GenomeNet

Database: PDB
Entry: 1ZLK
LinkDB: 1ZLK
Original site: 1ZLK 
HEADER    TRANSCRIPTION/DNA                       06-MAY-05   1ZLK              
TITLE     CRYSTAL STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS HYPOXIC           
TITLE    2 RESPONSE REGULATOR DOSR C-TERMINAL DOMAIN-DNA COMPLEX                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-                                                        
COMPND   3 D(*GP*GP*CP*CP*CP*GP*CP*GP*CP*TP*TP*TP*GP*GP*GP*GP*AP*CP*TP          
COMPND   4 *AP*AP*AP*GP*TP*CP*CP*CP*TP*AP*AP*CP*CP*CP*TP*GP*GP*CP*CP*A          
COMPND   5 P*CP*GP*AP*T)-3';                                                    
COMPND   6 CHAIN: C;                                                            
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-                                                        
COMPND  10 D(*CP*GP*TP*GP*GP*CP*CP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*AP*CP          
COMPND  11 *TP*TP*TP*AP*GP*TP*CP*CP*CP*CP*AP*AP*AP*GP*CP*GP*CP*GP*GP*G          
COMPND  12 P*CP*CP*AP*T)-3';                                                    
COMPND  13 CHAIN: D;                                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: DORMANCY SURVIVAL REGULATOR;                               
COMPND  17 CHAIN: A, B;                                                         
COMPND  18 FRAGMENT: C-TERMINAL DOMAIN;                                         
COMPND  19 SYNONYM: DOSR;                                                       
COMPND  20 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: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   7 ORGANISM_TAXID: 1773;                                                
SOURCE   8 GENE: DOSR, DEVR, RV3133C;                                           
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PET28(+)                                  
KEYWDS    HELIX-TURN-HELIX, PROTEIN-DNA COMPLEX, TRANSCRIPTION/DNA              
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.WISEDCHAISRI,M.WU,A.E.RICE,D.M.ROBERTS,D.R.SHERMAN,                 
AUTHOR   2 W.G.J.HOL                                                            
REVDAT   2   24-FEB-09 1ZLK    1       VERSN                                    
REVDAT   1   31-JAN-06 1ZLK    0                                                
JRNL        AUTH   G.WISEDCHAISRI,M.WU,A.E.RICE,D.M.ROBERTS,                    
JRNL        AUTH 2 D.R.SHERMAN,W.G.J.HOL                                        
JRNL        TITL   STRUCTURES OF MYCOBACTERIUM TUBERCULOSIS DOSR AND            
JRNL        TITL 2 DOSR-DNA COMPLEX INVOLVED IN GENE ACTIVATION                 
JRNL        TITL 3 DURING ADAPTATION TO HYPOXIC LATENCY.                        
JRNL        REF    J.MOL.BIOL.                   V. 354   630 2005              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16246368                                                     
JRNL        DOI    10.1016/J.JMB.2005.09.048                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 7800                           
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) : 0.272                           
REMARK   3   R VALUE            (WORKING SET) : 0.272                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 407                             
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) : 385                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 15                           
REMARK   3   BIN FREE R VALUE                    : 0.5690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1010                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1008                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 72.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.05000                                             
REMARK   3    B22 (A**2) : -4.00000                                             
REMARK   3    B33 (A**2) : 8.37000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.86000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.996         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.499         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.394         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.638        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.892                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.865                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2148 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1471 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3104 ; 1.086 ; 2.565       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3503 ; 0.841 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   128 ; 4.242 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   313 ; 0.048 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1622 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   206 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   524 ; 0.220 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1961 ; 0.258 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1001 ; 0.088 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    67 ; 0.227 ; 0.500       
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):     7 ; 0.254 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    29 ; 0.262 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.087 ; 0.500       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    145       A     209      2                      
REMARK   3           1     B    145       B     209      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    C    (A):    384 ;  0.05 ;  0.10           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    619 ;  0.19 ;  0.40           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     14       C      19      4                      
REMARK   3           1     D     14       D      19      4                      
REMARK   3           2     C     22       C      27      4                      
REMARK   3           2     D     22       D      27      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    360 ;  0.14 ;  0.40           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1ZLK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032860.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96411                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8211                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 79.5                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
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     (%) : 60.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.030                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ZLJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, HEPES, CALCIUM CHLORIDE,        
REMARK 280  PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       71.19850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.39550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.19850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.39550            
REMARK 290   SMTRY3   4  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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS 2 BIOLOGICAL PROTEIN            
REMARK 300 MONOMERS FORMING ONE FUNCTIONAL DIMER BOUND TO DOUBLE-STRANDED       
REMARK 300 OLIGONUCLEOTIDE.                                                     
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: C, D, A, B                            
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      DG C     1                                                      
