                                                      
REMARK 465     PRO B    50                                                      
REMARK 465     LEU B   129                                                      
REMARK 465     ALA B   130                                                      
REMARK 465     PRO B   131                                                      
REMARK 465     THR B   132                                                      
REMARK 465     ALA B   133                                                      
REMARK 465     ASN B   134                                                      
REMARK 465     ARG B   135                                                      
REMARK 465     ALA B   136                                                      
REMARK 465     GLY B   137                                                      
REMARK 465      DC E     1                                                      
REMARK 465      DT E     2                                                      
REMARK 465      DA F     9                                                      
REMARK 465      DG F    10                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470      DG E   3    P    OP1  OP2                                       
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     ASP A   78   CG   OD1  OD2                                       
REMARK 480     ASP B   78   CG   OD1  OD2                                       
REMARK 480     LYS B  103   CG   CD   CE   NZ                                   
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 D   3   C3' -  C2' -  C1' ANGL. DEV. =  -5.0 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    ASP A  78     -149.87   -119.70                                   
REMARK 500    LYS A 127       64.41     33.18                                   
REMARK 500    TRP A 138      108.58   -163.90                                   
REMARK 500    HIS A 225       59.16   -140.54                                   
REMARK 500    PHE B  45     -169.86    -75.39                                   
REMARK 500    ASP B  78     -158.92   -107.50                                   
REMARK 500    ASN B 104       45.14   -105.60                                   
REMARK 500    HIS B 225       58.57   -142.72                                   
REMARK 500    ARG B 248       44.66     70.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DT D   2         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A   2   OE1                                                    
REMARK 620 2 HIS A   4   ND1 108.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  37   SG                                                     
REMARK 620 2 CYS B  34   SG  114.0                                              
REMARK 620 3 CYS B  59   SG  118.4 102.3                                        
REMARK 620 4 CYS B  56   SG  102.5 111.4 108.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  59   SG                                                     
REMARK 620 2 CYS A  56   SG  110.6                                              
REMARK 620 3 CYS A  37   SG  120.1 100.3                                        
REMARK 620 4 CYS A  34   SG  101.6 108.2 115.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 101                 
DBREF  4ESJ A    1   254  UNP    P0A460   T2D1_STRR6       1    254             
DBREF  4ESJ B    1   254  UNP    P0A460   T2D1_STRR6       1    254             
DBREF  4ESJ C    1    10  PDB    4ESJ     4ESJ             1     10             
DBREF  4ESJ D    1    10  PDB    4ESJ     4ESJ             1     10             
DBREF  4ESJ E    1    10  PDB    4ESJ     4ESJ             1     10             
DBREF  4ESJ F    1    10  PDB    4ESJ     4ESJ             1     10             
SEQADV 4ESJ GLY A   -2  UNP  P0A460              EXPRESSION TAG                 
SEQADV 4ESJ PRO A   -1  UNP  P0A460              EXPRESSION TAG                 
SEQADV 4ESJ HIS A    0  UNP  P0A460              EXPRESSION TAG                 
SEQADV 4ESJ ASN A  134  UNP  P0A460    ARG   134 ENGINEERED MUTATION            
SEQADV 4ESJ GLY B   -2  UNP  P0A460              EXPRESSION TAG                 
