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Database: PDB
Entry: 5W34
LinkDB: 5W34
Original site: 5W34 
HEADER    TRANSFERASE                             07-JUN-17   5W34              
TITLE     CRYSTAL STRUCTURE OF THE RNA POLYMERASE DOMAIN (RPD) OF MYCOBACTERIUM 
TITLE    2 TUBERCULOSIS PRIMASE DNAG IN COMPLEX WITH DOUBLE-STRANDED DNA        
TITLE    3 GACCGGAAGTGG                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA PRIMASE;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.7.-;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA OLIGOMER 5'-CCACTTCCGGTC;                              
COMPND   8 CHAIN: C;                                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: DNA OLIGOMER 5'-GACCGGAAGTGG;                              
COMPND  12 CHAIN: D;                                                            
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 / 
SOURCE   3 H37RV);                                                              
SOURCE   4 ORGANISM_TAXID: 83332;                                               
SOURCE   5 STRAIN: ATCC 25618 / H37RV;                                          
SOURCE   6 GENE: DNAG, RV2343C, MTCY98.12C;                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  13 ORGANISM_TAXID: 32630;                                               
SOURCE  14 MOL_ID: 3;                                                           
SOURCE  15 SYNTHETIC: YES;                                                      
SOURCE  16 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  17 ORGANISM_TAXID: 32630                                                
KEYWDS    DNA REPLICATION, REPLISOME, TOPRIM FOLD, DNA BINDING, TRANSFERASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.HOU,O.V.TSODIKOV                                                    
REVDAT   2   18-APR-18 5W34    1       JRNL                                     
REVDAT   1   28-MAR-18 5W34    0                                                
JRNL        AUTH   C.HOU,T.BISWAS,O.V.TSODIKOV                                  
JRNL        TITL   STRUCTURES OF THE CATALYTIC DOMAIN OF BACTERIAL PRIMASE DNAG 
JRNL        TITL 2 IN COMPLEXES WITH DNA PROVIDE INSIGHT INTO KEY PRIMING       
JRNL        TITL 3 EVENTS.                                                      
JRNL        REF    BIOCHEMISTRY                  V.  57  2084 2018              
JRNL        REFN                   ISSN 1520-4995                               
JRNL        PMID   29558114                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.8B00036                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 15508                          
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) : 0.238                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 781                             
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) : 2.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1086                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 58                           
REMARK   3   BIN FREE R VALUE                    : 0.3790                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4885                                    
REMARK   3   NUCLEIC ACID ATOMS       : 252                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.86000                                              
REMARK   3    B22 (A**2) : -4.12000                                             
REMARK   3    B33 (A**2) : -0.66000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.46000                                             
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): 0.502         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.452         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.535        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5259 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4819 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7131 ; 1.130 ; 1.907       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11063 ; 0.944 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   635 ; 6.081 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   235 ;31.552 ;22.085       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   816 ;17.399 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;14.224 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   751 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5843 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1221 ; 0.001 ; 0.020       