REMARK 465      DG C     2                                                      
REMARK 465      DC C     3                                                      
REMARK 465      DC C     4                                                      
REMARK 465      DC C     5                                                      
REMARK 465      DG C     6                                                      
REMARK 465      DC C     7                                                      
REMARK 465      DC C    32                                                      
REMARK 465      DC C    33                                                      
REMARK 465      DT C    34                                                      
REMARK 465      DG C    35                                                      
REMARK 465      DG C    36                                                      
REMARK 465      DC C    37                                                      
REMARK 465      DC C    38                                                      
REMARK 465      DA C    39                                                      
REMARK 465      DC C    40                                                      
REMARK 465      DG C    41                                                      
REMARK 465      DA C    42                                                      
REMARK 465      DT C    43                                                      
REMARK 465      DC D     0                                                      
REMARK 465      DG D     1                                                      
REMARK 465      DT D     2                                                      
REMARK 465      DG D     3                                                      
REMARK 465      DG D     4                                                      
REMARK 465      DC D     5                                                      
REMARK 465      DC D     6                                                      
REMARK 465      DG D    32                                                      
REMARK 465      DC D    33                                                      
REMARK 465      DG D    34                                                      
REMARK 465      DC D    35                                                      
REMARK 465      DG D    36                                                      
REMARK 465      DG D    37                                                      
REMARK 465      DG D    38                                                      
REMARK 465      DC D    39                                                      
REMARK 465      DC D    40                                                      
REMARK 465      DA D    41                                                      
REMARK 465      DT D    42                                                      
REMARK 465     MET A   123                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     SER A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     HIS A   127                                                      
REMARK 465     HIS A   128                                                      
REMARK 465     HIS A   129                                                      
REMARK 465     HIS A   130                                                      
REMARK 465     HIS A   131                                                      
REMARK 465     HIS A   132                                                      
REMARK 465     SER A   133                                                      
REMARK 465     SER A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     LEU A   136                                                      
REMARK 465     VAL A   137                                                      
REMARK 465     PRO A   138                                                      
REMARK 465     ARG A   139                                                      
REMARK 465     GLY A   140                                                      
REMARK 465     SER A   141                                                      
REMARK 465     HIS A   142                                                      
REMARK 465     MET A   143                                                      
REMARK 465     GLN A   144                                                      
REMARK 465     SER A   210                                                      
REMARK 465     ARG A   211                                                      
REMARK 465     PRO A   212                                                      
REMARK 465     PRO A   213                                                      
REMARK 465     GLY A   214                                                      
REMARK 465     ASP A   215                                                      
REMARK 465     GLY A   216                                                      
REMARK 465     PRO A   217                                                      
REMARK 465     MET B   123                                                      
REMARK 465     GLY B   124                                                      
REMARK 465     SER B   125                                                      
REMARK 465     SER B   126                                                      
REMARK 465     HIS B   127                                                      
REMARK 465     HIS B   128                                                      
REMARK 465     HIS B   129                                                      
REMARK 465     HIS B   130                                                      
REMARK 465     HIS B   131                                                      
REMARK 465     HIS B   132                                                      
REMARK 465     SER B   133                                                      
REMARK 465     SER B   134                                                      
REMARK 465     GLY B   135                                                      
REMARK 465     LEU B   136                                                      
REMARK 465     VAL B   137                                                      
REMARK 465     PRO B   138                                                      
REMARK 465     ARG B   139                                                      
REMARK 465     GLY B   140                                                      
REMARK 465     SER B   141                                                      
REMARK 465     HIS B   142                                                      
REMARK 465     MET B   143                                                      
REMARK 465     GLN B   144                                                      
REMARK 465     SER B   210                                                      
REMARK 465     ARG B   211                                                      
REMARK 465     PRO B   212                                                      
REMARK 465     PRO B   213                                                      
REMARK 465     GLY B   214                                                      
REMARK 465     ASP B   215                                                      
REMARK 465     GLY B   216                                                      
REMARK 465     PRO B   217                                                      
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     ARG A 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 209    CG   CD   NE   CZ   NH1  NH2                        
