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Database: PDB
Entry: 3PKY
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Original site: 3PKY 
HEADER    TRANSFERASE/DNA                         12-NOV-10   3PKY              
TITLE     POLYMERASE DOMAIN FROM MYCOBACTERIUM TUBERCULOSIS LIGASE D IN COMPLEX 
TITLE    2 WITH DNA, UTP AND MANGANESE.                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE DNA LIGASE-LIKE PROTEIN;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.7.-;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA 5'-D(P*GP*CP*GP*GP*C)-3';                              
COMPND   8 CHAIN: C;                                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: DNA 5'-D(*G*CP*CP*GP*CP*AP*AP*CP*GP*CP*AP*CP*G)-3';        
COMPND  12 CHAIN: D;                                                            
COMPND  13 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: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES                                                       
KEYWDS    PROTEIN-DNA COMPLEX, TRANSFERASE-DNA COMPLEX, NUCLEOTIDE-BINDING,     
KEYWDS   2 POLYMERASE, PRIMASE, TRANSFERASE, NHEJ                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.C.BRISSETT,G.C.FOX,R.S.PITCHER,A.J.DOHERTY                          
REVDAT   1   16-FEB-11 3PKY    0                                                
JRNL        AUTH   N.C.BRISSETT,M.J.MARTIN,R.S.PITCHER,J.BIANCHI,R.JUAREZ,      
JRNL        AUTH 2 A.J.GREEN,G.C.FOX,L.BLANCO,A.J.DOHERTY                       
JRNL        TITL   STRUCTURE OF A PRETERNARY COMPLEX INVOLVING A PROKARYOTIC    
JRNL        TITL 2 NHEJ DNA POLYMERASE.                                         
JRNL        REF    MOL.CELL                      V.  41   221 2011              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   21255731                                                     
JRNL        DOI    10.1016/J.MOLCEL.2010.12.026                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 17577                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 897                             
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1192                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.33                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.3540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4377                                    
REMARK   3   NUCLEIC ACID ATOMS       : 209                                     
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 47                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.42000                                             
REMARK   3    B22 (A**2) : -0.42000                                             
REMARK   3    B33 (A**2) : 0.85000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.415         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.320         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.000        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4770 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6567 ; 1.297 ; 2.037       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   571 ; 6.105 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   183 ;33.324 ;22.678       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   698 ;18.122 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;19.050 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   753 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3540 ; 0.006 ; 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):  2865 ; 0.388 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4622 ; 0.738 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1905 ; 1.012 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1945 ; 1.831 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      6       B     290      4                      
REMARK   3           1     A      6       A     290      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   2172 ; 0.210 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   2172 ; 0.180 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     6        A   290                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1210  60.1950   1.5790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0170 T22:   0.0486                                     
REMARK   3      T33:   0.0740 T12:  -0.0191                                     
