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Database: PDB
Entry: 6NHZ
LinkDB: 6NHZ
Original site: 6NHZ 
HEADER    LIGASE                                  24-DEC-18   6NHZ              
TITLE     MYCOBACTERIAL DNA LIGASE D COMPLEXED WITH ATP AND MG                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT DNA LIGASE;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 6.5.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 GENE: ERS027656_00724;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 866768                                      
KEYWDS    DNA LIGASE, LIGASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SHUMAN,M.UNCIULEAC,Y.GOLDGUR                                        
REVDAT   3   10-APR-19 6NHZ    1       JRNL                                     
REVDAT   2   20-FEB-19 6NHZ    1       JRNL                                     
REVDAT   1   13-FEB-19 6NHZ    0                                                
JRNL        AUTH   M.C.UNCIULEAC,Y.GOLDGUR,S.SHUMAN                             
JRNL        TITL   STRUCTURES OF ATP-BOUND DNA LIGASE D IN A CLOSED DOMAIN      
JRNL        TITL 2 CONFORMATION REVEAL A NETWORK OF AMINO ACID AND METAL        
JRNL        TITL 3 CONTACTS TO THE ATP PHOSPHATES.                              
JRNL        REF    J. BIOL. CHEM.                V. 294  5094 2019              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   30718283                                                     
JRNL        DOI    10.1074/JBC.RA119.007445                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25742                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.770                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.4955 -  4.3297    0.96     1773   149  0.1806 0.1936        
REMARK   3     2  4.3297 -  3.4383    0.99     1795   152  0.1698 0.2174        
REMARK   3     3  3.4383 -  3.0042    0.99     1779   150  0.2021 0.2472        
REMARK   3     4  3.0042 -  2.7297    0.98     1764   148  0.2054 0.2376        
REMARK   3     5  2.7297 -  2.5342    0.93     1672   141  0.2212 0.2422        
REMARK   3     6  2.5342 -  2.3848    0.97     1705   144  0.2214 0.2741        
REMARK   3     7  2.3848 -  2.2655    0.96     1726   145  0.2169 0.2694        
REMARK   3     8  2.2655 -  2.1669    0.98     1740   146  0.2298 0.2703        
REMARK   3     9  2.1669 -  2.0835    0.98     1734   147  0.2236 0.2766        
REMARK   3    10  2.0835 -  2.0116    0.98     1742   146  0.2308 0.2874        
REMARK   3    11  2.0116 -  1.9487    0.95     1731   147  0.2338 0.2599        
REMARK   3    12  1.9487 -  1.8930    0.90     1560   130  0.2468 0.3076        
REMARK   3    13  1.8930 -  1.8432    0.85     1525   129  0.2862 0.3336        
REMARK   3    14  1.8432 -  1.7982    0.85     1496   126  0.3211 0.3714        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.630           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           2453                                  
REMARK   3   ANGLE     :  0.981           3330                                  
REMARK   3   CHIRALITY :  0.056            350                                  
REMARK   3   PLANARITY :  0.005            433                                  
REMARK   3   DIHEDRAL  :  8.209           1451                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6NHZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000238769.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-APR-17                          
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                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25765                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM MGCL2 0.1 M NH4F 20% PEG 3350,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
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       25.81500            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLU A   653                                                      
REMARK 465     GLY A   654                                                      
REMARK 465     GLY A   655                                                      
REMARK 465     ARG A   656                                                      
REMARK 465     SER A   657                                                      
REMARK 465     SER A   658                                                      
