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Database: PDB
Entry: 3BQ1
LinkDB: 3BQ1
Original site: 3BQ1 
HEADER    TRANSFERASE/DNA                         19-DEC-07   3BQ1              
TITLE     INSERTION TERNARY COMPLEX OF DBH DNA POLYMERASE                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (5'-D(*DGP*DAP*DAP*DGP*DCP*DCP*DGP*DGP*DCP*DG)-3');    
COMPND   3 CHAIN: P;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 OTHER_DETAILS: PRIMER;                                               
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA (5'-                                                   
COMPND   8 D(*DT*DTP*DCP*DCP*DGP*DCP*DCP*DCP*DGP*DGP*DCP*DTP*DTP*DCP*DC)-3');   
COMPND   9 CHAIN: T;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 OTHER_DETAILS: TEMPLATE;                                             
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: DNA POLYMERASE IV;                                         
COMPND  14 CHAIN: A;                                                            
COMPND  15 SYNONYM: POL IV, DBH;                                                
COMPND  16 EC: 2.7.7.7;                                                         
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: SULFOLOBUS ACIDOCALDARIUS;                      
SOURCE   7 ORGANISM_TAXID: 2285;                                                
SOURCE   8 GENE: DBH;                                                           
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  11 EXPRESSION_SYSTEM_STRAIN: BLR(DE3)PLYSS;                             
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PKKT7                                     
KEYWDS    DNA POLYMERASE, Y-FAMILY, LESION BYPASS, SINGLE-BASE DELETION, -1     
KEYWDS   2 FRAMESHIFT, DNA DAMAGE, DNA REPAIR, DNA REPLICATION, DNA-BINDING,    
KEYWDS   3 DNA-DIRECTED DNA POLYMERASE, MAGNESIUM, METAL-BINDING, MUTATOR       
KEYWDS   4 PROTEIN, NUCLEOTIDYLTRANSFERASE, TRANSFERASE, TRANSFERASE-DNA        
KEYWDS   5 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.D.PATA,R.C.WILSON                                                   
REVDAT   4   30-AUG-23 3BQ1    1       REMARK LINK                              
REVDAT   3   13-JUL-11 3BQ1    1       VERSN                                    
REVDAT   2   24-FEB-09 3BQ1    1       VERSN                                    
REVDAT   1   08-APR-08 3BQ1    0                                                
JRNL        AUTH   R.C.WILSON,J.D.PATA                                          
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE GENERATION OF SINGLE-BASE       
JRNL        TITL 2 DELETIONS BY THE Y FAMILY DNA POLYMERASE DBH.                
JRNL        REF    MOL.CELL                      V.  29   767 2008              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   18374650                                                     
JRNL        DOI    10.1016/J.MOLCEL.2008.01.014                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 14437                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 711                             
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 257                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.13                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 6                            
REMARK   3   BIN FREE R VALUE                    : 0.3970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2719                                    
REMARK   3   NUCLEIC ACID ATOMS       : 466                                     
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 41                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.66000                                              
REMARK   3    B22 (A**2) : 0.66000                                              
REMARK   3    B33 (A**2) : -1.32000                                             
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): 1.225         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.359         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.301         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.757        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3316 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4572 ; 1.242 ; 2.181       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   343 ; 4.720 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   115 ;39.030 ;24.783       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   542 ;17.946 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;13.984 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   527 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2253 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1356 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2209 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   113 ; 0.127 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.019 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    44 ; 0.178 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.117 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1766 ; 0.339 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2786 ; 0.593 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1901 ; 0.823 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1786 ; 1.411 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