REMARK   3      T13:  -0.0194 T23:   0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7500 L22:   3.6640                                     
REMARK   3      L33:   3.7442 L12:   0.5508                                     
REMARK   3      L13:   1.0458 L23:   1.1189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1212 S12:  -0.0457 S13:  -0.0235                       
REMARK   3      S21:  -0.1598 S22:   0.1280 S23:   0.1876                       
REMARK   3      S31:  -0.1784 S32:   0.1814 S33:  -0.0068                       
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     6        B   290                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5880  25.6940  -9.6230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0450 T22:   0.0147                                     
REMARK   3      T33:   0.0793 T12:  -0.0173                                     
REMARK   3      T13:   0.0495 T23:  -0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5552 L22:   2.7229                                     
REMARK   3      L33:   4.1059 L12:   0.4844                                     
REMARK   3      L13:   1.0674 L23:   0.9496                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1243 S12:  -0.1173 S13:   0.2102                       
REMARK   3      S21:  -0.0506 S22:  -0.1206 S23:  -0.0003                       
REMARK   3      S31:   0.1948 S32:  -0.1641 S33:  -0.0036                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   303                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2500  41.6990 -11.6520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3573 T22:   0.5356                                     
REMARK   3      T33:   0.7008 T12:   0.1498                                     
REMARK   3      T13:   0.0841 T23:   0.0814                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.8898 L22:   5.9352                                     
REMARK   3      L33:   5.3361 L12:   8.3703                                     
REMARK   3      L13:  -2.7591 L23:  -3.3165                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6818 S12:  -0.1206 S13:   0.0831                       
REMARK   3      S21:  -0.7355 S22:  -0.4810 S23:  -0.2794                       
REMARK   3      S31:   1.0733 S32:   1.1058 S33:   1.1628                       
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     1        B   303                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.1500  46.2630   4.1930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4947 T22:   0.3949                                     
REMARK   3      T33:   0.6435 T12:   0.2855                                     
REMARK   3      T13:   0.0950 T23:  -0.0525                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3723 L22:  10.9019                                     
REMARK   3      L33:   3.4469 L12:   3.5322                                     
REMARK   3      L13:  -1.8773 L23:   0.5200                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5536 S12:  -0.5565 S13:  -0.0975                       
REMARK   3      S21:   0.4912 S22:   0.0356 S23:   0.4637                       
REMARK   3      S31:   1.1902 S32:   0.9328 S33:   0.5180                       
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   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3PKY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062499.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM16                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17593                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.16100                            
REMARK 200  R SYM                      (I) : 0.16100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V)PEG 3350, 0.2 M AMMONIUM         
REMARK 280  CHLORIDE, 10MM MNCL2, PH 7.5, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 285K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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       22.48000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       11.24000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       33.72000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     VAL A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     ASP A   295                                                      