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):  2549 ; 2.750 ; 8.962       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2548 ; 2.751 ; 8.961       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3181 ; 4.776 ;13.437       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3182 ; 4.776 ;13.438       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2710 ; 2.335 ;10.045       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2709 ; 2.336 ;10.043       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3951 ; 4.170 ;15.001       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5768 ; 7.210 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5769 ; 7.210 ;  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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 5W34 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228349.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16383                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: 5W33                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.0, 7% W/V PEG 4000,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      106.05800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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   108                                                      
REMARK 465     PRO A   109                                                      
REMARK 465     HIS A   110                                                      
REMARK 465     ASP A   307                                                      
REMARK 465     SER A   308                                                      
REMARK 465     ASP A   430                                                      
REMARK 465     VAL A   431                                                      
REMARK 465     ALA A   432                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     PRO B   109                                                      
REMARK 465     HIS B   110                                                      
REMARK 465     ALA B   432                                                      
REMARK 465      DC C    13                                                      
REMARK 465      DC C    14                                                      
REMARK 465      DT C    18                                                      
REMARK 465      DG C    22                                                      
REMARK 465      DT C    23                                                      
REMARK 465      DC C    24                                                      
REMARK 465      DG D     1                                                      
REMARK 465      DA D     2                                                      
REMARK 465      DT D    10                                                      
REMARK 465      DG D    11                                                      
REMARK 465      DG D    12                                                      
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     MET A 299    CE                                                  
REMARK 470     MET B 299    CE                                                  
REMARK 470     GLU B 386    CG   CD   OE1  OE2                                  
REMARK 470      DA C  15    P    OP1  OP2  O5'                                  
REMARK 470      DG C  21    N9   C8   N7   C5   C6   O6   C2                    
REMARK 470      DG C  21    N2   N3   C4                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 167       40.79   -154.55                                   
REMARK 500    GLU A 238       93.11    -66.40                                   
REMARK 500    LYS A 255      -50.90    -26.60                                   
REMARK 500    PHE A 310      -69.15     87.47                                   
REMARK 500    ARG A 311     -164.17    -73.97                                   
REMARK 500    GLN A 336       80.77     36.93                                   
REMARK 500    PRO A 348      151.36    -44.52                                   
REMARK 500    GLU A 386       50.76   -103.23                                   
REMARK 500    ASP A 388      -71.79    -53.50                                   
REMARK 500    ALA B 137       31.93    -88.40                                   
REMARK 500    ASP B 167       50.54   -149.13                                   
REMARK 500    LYS B 255      -58.88    -26.27                                   
REMARK 500    CYS B 288       79.49     71.19                                   
REMARK 500    LYS B 337     -178.14    -63.87                                   
REMARK 500    ASP B 349      107.29    -31.77                                   
REMARK 500    ARG B 372     -169.55   -104.03                                   
REMARK 500    SER B 391     -163.79     61.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5W33   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W35   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W36   RELATED DB: PDB                                   
DBREF  5W34 A  112   432  UNP    P9WNW1   DNAG_MYCTU     112    432             
DBREF  5W34 B  112   432  UNP    P9WNW1   DNAG_MYCTU     112    432             