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 712    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1055     O    HOH A  1105              1.82            
REMARK 500   O    HOH A  1029     O    HOH A  1117              1.98            
REMARK 500   O    GLY A   680     O    HOH A   901              1.99            
REMARK 500   O    HOH A  1015     O    HOH A  1103              2.00            
REMARK 500   NE   ARG A   748     O    HOH A   902              2.05            
REMARK 500   OD1  ASP A   483     O    HOH A   903              2.08            
REMARK 500   O    HOH A   983     O    HOH A  1094              2.10            
REMARK 500   NH2  ARG A   678     O    HOH A   904              2.10            
REMARK 500   O    HOH A  1102     O    HOH A  1112              2.14            
REMARK 500   OE1  GLU A   759     O    HOH A   905              2.15            
REMARK 500   O    HOH A   989     O    HOH A  1047              2.17            
REMARK 500   NH2  ARG A   497     O    HOH A   906              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   933     O    HOH A   940     2555     2.16            
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    GLU A 685     -106.16     48.70                                   
REMARK 500    HIS A 699      132.97    -39.94                                   
REMARK 500    GLN A 741       60.16     39.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1134        DISTANCE =  6.50 ANGSTROMS                       
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                              MG A 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 801   O3G                                                    
REMARK 620 2 ATP A 801   O2B  65.7                                              
REMARK 620 3 HOH A1096   O   103.4 169.0                                        
REMARK 620 4 HOH A1023   O   117.6  67.1 119.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 803  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 801   O2A                                                    
REMARK 620 2 HOH A1023   O   113.9                                              
REMARK 620 3 HOH A 915   O    98.0 100.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 803                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6NHX   RELATED DB: PDB                                   
DBREF1 6NHZ A  452   759  UNP                  A0A0T9BTX3_MYCTX                 
DBREF2 6NHZ A     A0A0T9BTX3                          1         308             
SEQADV 6NHZ SER A  451  UNP  A0A0T9BTX           EXPRESSION TAG                 
SEQADV 6NHZ MET A  481  UNP  A0A0T9BTX LYS    30 ENGINEERED MUTATION            
SEQRES   1 A  309  SER MET PHE GLU PHE ASP ASN LEU ALA PRO MET LEU ALA          
SEQRES   2 A  309  THR HIS GLY THR VAL ALA GLY LEU LYS ALA SER GLN TRP          
SEQRES   3 A  309  ALA PHE GLU GLY MET TRP ASP GLY TYR ARG LEU LEU VAL          
SEQRES   4 A  309  GLU ALA ASP HIS GLY ALA VAL ARG LEU ARG SER ARG SER          
SEQRES   5 A  309  GLY ARG ASP VAL THR ALA GLU TYR PRO GLN LEU ARG ALA          
SEQRES   6 A  309  LEU ALA GLU ASP LEU ALA ASP HIS HIS VAL VAL LEU ASP          
SEQRES   7 A  309  GLY GLU ALA VAL VAL LEU ASP SER SER GLY VAL PRO SER          
SEQRES   8 A  309  PHE SER GLN MET GLN ASN ARG GLY ARG ASP THR ARG VAL          
SEQRES   9 A  309  GLU PHE TRP ALA PHE ASP LEU LEU TYR LEU ASP GLY ARG          
SEQRES  10 A  309  ALA LEU LEU GLY THR ARG TYR GLN ASP ARG ARG LYS LEU          
SEQRES  11 A  309  LEU GLU THR LEU ALA ASN ALA THR SER LEU THR VAL PRO          
SEQRES  12 A  309  GLU LEU LEU PRO GLY ASP GLY ALA GLN ALA PHE ALA CYS          
SEQRES  13 A  309  SER ARG LYS HIS GLY TRP GLU GLY VAL ILE ALA LYS ARG          
SEQRES  14 A  309  ARG ASP SER ARG TYR GLN PRO GLY ARG ARG CYS ALA SER          
SEQRES  15 A  309  TRP VAL LYS ASP LYS HIS TRP ASN THR GLN GLU VAL VAL          
SEQRES  16 A  309  ILE GLY GLY TRP ARG ALA GLY GLU GLY GLY ARG SER SER          
SEQRES  17 A  309  GLY VAL GLY SER LEU LEU MET GLY ILE PRO GLY PRO GLY          
SEQRES  18 A  309  GLY LEU GLN PHE ALA GLY ARG VAL GLY THR GLY LEU SER          
SEQRES  19 A  309  GLU ARG GLU LEU ALA ASN LEU LYS GLU MET LEU ALA PRO          
SEQRES  20 A  309  LEU HIS THR ASP GLU SER PRO PHE ASP VAL PRO LEU PRO          