REMARK 465     ARG A   296                                                      
REMARK 465     LEU A   297                                                      
REMARK 465     THR A   298                                                      
REMARK 465     ARG A   299                                                      
REMARK 465     TYR A   300                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     VAL B   293                                                      
REMARK 465     ALA B   294                                                      
REMARK 465     ASP B   295                                                      
REMARK 465     ARG B   296                                                      
REMARK 465     LEU B   297                                                      
REMARK 465     THR B   298                                                      
REMARK 465     ARG B   299                                                      
REMARK 465     TYR B   300                                                      
REMARK 465      DG D     1                                                      
REMARK 465      DC D     8                                                      
REMARK 465      DG D     9                                                      
REMARK 465      DC D    10                                                      
REMARK 465      DA D    11                                                      
REMARK 465      DC D    12                                                      
REMARK 465      DG D    13                                                      
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      DC D   2    P    OP1  OP2  O5'  C5'  C4'  O4'                   
REMARK 470      DC D   2    C2'  C1'  N1   C2   O2   N3   C4                    
REMARK 470      DC D   2    N4   C5   C6                                        
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     LEU A   18   CD1                                                 
REMARK 480     VAL A   58   CG2                                                 
REMARK 480     LEU A   76   CD1                                                 
REMARK 480     ALA A   82   CB                                                  
REMARK 480     SER A   85   OG                                                  
REMARK 480     ALA A   96   CB                                                  
REMARK 480     ALA A  147   CB                                                  
REMARK 480     GLN A  148   CG   CD   OE1  NE2                                  
REMARK 480     LYS A  175   NZ                                                  
REMARK 480     LEU A  183   CD2                                                 
REMARK 480     LEU A  210   CD1  CD2                                            
REMARK 480     THR A  256   CG2                                                 
REMARK 480     ALA A  264   CB                                                  
REMARK 480     LEU A  265   CD2                                                 
REMARK 480     THR A  275   CG2                                                 
REMARK 480     ILE A  277   CG2  CD1                                            
REMARK 480     LEU A  284   CD1  CD2                                            
REMARK 480     THR B   10   CG2                                                 
REMARK 480     LEU B   11   CD1  CD2                                            
REMARK 480     THR B   12   CG2                                                 
REMARK 480     THR B   25   CG2                                                 
REMARK 480     LEU B   41   CD1                                                 
REMARK 480     LEU B   70   CD2                                                 
REMARK 480     ALA B   82   CB                                                  
REMARK 480     SER B   85   OG                                                  
REMARK 480     ALA B   96   CB                                                  
REMARK 480     VAL B  144   CG2                                                 
REMARK 480     ALA B  147   CB                                                  
REMARK 480     VAL B  166   CG1  CG2                                            
REMARK 480     LYS B  175   CE   NZ                                             
REMARK 480     LEU B  210   CD1  CD2                                            