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     1        A   168                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.4731  23.7167 -16.2550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1364 T22:  -0.2609                                     
REMARK   3      T33:  -0.1699 T12:   0.1040                                     
REMARK   3      T13:   0.0034 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7732 L22:   2.9560                                     
REMARK   3      L33:   8.4046 L12:  -1.7225                                     
REMARK   3      L13:   2.8887 L23:  -2.2423                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1278 S12:  -0.1759 S13:   0.0944                       
REMARK   3      S21:   0.5939 S22:   0.2680 S23:   0.0603                       
REMARK   3      S31:  -0.1606 S32:   0.0261 S33:  -0.1402                       
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   169        A   232                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.4967   8.0272   3.1778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7697 T22:   0.3022                                     
REMARK   3      T33:   0.5936 T12:   0.1921                                     
REMARK   3      T13:   0.3154 T23:   0.0561                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2892 L22:   5.1271                                     
REMARK   3      L33:   4.4685 L12:   3.2636                                     
REMARK   3      L13:   0.5072 L23:  -0.1177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1621 S12:  -0.5781 S13:  -0.6095                       
REMARK   3      S21:   1.5075 S22:  -0.1418 S23:   1.5165                       
REMARK   3      S31:   0.6813 S32:  -0.7497 S33:   0.3039                       
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   233        A   344                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.0571  -2.7752 -25.8630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1066 T22:   0.0167                                     
REMARK   3      T33:  -0.0451 T12:   0.0255                                     
REMARK   3      T13:   0.0388 T23:   0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8478 L22:   7.4374                                     
REMARK   3      L33:   9.3826 L12:   0.3578                                     
REMARK   3      L13:   0.3188 L23:   3.7325                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3965 S12:   0.3756 S13:  -0.4833                       
REMARK   3      S21:  -0.3564 S22:   0.2454 S23:  -0.3253                       
REMARK   3      S31:   0.7984 S32:   0.1979 S33:   0.1511                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   P     1        P    10                          
REMARK   3    RESIDUE RANGE :   T     2        T    15                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0816  -2.6905 -16.7683              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3642 T22:  -0.0767                                     
REMARK   3      T33:   0.5107 T12:   0.1741                                     
REMARK   3      T13:  -0.1298 T23:   0.2685                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3760 L22:  10.4653                                     
REMARK   3      L33:   2.6938 L12:   0.3269                                     
REMARK   3      L13:   0.5364 L23:  -0.7635                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0688 S12:   0.7358 S13:   0.6858                       
REMARK   3      S21:  -0.3183 S22:   0.0520 S23:   1.8674                       
REMARK   3      S31:  -0.4840 S32:  -0.2952 S33:   0.0169                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3BQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000045824.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0809                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15669                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -0.500                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1IM4 AND 1K1Q                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-3350, CALCIUM ACETATE, GLYCEROL,     
REMARK 280  HEPES, PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       35.10500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       62.48000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       62.48000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       17.55250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       62.48000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       62.48000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       52.65750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       62.48000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       62.48000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       17.55250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       62.48000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       62.48000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       52.65750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       35.10500            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, T, A                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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      DT T     1                                                      