SEQADV 4ESJ PRO B   -1  UNP  P0A460              EXPRESSION TAG                 
SEQADV 4ESJ HIS B    0  UNP  P0A460              EXPRESSION TAG                 
SEQADV 4ESJ ASN B  134  UNP  P0A460    ARG   134 ENGINEERED MUTATION            
SEQRES   1 A  257  GLY PRO HIS MET GLU LEU HIS PHE ASN LEU GLU LEU VAL          
SEQRES   2 A  257  GLU THR TYR LYS SER ASN SER GLN LYS ALA ARG ILE LEU          
SEQRES   3 A  257  THR GLU ASP TRP VAL TYR ARG GLN SER TYR CYS PRO ASN          
SEQRES   4 A  257  CYS GLY ASN ASN PRO LEU ASN HIS PHE GLU ASN ASN ARG          
SEQRES   5 A  257  PRO VAL ALA ASP PHE TYR CYS ASN HIS CYS SER GLU GLU          
SEQRES   6 A  257  PHE GLU LEU LYS SER LYS LYS GLY ASN PHE SER SER THR          
SEQRES   7 A  257  ILE ASN ASP GLY ALA TYR ALA THR MET MET LYS ARG VAL          
SEQRES   8 A  257  GLN ALA ASP ASN ASN PRO ASN PHE PHE PHE LEU THR TYR          
SEQRES   9 A  257  THR LYS ASN PHE GLU VAL ASN ASN PHE LEU VAL LEU PRO          
SEQRES  10 A  257  LYS GLN PHE VAL THR PRO LYS SER ILE ILE GLN ARG LYS          
SEQRES  11 A  257  PRO LEU ALA PRO THR ALA ASN ARG ALA GLY TRP ILE GLY          
SEQRES  12 A  257  CYS ASN ILE ASP LEU SER GLN VAL PRO SER LYS GLY ARG          
SEQRES  13 A  257  ILE PHE LEU VAL GLN ASP GLY GLN VAL ARG ASP PRO GLU          
SEQRES  14 A  257  LYS VAL THR LYS GLU PHE LYS GLN GLY LEU PHE LEU ARG          
SEQRES  15 A  257  LYS SER SER LEU SER SER ARG GLY TRP THR ILE GLU ILE          
SEQRES  16 A  257  LEU ASN CYS ILE ASP LYS ILE GLU GLY SER GLU PHE THR          
SEQRES  17 A  257  LEU GLU ASP MET TYR ARG PHE GLU SER ASP LEU LYS ASN          
SEQRES  18 A  257  ILE PHE VAL LYS ASN ASN HIS ILE LYS GLU LYS ILE ARG          
SEQRES  19 A  257  GLN GLN LEU GLN ILE LEU ARG ASP LYS GLU ILE ILE GLU          
SEQRES  20 A  257  PHE LYS GLY ARG GLY LYS TYR ARG LYS LEU                      
SEQRES   1 B  257  GLY PRO HIS MET GLU LEU HIS PHE ASN LEU GLU LEU VAL          
SEQRES   2 B  257  GLU THR TYR LYS SER ASN SER GLN LYS ALA ARG ILE LEU          
SEQRES   3 B  257  THR GLU ASP TRP VAL TYR ARG GLN SER TYR CYS PRO ASN          
SEQRES   4 B  257  CYS GLY ASN ASN PRO LEU ASN HIS PHE GLU ASN ASN ARG          
SEQRES   5 B  257  PRO VAL ALA ASP PHE TYR CYS ASN HIS CYS SER GLU GLU          
SEQRES   6 B  257  PHE GLU LEU LYS SER LYS LYS GLY ASN PHE SER SER THR          
SEQRES   7 B  257  ILE ASN ASP GLY ALA TYR ALA THR MET MET LYS ARG VAL          
SEQRES   8 B  257  GLN ALA ASP ASN ASN PRO ASN PHE PHE PHE LEU THR TYR          
SEQRES   9 B  257  THR LYS ASN PHE GLU VAL ASN ASN PHE LEU VAL LEU PRO          
SEQRES  10 B  257  LYS GLN PHE VAL THR PRO LYS SER ILE ILE GLN ARG LYS          
SEQRES  11 B  257  PRO LEU ALA PRO THR ALA ASN ARG ALA GLY TRP ILE GLY          
SEQRES  12 B  257  CYS ASN ILE ASP LEU SER GLN VAL PRO SER LYS GLY ARG          
SEQRES  13 B  257  ILE PHE LEU VAL GLN ASP GLY GLN VAL ARG ASP PRO GLU          
SEQRES  14 B  257  LYS VAL THR LYS GLU PHE LYS GLN GLY LEU PHE LEU ARG          
SEQRES  15 B  257  LYS SER SER LEU SER SER ARG GLY TRP THR ILE GLU ILE          
SEQRES  16 B  257  LEU ASN CYS ILE ASP LYS ILE GLU GLY SER GLU PHE THR          
SEQRES  17 B  257  LEU GLU ASP MET TYR ARG PHE GLU SER ASP LEU LYS ASN          
SEQRES  18 B  257  ILE PHE VAL LYS ASN ASN HIS ILE LYS GLU LYS ILE ARG          
SEQRES  19 B  257  GLN GLN LEU GLN ILE LEU ARG ASP LYS GLU ILE ILE GLU          
SEQRES  20 B  257  PHE LYS GLY ARG GLY LYS TYR ARG LYS LEU                      
SEQRES   1 C   10   DC  DT  DG  DG 6MA  DT  DC  DC  DA  DG                      
SEQRES   1 D   10   DC  DT  DG  DG 6MA  DT  DC  DC  DA  DG                      
SEQRES   1 E   10   DC  DT  DG  DG 6MA  DT  DC  DC  DA  DG                      
SEQRES   1 F   10   DC  DT  DG  DG 6MA  DT  DC  DC  DA  DG                      
MODRES 4ESJ 6MA C    5    A                                                     
MODRES 4ESJ 6MA D    5    A                                                     
MODRES 4ESJ 6MA E    5    A                                                     
MODRES 4ESJ 6MA F    5    A                                                     