REMARK 480     LEU B  219   CD1                                                 
REMARK 480     ALA B  221   CB                                                  
REMARK 480     ALA B  264   CB                                                  
REMARK 480     THR B  275   CG2                                                 
REMARK 480     ILE B  277   CD1                                                 
REMARK 480     LEU B  284   CD1                                                 
REMARK 480     ALA B  289   CB                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DG C   1   P      DG C   1   OP3    -0.134                       
REMARK 500     DC D   2   O3'    DC D   2   C3'    -0.060                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DG C   1   OP1 -  P   -  OP2 ANGL. DEV. = -14.7 DEGREES          
REMARK 500     DG C   1   O4' -  C1' -  N9  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500     DC D   5   O4' -  C1' -  N1  ANGL. DEV. =   2.8 DEGREES          
REMARK 500     DA D   7   O4' -  C1' -  N9  ANGL. DEV. =   2.6 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    ARG A  84      -98.93      8.80                                   
REMARK 500    ASP A  94       17.80   -148.60                                   
REMARK 500    GLU A 142      123.43    -38.52                                   
REMARK 500    ASP A 162       18.36    -67.34                                   
REMARK 500    ILE A 163       27.09   -146.05                                   
REMARK 500    SER A 174     -103.51   -138.08                                   
REMARK 500    TYR A 241       -0.06     88.40                                   
REMARK 500    ALA A 252       82.75    -68.97                                   
REMARK 500    ALA A 291      157.24     68.53                                   
REMARK 500    ARG B  84      -73.63    -12.03                                   
REMARK 500    ASP B  94       16.92   -150.45                                   
REMARK 500    ILE B 163       24.93   -145.24                                   
REMARK 500    SER B 174     -106.07   -120.05                                   
REMARK 500    TYR B 241        9.00     82.34                                   
REMARK 500    ALA B 252       92.09    -66.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 302  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 UTP B 301   O2A                                                    
REMARK 620 2 ASP B 139   OD1 100.8                                              
REMARK 620 3 UTP B 301   O1B  84.4 169.8                                        
REMARK 620 4 ASP B 137   OD1 103.8  85.8 101.5                                  
REMARK 620 5 UTP B 301   O3G  81.9  90.7  81.3 173.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 302  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 UTP A 301   O2A                                                    
REMARK 620 2 ASP A 137   OD1 107.3                                              
REMARK 620 3 ASP A 139   OD1  78.6  87.8                                        
REMARK 620 4 UTP A 301   O1B  92.0 105.3 165.8                                  
REMARK 620 5 UTP A 301   O3G  75.3 170.4  83.7  83.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 303  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 139   OD2                                                    
REMARK 620 2 ASP B 137   OD2  89.2                                              
REMARK 620 3 ASP B 227   OD2 101.1  86.4                                        
REMARK 620 4 UTP B 301   O2A  88.4  75.2 159.3                                  
REMARK 620 5 HOH B 305   O   161.5  72.4  76.3  88.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 303  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 137   OD2                                                    
REMARK 620 2 ASP A 139   OD2  87.3                                              
REMARK 620 3 ASP A 227   OD2  83.9  86.1                                        
REMARK 620 4 UTP A 301   O2A  84.7  81.3 163.4                                  
REMARK 620 5 HOH A 307   O   162.1  76.7 102.8  84.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UTP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UTP B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 303                  
DBREF  3PKY A    1   300  UNP    P71571   Y938_MYCTU       1    300             