REMARK 465     LYS A   345                                                      
REMARK 465     THR A   346                                                      
REMARK 465     ASN A   347                                                      
REMARK 465     LEU A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     PHE A   351                                                      
REMARK 465     PHE A   352                                                      
REMARK 465     ASP A   353                                                      
REMARK 465     ILE A   354                                                      
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      DT T   2    P    OP1  OP2                                       
REMARK 470      DC T  15    C5'  C4'  O4'  C3'  O3'  C2'  C1'                   
REMARK 470      DC T  15    N1   C2   O2   N3   C4   N4   C5                    
REMARK 470      DC T  15    C6                                                  
REMARK 470     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A  37    OG1  CG2                                            
REMARK 470     LYS A  38    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     DA P   2   C3' -  C2' -  C1' ANGL. DEV. =  -6.3 DEGREES          
REMARK 500     DG P   4   O4' -  C1' -  N9  ANGL. DEV. =   3.5 DEGREES          
REMARK 500     DG P   4   C3' -  O3' -  P   ANGL. DEV. =   8.4 DEGREES          
REMARK 500     DC P   6   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT T   2   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DT T   2   C3' -  O3' -  P   ANGL. DEV. =   8.9 DEGREES          
REMARK 500     DC T   7   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DC T   8   C3' -  C2' -  C1' ANGL. DEV. =  -4.8 DEGREES          
REMARK 500     DC T   8   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DC T  11   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DT T  12   O4' -  C1' -  N1  ANGL. DEV. =   2.4 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    TYR A  10       60.16     28.61                                   
REMARK 500    ARG A  36     -162.98    -68.58                                   
REMARK 500    LYS A 220      -64.64   -146.06                                   
REMARK 500    SER A 235       36.67   -166.88                                   
REMARK 500    LEU A 293      -11.52     71.07                                   
REMARK 500    LYS A 298      135.31   -174.06                                   
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                              CA A4001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 DG3 P  11   O2B                                                    
REMARK 620 2 DG3 P  11   O2G  77.7                                              
REMARK 620 3 ASP A   7   OD2 161.2 102.9                                        
REMARK 620 4 PHE A   8   O    84.8  98.4  76.5                                  
REMARK 620 5 ASP A 105   OD2  88.4 162.0  93.9  91.7                            
REMARK 620 6 HOH A4018   O   112.0 109.9  85.7 149.3  64.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DG3 P 11                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BQ0   RELATED DB: PDB                                   
REMARK 900 PRE-INSERTION BINARY COMPLEX OF DBH                                  
REMARK 900 RELATED ID: 3BQ2   RELATED DB: PDB                                   
REMARK 900 POST-INSERTION BINARY COMPLEX OF DBH                                 
DBREF  3BQ1 A    1   354  UNP    Q4JB80   DPO4_SULAC       1    354             
DBREF  3BQ1 P    1    10  PDB    3BQ1     3BQ1             1     10             
DBREF  3BQ1 T    1    15  PDB    3BQ1     3BQ1             1     15             
SEQRES   1 P   10   DG  DA  DA  DG  DC  DC  DG  DG  DC  DG                      
SEQRES   1 T   15   DT  DT  DC  DC  DG  DC  DC  DC  DG  DG  DC  DT  DT          
SEQRES   2 T   15   DC  DC                                                      
SEQRES   1 A  354  MET ILE VAL ILE PHE VAL ASP PHE ASP TYR PHE PHE ALA          
SEQRES   2 A  354  GLN VAL GLU GLU VAL LEU ASN PRO GLN TYR LYS GLY LYS          
SEQRES   3 A  354  PRO LEU VAL VAL CYS VAL TYR SER GLY ARG THR LYS THR          
SEQRES   4 A  354  SER GLY ALA VAL ALA THR ALA ASN TYR GLU ALA ARG LYS          
SEQRES   5 A  354  LEU GLY VAL LYS ALA GLY MET PRO ILE ILE LYS ALA MET          
SEQRES   6 A  354  GLN ILE ALA PRO SER ALA ILE TYR VAL PRO MET ARG LYS          
SEQRES   7 A  354  PRO ILE TYR GLU ALA PHE SER ASN ARG ILE MET ASN LEU          
SEQRES   8 A  354  LEU ASN LYS HIS ALA ASP LYS ILE GLU VAL ALA SER ILE          
SEQRES   9 A  354  ASP GLU ALA TYR LEU ASP VAL THR ASN LYS VAL GLU GLY          
SEQRES  10 A  354  ASN PHE GLU ASN GLY ILE GLU LEU ALA ARG LYS ILE LYS          
SEQRES  11 A  354  GLN GLU ILE LEU GLU LYS GLU LYS ILE THR VAL THR VAL          
SEQRES  12 A  354  GLY VAL ALA PRO ASN LYS ILE LEU ALA LYS ILE ILE ALA          
SEQRES  13 A  354  ASP LYS SER LYS PRO ASN GLY LEU GLY VAL ILE ARG PRO          
SEQRES  14 A  354  THR GLU VAL GLN ASP PHE LEU ASN GLU LEU ASP ILE ASP          