DBREF  5W34 C   13    24  PDB    5W34     5W34            13     24             
DBREF  5W34 D    1    12  PDB    5W34     5W34             1     12             
SEQADV 5W34 GLY A  108  UNP  P9WNW1              EXPRESSION TAG                 
SEQADV 5W34 PRO A  109  UNP  P9WNW1              EXPRESSION TAG                 
SEQADV 5W34 HIS A  110  UNP  P9WNW1              EXPRESSION TAG                 
SEQADV 5W34 MET A  111  UNP  P9WNW1              EXPRESSION TAG                 
SEQADV 5W34 GLY B  108  UNP  P9WNW1              EXPRESSION TAG                 
SEQADV 5W34 PRO B  109  UNP  P9WNW1              EXPRESSION TAG                 
SEQADV 5W34 HIS B  110  UNP  P9WNW1              EXPRESSION TAG                 
SEQADV 5W34 MET B  111  UNP  P9WNW1              EXPRESSION TAG                 
SEQRES   1 A  325  GLY PRO HIS MET GLY SER ARG SER ARG LEU LEU ALA ALA          
SEQRES   2 A  325  ASN ALA ALA ALA ALA ALA PHE TYR ALA GLN ALA LEU GLN          
SEQRES   3 A  325  SER ASP GLU ALA ALA PRO ALA ARG GLN TYR LEU THR GLU          
SEQRES   4 A  325  ARG SER PHE ASP ALA ALA ALA ALA ARG LYS PHE GLY CYS          
SEQRES   5 A  325  GLY PHE ALA PRO SER GLY TRP ASP SER LEU THR LYS HIS          
SEQRES   6 A  325  LEU GLN ARG LYS GLY PHE GLU PHE GLU GLU LEU GLU ALA          
SEQRES   7 A  325  ALA GLY LEU SER ARG GLN GLY ARG HIS GLY PRO MET ASP          
SEQRES   8 A  325  ARG PHE HIS ARG ARG LEU LEU TRP PRO ILE ARG THR SER          
SEQRES   9 A  325  ALA GLY GLU VAL VAL GLY PHE GLY ALA ARG ARG LEU PHE          
SEQRES  10 A  325  ASP ASP ASP ALA MET GLU ALA LYS TYR VAL ASN THR PRO          
SEQRES  11 A  325  GLU THR LEU LEU TYR LYS LYS SER SER VAL MET PHE GLY          
SEQRES  12 A  325  ILE ASP LEU ALA LYS ARG ASP ILE ALA LYS GLY HIS GLN          
SEQRES  13 A  325  ALA VAL VAL VAL GLU GLY TYR THR ASP VAL MET ALA MET          
SEQRES  14 A  325  HIS LEU ALA GLY VAL THR THR ALA VAL ALA SER CYS GLY          
SEQRES  15 A  325  THR ALA PHE GLY GLY GLU HIS LEU ALA MET LEU ARG ARG          
SEQRES  16 A  325  LEU MET MET ASP ASP SER PHE PHE ARG GLY GLU LEU ILE          
SEQRES  17 A  325  TYR VAL PHE ASP GLY ASP GLU ALA GLY ARG ALA ALA ALA          
SEQRES  18 A  325  LEU LYS ALA PHE ASP GLY GLU GLN LYS LEU ALA GLY GLN          
SEQRES  19 A  325  SER PHE VAL ALA VAL ALA PRO ASP GLY MET ASP PRO CYS          
SEQRES  20 A  325  ASP LEU ARG LEU LYS CYS GLY ASP ALA ALA LEU ARG ASP          
SEQRES  21 A  325  LEU VAL ALA ARG ARG THR PRO LEU PHE GLU PHE ALA ILE          
SEQRES  22 A  325  ARG ALA ALA ILE ALA GLU MET ASP LEU ASP SER ALA GLU          
SEQRES  23 A  325  GLY ARG VAL ALA ALA LEU ARG ARG CYS VAL PRO MET VAL          
SEQRES  24 A  325  GLY GLN ILE LYS ASP PRO THR LEU ARG ASP GLU TYR ALA          
SEQRES  25 A  325  ARG GLN LEU ALA GLY TRP VAL GLY TRP ALA ASP VAL ALA          
SEQRES   1 B  325  GLY PRO HIS MET GLY SER ARG SER ARG LEU LEU ALA ALA          
SEQRES   2 B  325  ASN ALA ALA ALA ALA ALA PHE TYR ALA GLN ALA LEU GLN          
SEQRES   3 B  325  SER ASP GLU ALA ALA PRO ALA ARG GLN TYR LEU THR GLU          
SEQRES   4 B  325  ARG SER PHE ASP ALA ALA ALA ALA ARG LYS PHE GLY CYS          
SEQRES   5 B  325  GLY PHE ALA PRO SER GLY TRP ASP SER LEU THR LYS HIS          
SEQRES   6 B  325  LEU GLN ARG LYS GLY PHE GLU PHE GLU GLU LEU GLU ALA          
SEQRES   7 B  325  ALA GLY LEU SER ARG GLN GLY ARG HIS GLY PRO MET ASP          
SEQRES   8 B  325  ARG PHE HIS ARG ARG LEU LEU TRP PRO ILE ARG THR SER          
SEQRES   9 B  325  ALA GLY GLU VAL VAL GLY PHE GLY ALA ARG ARG LEU PHE          
SEQRES  10 B  325  ASP ASP ASP ALA MET GLU ALA LYS TYR VAL ASN THR PRO          
SEQRES  11 B  325  GLU THR LEU LEU TYR LYS LYS SER SER VAL MET PHE GLY          
SEQRES  12 B  325  ILE ASP LEU ALA LYS ARG ASP ILE ALA LYS GLY HIS GLN          
SEQRES  13 B  325  ALA VAL VAL VAL GLU GLY TYR THR ASP VAL MET ALA MET          
SEQRES  14 B  325  HIS LEU ALA GLY VAL THR THR ALA VAL ALA SER CYS GLY          
SEQRES  15 B  325  THR ALA PHE GLY GLY GLU HIS LEU ALA MET LEU ARG ARG          
SEQRES  16 B  325  LEU MET MET ASP ASP SER PHE PHE ARG GLY GLU LEU ILE          
SEQRES  17 B  325  TYR VAL PHE ASP GLY ASP GLU ALA GLY ARG ALA ALA ALA          
SEQRES  18 B  325  LEU LYS ALA PHE ASP GLY GLU GLN LYS LEU ALA GLY GLN          
SEQRES  19 B  325  SER PHE VAL ALA VAL ALA PRO ASP GLY MET ASP PRO CYS          
SEQRES  20 B  325  ASP LEU ARG LEU LYS CYS GLY ASP ALA ALA LEU ARG ASP          
SEQRES  21 B  325  LEU VAL ALA ARG ARG THR PRO LEU PHE GLU PHE ALA ILE          
SEQRES  22 B  325  ARG ALA ALA ILE ALA GLU MET ASP LEU ASP SER ALA GLU          
SEQRES  23 B  325  GLY ARG VAL ALA ALA LEU ARG ARG CYS VAL PRO MET VAL          
SEQRES  24 B  325  GLY GLN ILE LYS ASP PRO THR LEU ARG ASP GLU TYR ALA          
SEQRES  25 B  325  ARG GLN LEU ALA GLY TRP VAL GLY TRP ALA ASP VAL ALA          
SEQRES   1 C   12   DC  DC  DA  DC  DT  DT  DC  DC  DG  DG  DT  DC              