DBREF  3PKY B    1   300  UNP    P71571   Y938_MYCTU       1    300             
DBREF  3PKY C    1     5  PDB    3PKY     3PKY             1      5             
DBREF  3PKY D    1    13  PDB    3PKY     3PKY             1     13             
SEQADV 3PKY GLY A   -2  UNP  P71571              EXPRESSION TAG                 
SEQADV 3PKY SER A   -1  UNP  P71571              EXPRESSION TAG                 
SEQADV 3PKY HIS A    0  UNP  P71571              EXPRESSION TAG                 
SEQADV 3PKY GLY B   -2  UNP  P71571              EXPRESSION TAG                 
SEQADV 3PKY SER B   -1  UNP  P71571              EXPRESSION TAG                 
SEQADV 3PKY HIS B    0  UNP  P71571              EXPRESSION TAG                 
SEQRES   1 A  303  GLY SER HIS MET GLY SER ALA SER GLU GLN ARG VAL THR          
SEQRES   2 A  303  LEU THR ASN ALA ASP LYS VAL LEU TYR PRO ALA THR GLY          
SEQRES   3 A  303  THR THR LYS SER ASP ILE PHE ASP TYR TYR ALA GLY VAL          
SEQRES   4 A  303  ALA GLU VAL MET LEU GLY HIS ILE ALA GLY ARG PRO ALA          
SEQRES   5 A  303  THR ARG LYS ARG TRP PRO ASN GLY VAL ASP GLN PRO ALA          
SEQRES   6 A  303  PHE PHE GLU LYS GLN LEU ALA LEU SER ALA PRO PRO TRP          
SEQRES   7 A  303  LEU SER ARG ALA THR VAL ALA HIS ARG SER GLY THR THR          
SEQRES   8 A  303  THR TYR PRO ILE ILE ASP SER ALA THR GLY LEU ALA TRP          
SEQRES   9 A  303  ILE ALA GLN GLN ALA ALA LEU GLU VAL HIS VAL PRO GLN          
SEQRES  10 A  303  TRP ARG PHE VAL ALA GLU PRO GLY SER GLY GLU LEU ASN          
SEQRES  11 A  303  PRO GLY PRO ALA THR ARG LEU VAL PHE ASP LEU ASP PRO          
SEQRES  12 A  303  GLY GLU GLY VAL MET MET ALA GLN LEU ALA GLU VAL ALA          
SEQRES  13 A  303  ARG ALA VAL ARG ASP LEU LEU ALA ASP ILE GLY LEU VAL          
SEQRES  14 A  303  THR PHE PRO VAL THR SER GLY SER LYS GLY LEU HIS LEU          
SEQRES  15 A  303  TYR THR PRO LEU ASP GLU PRO VAL SER SER ARG GLY ALA          
SEQRES  16 A  303  THR VAL LEU ALA LYS ARG VAL ALA GLN ARG LEU GLU GLN          
SEQRES  17 A  303  ALA MET PRO ALA LEU VAL THR SER THR MET THR LYS SER          
SEQRES  18 A  303  LEU ARG ALA GLY LYS VAL PHE VAL ASP TRP SER GLN ASN          
SEQRES  19 A  303  SER GLY SER LYS THR THR ILE ALA PRO TYR SER LEU ARG          
SEQRES  20 A  303  GLY ARG THR HIS PRO THR VAL ALA ALA PRO ARG THR TRP          
SEQRES  21 A  303  ALA GLU LEU ASP ASP PRO ALA LEU ARG GLN LEU SER TYR          
SEQRES  22 A  303  ASP GLU VAL LEU THR ARG ILE ALA ARG ASP GLY ASP LEU          
SEQRES  23 A  303  LEU GLU ARG LEU ASP ALA ASP ALA PRO VAL ALA ASP ARG          
SEQRES  24 A  303  LEU THR ARG TYR                                              
SEQRES   1 B  303  GLY SER HIS MET GLY SER ALA SER GLU GLN ARG VAL THR          
SEQRES   2 B  303  LEU THR ASN ALA ASP LYS VAL LEU TYR PRO ALA THR GLY          
SEQRES   3 B  303  THR THR LYS SER ASP ILE PHE ASP TYR TYR ALA GLY VAL          
SEQRES   4 B  303  ALA GLU VAL MET LEU GLY HIS ILE ALA GLY ARG PRO ALA          
SEQRES   5 B  303  THR ARG LYS ARG TRP PRO ASN GLY VAL ASP GLN PRO ALA          
SEQRES   6 B  303  PHE PHE GLU LYS GLN LEU ALA LEU SER ALA PRO PRO TRP          
SEQRES   7 B  303  LEU SER ARG ALA THR VAL ALA HIS ARG SER GLY THR THR          
SEQRES   8 B  303  THR TYR PRO ILE ILE ASP SER ALA THR GLY LEU ALA TRP          
SEQRES   9 B  303  ILE ALA GLN GLN ALA ALA LEU GLU VAL HIS VAL PRO GLN          
SEQRES  10 B  303  TRP ARG PHE VAL ALA GLU PRO GLY SER GLY GLU LEU ASN          
SEQRES  11 B  303  PRO GLY PRO ALA THR ARG LEU VAL PHE ASP LEU ASP PRO          
SEQRES  12 B  303  GLY GLU GLY VAL MET MET ALA GLN LEU ALA GLU VAL ALA          
SEQRES  13 B  303  ARG ALA VAL ARG ASP LEU LEU ALA ASP ILE GLY LEU VAL          
SEQRES  14 B  303  THR PHE PRO VAL THR SER GLY SER LYS GLY LEU HIS LEU          
SEQRES  15 B  303  TYR THR PRO LEU ASP GLU PRO VAL SER SER ARG GLY ALA          
SEQRES  16 B  303  THR VAL LEU ALA LYS ARG VAL ALA GLN ARG LEU GLU GLN          
SEQRES  17 B  303  ALA MET PRO ALA LEU VAL THR SER THR MET THR LYS SER          
SEQRES  18 B  303  LEU ARG ALA GLY LYS VAL PHE VAL ASP TRP SER GLN ASN          
SEQRES  19 B  303  SER GLY SER LYS THR THR ILE ALA PRO TYR SER LEU ARG          
SEQRES  20 B  303  GLY ARG THR HIS PRO THR VAL ALA ALA PRO ARG THR TRP          
SEQRES  21 B  303  ALA GLU LEU ASP ASP PRO ALA LEU ARG GLN LEU SER TYR          
SEQRES  22 B  303  ASP GLU VAL LEU THR ARG ILE ALA ARG ASP GLY ASP LEU          