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     DC C   9   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DG C  14   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DA C  17   O4' -  C1' -  N9  ANGL. DEV. =   3.4 DEGREES          
REMARK 500     DA C  20   O4' -  C1' -  N9  ANGL. DEV. =   3.9 DEGREES          
REMARK 500     DA C  21   O4' -  C1' -  N9  ANGL. DEV. =   3.3 DEGREES          
REMARK 500     DC C  26   C3' -  C2' -  C1' ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     DC C  26   O4' -  C1' -  N1  ANGL. DEV. =   4.8 DEGREES          
REMARK 500     DC C  27   O4' -  C1' -  N1  ANGL. DEV. =   3.8 DEGREES          
REMARK 500     DT C  28   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DT D  11   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DG D  14   O4' -  C1' -  N9  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DA D  17   O4' -  C1' -  N9  ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DC D  26   O4' -  C1' -  N1  ANGL. DEV. =   4.8 DEGREES          
REMARK 500     DC D  27   O4' -  C1' -  N1  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DC D  28   O4' -  C1' -  N1  ANGL. DEV. =   2.7 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    THR A 151     -174.27    -61.98                                   
REMARK 500    THR B 151     -173.30    -64.48                                   
REMARK 500    ASP B 152      -70.67    -45.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ZLJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS HYPOXIC          
REMARK 900 RESPONSE REGULATOR DOSR C-TERMINAL DOMAIN                            
DBREF  1ZLK A  144   217  GB     15610269 NP_217649      144    217             
DBREF  1ZLK B  144   217  GB     15610269 NP_217649      144    217             
DBREF  1ZLK C    1    43  PDB    1ZLK     1ZLK             1     43             
DBREF  1ZLK D    0    42  PDB    1ZLK     1ZLK             0     42             
SEQADV 1ZLK MET A  123  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK GLY A  124  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK SER A  125  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK SER A  126  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK HIS A  127  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK HIS A  128  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK HIS A  129  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK HIS A  130  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK HIS A  131  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK HIS A  132  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK SER A  133  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK SER A  134  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK GLY A  135  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK LEU A  136  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK VAL A  137  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK PRO A  138  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK ARG A  139  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK GLY A  140  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK SER A  141  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK HIS A  142  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK MET A  143  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK MET B  123  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK GLY B  124  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK SER B  125  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK SER B  126  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK HIS B  127  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK HIS B  128  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK HIS B  129  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK HIS B  130  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK HIS B  131  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK HIS B  132  GB   15610269            EXPRESSION TAG                 
SEQADV 1ZLK SER B  133  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK SER B  134  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK GLY B  135  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK LEU B  136  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK VAL B  137  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK PRO B  138  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK ARG B  139  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK GLY B  140  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK SER B  141  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK HIS B  142  GB   15610269            CLONING ARTIFACT               
SEQADV 1ZLK MET B  143  GB   15610269            CLONING ARTIFACT               
SEQRES   1 C   43   DG  DG  DC  DC  DC  DG  DC  DG  DC  DT  DT  DT  DG          
SEQRES   2 C   43   DG  DG  DG  DA  DC  DT  DA  DA  DA  DG  DT  DC  DC          
SEQRES   3 C   43   DC  DT  DA  DA  DC  DC  DC  DT  DG  DG  DC  DC  DA          
SEQRES   4 C   43   DC  DG  DA  DT                                              
SEQRES   1 D   43   DC  DG  DT  DG  DG  DC  DC  DA  DG  DG  DG  DT  DT          
SEQRES   2 D   43   DA  DG  DG  DG  DA  DC  DT  DT  DT  DA  DG  DT  DC          
SEQRES   3 D   43   DC  DC  DC  DA  DA  DA  DG  DC  DG  DC  DG  DG  DG          
SEQRES   4 D   43   DC  DC  DA  DT                                              
SEQRES   1 A   95  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A   95  LEU VAL PRO ARG GLY SER HIS MET GLN ASP PRO LEU SER          
SEQRES   3 A   95  GLY LEU THR ASP GLN GLU ARG THR LEU LEU GLY LEU LEU          
SEQRES   4 A   95  SER GLU GLY LEU THR ASN LYS GLN ILE ALA ASP ARG MET          
SEQRES   5 A   95  PHE LEU ALA GLU LYS THR VAL LYS ASN TYR VAL SER ARG          
SEQRES   6 A   95  LEU LEU ALA LYS LEU GLY MET GLU ARG ARG THR GLN ALA          
SEQRES   7 A   95  ALA VAL PHE ALA THR GLU LEU LYS ARG SER ARG PRO PRO          
SEQRES   8 A   95  GLY ASP GLY PRO                                              
SEQRES   1 B   95  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B   95  LEU VAL PRO ARG GLY SER HIS MET GLN ASP PRO LEU SER          
SEQRES   3 B   95  GLY LEU THR ASP GLN GLU ARG THR LEU LEU GLY LEU LEU          
SEQRES   4 B   95  SER GLU GLY LEU THR ASN LYS GLN ILE ALA ASP ARG MET          
SEQRES   5 B   95  PHE LEU ALA GLU LYS THR VAL LYS ASN TYR VAL SER ARG          
SEQRES   6 B   95  LEU LEU ALA LYS LEU GLY MET GLU ARG ARG THR GLN ALA          
SEQRES   7 B   95  ALA VAL PHE ALA THR GLU LEU LYS ARG SER ARG PRO PRO          
SEQRES   8 B   95  GLY ASP GLY PRO                                              
HELIX    1   1 LEU A  160  GLY A  164  5                                   5    
HELIX    2   2 THR A  166  ARG A  173  1                                   8    
HELIX    3   3 ALA A  177  GLY A  193  1                                  17    
HELIX    4   4 ARG A  196  ARG A  209  1                                  14    
HELIX    5   5 ARG B  155  LEU B  160  1                                   6    
HELIX    6   6 LEU B  161  GLY B  164  5                                   4    
HELIX    7   7 THR B  166  ARG B  173  1                                   8    
HELIX    8   8 ALA B  177  GLY B  193  1                                  17    
HELIX    9   9 ARG B  196  ARG B  209  1                                  14    
CRYST1  142.397   58.791   82.933  90.00 125.50  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007023  0.000000  0.005009        0.00000                         
SCALE2      0.000000  0.017009  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014811        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system