SEQRES   1 D   12   DG  DA  DC  DC  DG  DG  DA  DA  DG  DT  DG  DG              
HELIX    1 AA1 SER A  113  LEU A  132  1                                  20    
HELIX    2 AA2 ALA A  137  ARG A  147  1                                  11    
HELIX    3 AA3 ASP A  150  GLY A  158  1                                   9    
HELIX    4 AA4 ASP A  167  GLY A  177  1                                  11    
HELIX    5 AA5 GLU A  179  ALA A  186  1                                   8    
HELIX    6 AA6 GLY A  250  HIS A  262  1                                  13    
HELIX    7 AA7 GLY A  269  ALA A  279  1                                  11    
HELIX    8 AA8 GLY A  293  ASP A  306  1                                  14    
HELIX    9 AA9 GLU A  322  ALA A  327  1                                   6    
HELIX   10 AB1 ALA A  328  PHE A  332  5                                   5    
HELIX   11 AB2 GLN A  336  GLY A  340  5                                   5    
HELIX   12 AB3 ASP A  352  CYS A  360  1                                   9    
HELIX   13 AB4 GLY A  361  ARG A  371  1                                  11    
HELIX   14 AB5 LEU A  375  GLU A  386  1                                  12    
HELIX   15 AB6 SER A  391  CYS A  402  1                                  12    
HELIX   16 AB7 CYS A  402  ILE A  409  1                                   8    
HELIX   17 AB8 ASP A  411  VAL A  426  1                                  16    
HELIX   18 AB9 SER B  113  LEU B  132  1                                  20    
HELIX   19 AC1 ALA B  137  ARG B  147  1                                  11    
HELIX   20 AC2 ASP B  150  PHE B  157  1                                   8    
HELIX   21 AC3 LEU B  169  GLY B  177  1                                   9    
HELIX   22 AC4 GLU B  179  ALA B  186  1                                   8    
HELIX   23 AC5 GLY B  250  HIS B  262  1                                  13    
HELIX   24 AC6 GLY B  269  ALA B  279  1                                  11    
HELIX   25 AC7 GLY B  293  MET B  304  1                                  12    
HELIX   26 AC8 ASP B  321  LEU B  329  1                                   9    
HELIX   27 AC9 LYS B  330  PHE B  332  5                                   3    
HELIX   28 AD1 ASP B  352  ARG B  371  1                                  20    
HELIX   29 AD2 LEU B  375  GLU B  386  1                                  12    
HELIX   30 AD3 ALA B  392  GLN B  408  1                                  17    
HELIX   31 AD4 ASP B  411  GLY B  427  1                                  17    
SHEET    1 AA1 4 GLY A 160  ALA A 162  0                                        
SHEET    2 AA1 4 ARG A 203  ARG A 209 -1  O  LEU A 205   N  GLY A 160           
SHEET    3 AA1 4 VAL A 215  ARG A 222 -1  O  GLY A 219   N  TRP A 206           
SHEET    4 AA1 4 TYR A 233  ASN A 235 -1  O  VAL A 234   N  ALA A 220           
SHEET    1 AA2 2 SER A 189  GLY A 192  0                                        
SHEET    2 AA2 2 GLY A 195  ASP A 198 -1  O  MET A 197   N  ARG A 190           
SHEET    1 AA3 5 ALA A 284  ALA A 286  0                                        
SHEET    2 AA3 5 GLN A 263  VAL A 267  1  N  VAL A 265   O  VAL A 285           
SHEET    3 AA3 5 GLU A 313  GLY A 320  1  O  ILE A 315   N  VAL A 266           
SHEET    4 AA3 5 SER A 342  ASP A 349  1  O  PHE A 343   N  TYR A 316           
SHEET    5 AA3 5 THR A 373  PRO A 374 -1  O  THR A 373   N  VAL A 344           
SHEET    1 AA4 4 GLY B 160  ALA B 162  0                                        
SHEET    2 AA4 4 ARG B 203  ARG B 209 -1  O  LEU B 205   N  GLY B 160           
SHEET    3 AA4 4 VAL B 215  ARG B 222 -1  O  ARG B 221   N  LEU B 204           
SHEET    4 AA4 4 TYR B 233  ASN B 235 -1  O  VAL B 234   N  ALA B 220           
SHEET    1 AA5 2 SER B 189  ARG B 190  0                                        
SHEET    2 AA5 2 MET B 197  ASP B 198 -1  O  MET B 197   N  ARG B 190           
SHEET    1 AA6 5 ALA B 284  ALA B 286  0                                        
SHEET    2 AA6 5 GLN B 263  VAL B 267  1  N  VAL B 265   O  VAL B 285           
SHEET    3 AA6 5 GLU B 313  PHE B 318  1  O  ILE B 315   N  VAL B 266           
SHEET    4 AA6 5 SER B 342  VAL B 346  1  O  PHE B 343   N  TYR B 316           
SHEET    5 AA6 5 THR B 373  PRO B 374 -1  O  THR B 373   N  VAL B 344           
SHEET    1 AA7 2 MET B 305  ASP B 306  0                                        
SHEET    2 AA7 2 PHE B 309  PHE B 310 -1  O  PHE B 309   N  ASP B 306           
CRYST1   43.781  212.116   47.418  90.00 107.87  90.00 P 1 21 1      4          
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      0.022841  0.000000  0.007365        0.00000                         
SCALE2      0.000000  0.004714  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022158        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system