SEQRES  23 B  303  LEU GLU ARG LEU ASP ALA ASP ALA PRO VAL ALA ASP ARG          
SEQRES  24 B  303  LEU THR ARG TYR                                              
SEQRES   1 C    5   DG  DC  DG  DG  DC                                          
SEQRES   1 D   13   DG  DC  DC  DG  DC  DA  DA  DC  DG  DC  DA  DC  DG          
HET    UTP  A 301      29                                                       
HET     MN  A 302       1                                                       
HET     MN  A 303       1                                                       
HET    UTP  B 301      29                                                       
HET     MN  B 302       1                                                       
HET     MN  B 303       1                                                       
HETNAM     UTP URIDINE 5'-TRIPHOSPHATE                                          
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   5  UTP    2(C9 H15 N2 O15 P3)                                          
FORMUL   6   MN    4(MN 2+)                                                     
FORMUL  11  HOH   *47(H2 O)                                                     
HELIX    1   1 LYS A   26  LEU A   41  1                                  16    
HELIX    2   2 GLY A   42  ILE A   44  5                                   3    
HELIX    3   3 SER A   95  GLN A  105  1                                  11    
HELIX    4   4 MET A  145  ASP A  162  1                                  18    
HELIX    5   5 SER A  188  MET A  207  1                                  20    
HELIX    6   6 TRP A  228  SER A  232  5                                   5    
HELIX    7   7 THR A  256  ASP A  261  1                                   6    
HELIX    8   8 TYR A  270  GLY A  281  1                                  12    
HELIX    9   9 LYS B   26  VAL B   36  1                                  11    
HELIX   10  10 VAL B   36  ALA B   45  1                                  10    
HELIX   11  11 SER B   95  GLN B  105  1                                  11    
HELIX   12  12 MET B  145  ASP B  162  1                                  18    
HELIX   13  13 SER B  188  MET B  207  1                                  20    
HELIX   14  14 TRP B  228  SER B  232  5                                   5    
HELIX   15  15 THR B  256  ASP B  262  5                                   7    
HELIX   16  16 TYR B  270  GLY B  281  1                                  12    
SHEET    1   A 2 VAL A  17  TYR A  19  0                                        
SHEET    2   A 2 THR A  24  THR A  25 -1  O  THR A  24   N  LEU A  18           
SHEET    1   B 4 PHE A  63  GLU A  65  0                                        
SHEET    2   B 4 THR A  50  ARG A  53 -1  N  ARG A  51   O  GLU A  65           
SHEET    3   B 4 GLU A 109  VAL A 112 -1  O  HIS A 111   N  THR A  50           
SHEET    4   B 4 THR A 237  ILE A 238 -1  O  THR A 237   N  VAL A 112           
SHEET    1   C 2 SER A  77  ALA A  82  0                                        
SHEET    2   C 2 THR A  87  ILE A  92 -1  O  TYR A  90   N  ALA A  79           
SHEET    1   D 4 TRP A 115  ALA A 119  0                                        
SHEET    2   D 4 LEU A 126  PRO A 140 -1  O  ASN A 127   N  VAL A 118           
SHEET    3   D 4 VAL A 224  ASP A 227 -1  O  PHE A 225   N  ASP A 139           
SHEET    4   D 4 VAL A 211  THR A 212  1  N  THR A 212   O  VAL A 226           
SHEET    1   E 5 TRP A 115  ALA A 119  0                                        
SHEET    2   E 5 LEU A 126  PRO A 140 -1  O  ASN A 127   N  VAL A 118           
SHEET    3   E 5 LEU A 177  VAL A 187 -1  O  LEU A 179   N  PHE A 136           
SHEET    4   E 5 PHE A 168  THR A 171 -1  N  VAL A 170   O  HIS A 178           
SHEET    5   E 5 ALA A 253  PRO A 254 -1  O  ALA A 253   N  THR A 171           
SHEET    1   F 2 THR A 250  VAL A 251  0                                        
SHEET    2   F 2 LEU A 268  SER A 269 -1  O  LEU A 268   N  VAL A 251           
SHEET    1   G 2 VAL B  17  TYR B  19  0                                        
SHEET    2   G 2 THR B  24  THR B  25 -1  O  THR B  24   N  LEU B  18           
SHEET    1   H 4 PHE B  63  GLU B  65  0                                        
SHEET    2   H 4 THR B  50  ARG B  53 -1  N  ARG B  51   O  GLU B  65           
SHEET    3   H 4 GLU B 109  VAL B 112 -1  O  HIS B 111   N  THR B  50           
SHEET    4   H 4 THR B 237  ILE B 238 -1  O  THR B 237   N  VAL B 112           