HET    6MA  C   5      22                                                       
HET    6MA  D   5      22                                                       
HET    6MA  E   5      22                                                       
HET    6MA  F   5      22                                                       
HET     ZN  A 301       1                                                       
HET     ZN  A 302       1                                                       
HET    AZI  A 303       3                                                       
HET     ZN  B 301       1                                                       
HET    UNX  C 101       1                                                       
HET    GOL  D 101       6                                                       
HET    UNX  D 102       1                                                       
HETNAM     6MA N6-METHYL-DEOXY-ADENOSINE-5'-MONOPHOSPHATE                       
HETNAM      ZN ZINC ION                                                         
HETNAM     AZI AZIDE ION                                                        
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  6MA    4(C11 H16 N5 O6 P)                                           
FORMUL   7   ZN    3(ZN 2+)                                                     
FORMUL   9  AZI    N3 1-                                                        
FORMUL  11  UNX    2(X)                                                         
FORMUL  12  GOL    C3 H8 O3                                                     
FORMUL  14  HOH   *197(H2 O)                                                    
HELIX    1   1 ASN A    6  TYR A   13  1                                   8    
HELIX    2   2 GLN A   18  SER A   32  1                                  15    
HELIX    3   3 TYR A   81  ALA A   90  1                                  10    
HELIX    4   4 PRO A  114  VAL A  118  5                                   5    
HELIX    5   5 THR A  119  LYS A  121  5                                   3    
HELIX    6   6 SER A  146  VAL A  148  5                                   3    
HELIX    7   7 PRO A  149  ARG A  153  5                                   5    
HELIX    8   8 ASP A  164  GLY A  175  1                                  12    
HELIX    9   9 LEU A  176  SER A  181  5                                   6    
HELIX   10  10 SER A  182  ILE A  199  1                                  18    
HELIX   11  11 LEU A  206  ARG A  211  1                                   6    
HELIX   12  12 PHE A  212  PHE A  220  1                                   9    
HELIX   13  13 HIS A  225  LYS A  240  1                                  16    
HELIX   14  14 ASN B    6  TYR B   13  1                                   8    
HELIX   15  15 GLN B   18  SER B   32  1                                  15    
HELIX   16  16 TYR B   81  ALA B   90  1                                  10    
HELIX   17  17 PRO B  114  VAL B  118  5                                   5    
HELIX   18  18 THR B  119  LYS B  121  5                                   3    
HELIX   19  19 SER B  146  VAL B  148  5                                   3    
HELIX   20  20 PRO B  149  ARG B  153  5                                   5    
HELIX   21  21 ASP B  164  GLY B  175  1                                  12    
HELIX   22  22 LEU B  176  SER B  181  5                                   6    
HELIX   23  23 SER B  182  ILE B  199  1                                  18    
HELIX   24  24 LEU B  206  ARG B  211  1                                   6    
HELIX   25  25 PHE B  212  PHE B  220  1                                   9    
HELIX   26  26 HIS B  225  LYS B  240  1                                  16    
SHEET    1   A 7 ASN A  43  HIS A  44  0                                        
SHEET    2   A 7 ASP A  53  TYR A  55 -1  O  TYR A  55   N  ASN A  43           
SHEET    3   A 7 GLU A  62  LYS A  69 -1  O  PHE A  63   N  PHE A  54           
SHEET    4   A 7 ASN A  95  TYR A 101  1  O  PHE A  97   N  GLU A  64           
SHEET    5   A 7 VAL A 107  LEU A 113 -1  O  LEU A 113   N  PHE A  96           
SHEET    6   A 7 ILE A 154  GLN A 158 -1  O  LEU A 156   N  PHE A 110           