SEQRES  15 A  354  GLU ILE PRO GLY ILE GLY SER VAL LEU ALA ARG ARG LEU          
SEQRES  16 A  354  ASN GLU LEU GLY ILE GLN LYS LEU ARG ASP ILE LEU SER          
SEQRES  17 A  354  LYS ASN TYR ASN GLU LEU GLU LYS ILE THR GLY LYS ALA          
SEQRES  18 A  354  LYS ALA LEU TYR LEU LEU LYS LEU ALA GLN ASN LYS TYR          
SEQRES  19 A  354  SER GLU PRO VAL GLU ASN LYS SER LYS ILE PRO HIS GLY          
SEQRES  20 A  354  ARG TYR LEU THR LEU PRO TYR ASN THR ARG ASP VAL LYS          
SEQRES  21 A  354  VAL ILE LEU PRO TYR LEU LYS LYS ALA ILE ASN GLU ALA          
SEQRES  22 A  354  TYR ASN LYS VAL ASN GLY ILE PRO MET ARG ILE THR VAL          
SEQRES  23 A  354  ILE ALA ILE MET GLU ASP LEU ASP ILE LEU SER LYS GLY          
SEQRES  24 A  354  LYS LYS PHE LYS HIS GLY ILE SER ILE ASP ASN ALA TYR          
SEQRES  25 A  354  LYS VAL ALA GLU ASP LEU LEU ARG GLU LEU LEU VAL ARG          
SEQRES  26 A  354  ASP LYS ARG ARG ASN VAL ARG ARG ILE GLY VAL LYS LEU          
SEQRES  27 A  354  ASP ASN ILE ILE ILE ASN LYS THR ASN LEU SER ASP PHE          
SEQRES  28 A  354  PHE ASP ILE                                                  
HET    DG3  P  11      30                                                       
HET     CA  A4001       1                                                       
HETNAM     DG3 2'-3'-DIDEOXYGUANOSINE-5'-TRIPHOSPHATE                           
HETNAM      CA CALCIUM ION                                                      
FORMUL   4  DG3    C10 H16 N5 O12 P3                                            
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  HOH   *41(H2 O)                                                     
HELIX    1   1 TYR A   10  ASN A   20  1                                  11    
HELIX    2   2 PRO A   21  LYS A   24  5                                   4    
HELIX    3   3 ASN A   47  LEU A   53  1                                   7    
HELIX    4   4 PRO A   60  ALA A   68  1                                   9    
HELIX    5   5 ARG A   77  LYS A   94  1                                  18    
HELIX    6   6 ASN A  118  LYS A  138  1                                  21    
HELIX    7   7 ASN A  148  SER A  159  1                                  12    
HELIX    8   8 GLU A  171  LEU A  179  1                                   9    
HELIX    9   9 ASP A  180  ILE A  184  5                                   5    
HELIX   10  10 GLY A  188  GLU A  197  1                                  10    
HELIX   11  11 LYS A  202  ILE A  206  5                                   5    
HELIX   12  12 ASN A  210  GLY A  219  1                                  10    
HELIX   13  13 LYS A  220  GLN A  231  1                                  12    
HELIX   14  14 ASP A  258  VAL A  277  1                                  20    
HELIX   15  15 SER A  307  ASP A  326  1                                  20    
SHEET    1   A 5 LYS A  98  SER A 103  0                                        
SHEET    2   A 5 GLU A 106  ASP A 110 -1  O  TYR A 108   N  GLU A 100           
SHEET    3   A 5 VAL A   3  PHE A   8 -1  N  VAL A   6   O  ALA A 107           
SHEET    4   A 5 VAL A 141  ALA A 146 -1  O  ALA A 146   N  VAL A   3           
SHEET    5   A 5 LEU A 164  VAL A 166  1  O  GLY A 165   N  VAL A 143           
SHEET    1   B 3 ALA A  42  ALA A  46  0                                        
SHEET    2   B 3 LEU A  28  VAL A  32 -1  N  VAL A  30   O  THR A  45           
SHEET    3   B 3 ILE A  72  PRO A  75  1  O  VAL A  74   N  CYS A  31           
SHEET    1   C 2 LYS A 241  SER A 242  0                                        
SHEET    2   C 2 ILE A 341  ILE A 342 -1  O  ILE A 341   N  SER A 242           
SHEET    1   D 4 HIS A 246  THR A 256  0                                        
SHEET    2   D 4 VAL A 331  ASP A 339 -1  O  ILE A 334   N  LEU A 250           
SHEET    3   D 4 ARG A 283  MET A 290 -1  N  ILE A 289   O  ARG A 333           
SHEET    4   D 4 ILE A 295  LYS A 301 -1  O  LEU A 296   N  ALA A 288           
LINK         O2B DG3 P  11                CA    CA A4001     1555   1555  2.40  
LINK         O2G DG3 P  11                CA    CA A4001     1555   1555  2.32  
LINK         OD2 ASP A   7                CA    CA A4001     1555   1555  2.30  
LINK         O   PHE A   8                CA    CA A4001     1555   1555  2.32  
LINK         OD2 ASP A 105                CA    CA A4001     1555   1555  2.30  
LINK        CA    CA A4001                 O   HOH A4018     1555   1555  2.98  
CISPEP   1 LYS A  160    PRO A  161          0        -5.17                     
SITE     1 AC1  4 ASP A   7  PHE A   8  ASP A 105  HOH A4018                    
SITE     1 AC2 16 ASP A   7  PHE A   8  TYR A  10  PHE A  11                    
SITE     2 AC2 16 PHE A  12  ALA A  44  THR A  45  ARG A  51                    
SITE     3 AC2 16 GLY A  58  ASP A 105  LYS A 160  HOH A4018                    
SITE     4 AC2 16  DG P  10  HOH P  29   DC T   3   DC T   4                    
CRYST1  124.960  124.960   70.210  90.00  90.00  90.00 P 41 21 2     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      0.008003  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008003  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014243        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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