SHEET    1   I 2 SER B  77  ALA B  82  0                                        
SHEET    2   I 2 THR B  87  ILE B  92 -1  O  THR B  88   N  VAL B  81           
SHEET    1   J 4 TRP B 115  ALA B 119  0                                        
SHEET    2   J 4 LEU B 126  PRO B 140 -1  O  ASN B 127   N  VAL B 118           
SHEET    3   J 4 VAL B 224  ASP B 227 -1  O  PHE B 225   N  ASP B 139           
SHEET    4   J 4 VAL B 211  THR B 212  1  N  THR B 212   O  VAL B 224           
SHEET    1   K 5 TRP B 115  ALA B 119  0                                        
SHEET    2   K 5 LEU B 126  PRO B 140 -1  O  ASN B 127   N  VAL B 118           
SHEET    3   K 5 LEU B 177  VAL B 187 -1  O  LEU B 179   N  PHE B 136           
SHEET    4   K 5 PHE B 168  THR B 171 -1  N  VAL B 170   O  HIS B 178           
SHEET    5   K 5 ALA B 253  PRO B 254 -1  O  ALA B 253   N  THR B 171           
SHEET    1   L 2 THR B 250  VAL B 251  0                                        
SHEET    2   L 2 LEU B 268  SER B 269 -1  O  LEU B 268   N  VAL B 251           
LINK         O2A UTP B 301                MN    MN B 302     1555   1555  1.78  
LINK         OD1 ASP B 139                MN    MN B 302     1555   1555  1.87  
LINK         O2A UTP A 301                MN    MN A 302     1555   1555  1.96  
LINK         OD1 ASP A 137                MN    MN A 302     1555   1555  1.96  
LINK         OD1 ASP A 139                MN    MN A 302     1555   1555  1.98  
LINK         O1B UTP A 301                MN    MN A 302     1555   1555  2.11  
LINK         O1B UTP B 301                MN    MN B 302     1555   1555  2.20  
LINK         OD1 ASP B 137                MN    MN B 302     1555   1555  2.21  
LINK         O3G UTP A 301                MN    MN A 302     1555   1555  2.21  
LINK         O3G UTP B 301                MN    MN B 302     1555   1555  2.22  
LINK         OD2 ASP B 139                MN    MN B 303     1555   1555  2.29  
LINK         OD2 ASP A 137                MN    MN A 303     1555   1555  2.31  
LINK         OD2 ASP B 137                MN    MN B 303     1555   1555  2.33  
LINK         OD2 ASP A 139                MN    MN A 303     1555   1555  2.43  
LINK         OD2 ASP B 227                MN    MN B 303     1555   1555  2.48  
LINK         OD2 ASP A 227                MN    MN A 303     1555   1555  2.52  
LINK         O2A UTP A 301                MN    MN A 303     1555   1555  2.57  
LINK         O2A UTP B 301                MN    MN B 303     1555   1555  2.60  
LINK        MN    MN B 303                 O   HOH B 305     1555   1555  2.13  
LINK        MN    MN A 303                 O   HOH A 307     1555   1555  2.42  
SITE     1 AC1 18 PHE A  64  HIS A 111  ASP A 137  ASP A 139                    
SITE     2 AC1 18 SER A 172  SER A 174  LYS A 175  GLY A 176                    
SITE     3 AC1 18 HIS A 178  GLN A 230  THR A 236  THR A 237                    
SITE     4 AC1 18 ILE A 238  ARG A 244   MN A 302   MN A 303                    
SITE     5 AC1 18 HOH A 305   DA D   6                                          
SITE     1 AC2  4 ASP A 137  ASP A 139  HIS A 178  UTP A 301                    
SITE     1 AC3  5 ASP A 137  ASP A 139  ASP A 227  UTP A 301                    
SITE     2 AC3  5 HOH A 307                                                     
SITE     1 AC4 19 PHE B  64  HIS B 111  ASP B 137  ASP B 139                    
SITE     2 AC4 19 SER B 172  SER B 174  LYS B 175  GLY B 176                    
SITE     3 AC4 19 HIS B 178  GLN B 230  THR B 236  THR B 237                    
SITE     4 AC4 19 ILE B 238  ARG B 244   MN B 302   MN B 303                    
SITE     5 AC4 19 HOH B 305  HOH B 314   DG C   4                               
SITE     1 AC5  5 ASP B 137  ASP B 139  HIS B 178  UTP B 301                    
SITE     2 AC5  5  MN B 303                                                     
SITE     1 AC6  6 ASP B 137  ASP B 139  ASP B 227  UTP B 301                    
SITE     2 AC6  6  MN B 302  HOH B 305                                          
CRYST1  145.711  145.711   44.960  90.00  90.00  90.00 P 41          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      0.006863  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006863  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022242        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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