SHEET    7   A 7 GLN A 161  VAL A 162 -1  O  GLN A 161   N  GLN A 158           
SHEET    1   B 3 THR A  75  ALA A  80  0                                        
SHEET    2   B 3 TRP A 138  ASP A 144 -1  O  ILE A 143   N  ILE A  76           
SHEET    3   B 3 ILE A 123  LEU A 129 -1  N  ARG A 126   O  GLY A 140           
SHEET    1   C 3 GLU A 203  THR A 205  0                                        
SHEET    2   C 3 LYS A 250  LYS A 253 -1  O  TYR A 251   N  PHE A 204           
SHEET    3   C 3 ILE A 243  PHE A 245 -1  N  GLU A 244   O  ARG A 252           
SHEET    1   D 7 ASN B  43  HIS B  44  0                                        
SHEET    2   D 7 PHE B  54  TYR B  55 -1  O  TYR B  55   N  ASN B  43           
SHEET    3   D 7 GLU B  62  LYS B  69 -1  O  PHE B  63   N  PHE B  54           
SHEET    4   D 7 ASN B  95  TYR B 101  1  O  PHE B  97   N  GLU B  64           
SHEET    5   D 7 VAL B 107  LEU B 113 -1  O  LEU B 113   N  PHE B  96           
SHEET    6   D 7 ILE B 154  GLN B 158 -1  O  LEU B 156   N  PHE B 110           
SHEET    7   D 7 GLN B 161  VAL B 162 -1  O  GLN B 161   N  GLN B 158           
SHEET    1   E 3 THR B  75  ALA B  80  0                                        
SHEET    2   E 3 GLY B 140  ASP B 144 -1  O  ILE B 143   N  ILE B  76           
SHEET    3   E 3 ILE B 123  GLN B 125 -1  N  ILE B 124   O  ASN B 142           
SHEET    1   F 3 GLU B 203  THR B 205  0                                        
SHEET    2   F 3 LYS B 250  LYS B 253 -1  O  TYR B 251   N  PHE B 204           
SHEET    3   F 3 ILE B 243  PHE B 245 -1  N  GLU B 244   O  ARG B 252           
LINK         O3'  DG C   4                 P   6MA C   5     1555   1555  1.60  
LINK         O3' 6MA C   5                 P    DT C   6     1555   1555  1.60  
LINK         O3'  DG D   4                 P   6MA D   5     1555   1555  1.61  
LINK         O3' 6MA D   5                 P    DT D   6     1555   1555  1.61  
LINK         O3'  DG E   4                 P   6MA E   5     1555   1555  1.60  
LINK         O3' 6MA E   5                 P    DT E   6     1555   1555  1.61  
LINK         O3'  DG F   4                 P   6MA F   5     1555   1555  1.60  
LINK         O3' 6MA F   5                 P    DT F   6     1555   1555  1.61  
LINK         OE1 GLU A   2                ZN    ZN A 302     1555   1555  1.77  
LINK         ND1 HIS A   4                ZN    ZN A 302     1555   1555  2.12  
LINK         SG  CYS B  37                ZN    ZN B 301     1555   1555  2.25  
LINK         SG  CYS B  34                ZN    ZN B 301     1555   1555  2.25  
LINK         SG  CYS B  59                ZN    ZN B 301     1555   1555  2.26  
LINK         SG  CYS B  56                ZN    ZN B 301     1555   1555  2.27  
LINK         SG  CYS A  59                ZN    ZN A 301     1555   1555  2.28  
LINK         SG  CYS A  56                ZN    ZN A 301     1555   1555  2.29  
LINK         SG  CYS A  37                ZN    ZN A 301     1555   1555  2.31  
LINK         SG  CYS A  34                ZN    ZN A 301     1555   1555  2.33  
CISPEP   1 ASN A   40    PRO A   41          0        -2.56                     
CISPEP   2 ASN B   40    PRO B   41          0       -14.32                     
SITE     1 AC1  4 CYS A  34  CYS A  37  CYS A  56  CYS A  59                    
SITE     1 AC2  2 GLU A   2  HIS A   4                                          
SITE     1 AC3  7 ASN A   6  ASP A  26  ARG A  30  TYR B  29                    
SITE     2 AC3  7 ASN B  43  HIS B  44  HOH B 427                               
SITE     1 AC4  4 CYS B  34  CYS B  37  CYS B  56  CYS B  59                    
SITE     1 AC5  6 SER A  15  SER A  17  HIS A 225  HOH A 479                    
SITE     2 AC5  6 GLU B   8   DT D   6                                          
CRYST1  130.518   98.411   83.884  90.00 112.21  90.00 C 1 2 1      16          
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      0.007662  0.000000  0.003129        0.00000                         
SCALE2      0.000000  0.010161  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012877        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system