SEQRES  21 A  309  ALA ARG ASP ALA LYS GLY ILE THR TYR VAL LYS PRO ALA          
SEQRES  22 A  309  LEU VAL ALA GLU VAL ARG TYR SER GLU TRP THR PRO GLU          
SEQRES  23 A  309  GLY ARG LEU ARG GLN SER SER TRP ARG GLY LEU ARG PRO          
SEQRES  24 A  309  ASP LYS LYS PRO SER GLU VAL VAL ARG GLU                      
HET    ATP  A 801      31                                                       
HET     MG  A 802       1                                                       
HET     MG  A 803       1                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  ATP    C10 H16 N5 O13 P3                                            
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  HOH   *234(H2 O)                                                    
HELIX    1 AA1 GLU A  454  LEU A  458  5                                   5    
HELIX    2 AA2 VAL A  506  ARG A  514  5                                   9    
HELIX    3 AA3 SER A  541  ASN A  547  1                                   7    
HELIX    4 AA4 ARG A  573  ASN A  586  1                                  14    
HELIX    5 AA5 ASP A  599  HIS A  610  1                                  12    
HELIX    6 AA6 GLU A  685  ALA A  696  1                                  12    
HELIX    7 AA7 PRO A  710  LYS A  715  1                                   6    
HELIX    8 AA8 LYS A  752  VAL A  756  5                                   5    
SHEET    1 AA1 4 LEU A 462  HIS A 465  0                                        
SHEET    2 AA1 4 ARG A 629  LYS A 637  1  O  TRP A 633   N  THR A 464           
SHEET    3 AA1 4 GLY A 614  ARG A 619 -1  N  ALA A 617   O  VAL A 634           
SHEET    4 AA1 4 TRP A 476  GLY A 480 -1  N  ALA A 477   O  LYS A 618           
SHEET    1 AA2 5 ALA A 495  ARG A 499  0                                        
SHEET    2 AA2 5 TYR A 485  ASP A 492 -1  N  GLU A 490   O  ARG A 497           
SHEET    3 AA2 5 HIS A 524  VAL A 532 -1  O  LEU A 527   N  VAL A 489           
SHEET    4 AA2 5 GLU A 555  LEU A 564 -1  O  GLU A 555   N  VAL A 532           
SHEET    5 AA2 5 ARG A 567  ALA A 568 -1  O  ARG A 567   N  LEU A 564           
SHEET    1 AA3 5 GLY A 672  VAL A 679  0                                        
SHEET    2 AA3 5 SER A 662  GLY A 669 -1  N  ILE A 667   O  GLN A 674           
SHEET    3 AA3 5 ASN A 640  ARG A 650 -1  N  GLY A 647   O  LEU A 664           
SHEET    4 AA3 5 THR A 718  VAL A 720 -1  O  VAL A 720   N  GLY A 647           
SHEET    5 AA3 5 HIS A 699  THR A 700 -1  N  THR A 700   O  TYR A 719           
SHEET    1 AA4 5 GLY A 672  VAL A 679  0                                        
SHEET    2 AA4 5 SER A 662  GLY A 669 -1  N  ILE A 667   O  GLN A 674           
SHEET    3 AA4 5 ASN A 640  ARG A 650 -1  N  GLY A 647   O  LEU A 664           
SHEET    4 AA4 5 VAL A 725  TYR A 730 -1  O  VAL A 728   N  GLN A 642           
SHEET    5 AA4 5 SER A 743  LEU A 747 -1  O  GLY A 746   N  GLU A 727           
LINK         O3G ATP A 801                MG    MG A 802     1555   1555  2.79  
LINK         O2B ATP A 801                MG    MG A 802     1555   1555  2.61  
LINK         O2A ATP A 801                MG    MG A 803     1555   1555  2.48  
LINK        MG    MG A 802                 O   HOH A1096     1555   1555  2.72  
LINK        MG    MG A 802                 O   HOH A1023     1555   1555  2.53  
LINK        MG    MG A 803                 O   HOH A1023     1555   1555  2.74  
LINK        MG    MG A 803                 O   HOH A 915     1555   1555  2.98  
SITE     1 AC1 23 HIS A 465  GLU A 479  GLY A 480  MET A 481                    
SITE     2 AC1 23 TRP A 482  ARG A 486  ARG A 501  GLU A 530                    
SITE     3 AC1 23 PHE A 559  ILE A 616  LYS A 618  ARG A 629                    
SITE     4 AC1 23 TRP A 633  LYS A 635  LYS A 637   MG A 802                    
SITE     5 AC1 23  MG A 803  HOH A 915  HOH A 968  HOH A 971                    
SITE     6 AC1 23 HOH A1017  HOH A1023  HOH A1067                               
SITE     1 AC2  4 ARG A 501  ATP A 801  HOH A1023  HOH A1096                    
SITE     1 AC3  5 GLU A 613  ARG A 745  ATP A 801  HOH A 915                    
SITE     2 AC3  5 HOH A1023                                                     
CRYST1   39.618   51.630   72.874  90.00  99.57  90.00 P 1 21 1      2          
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      0.025241  0.000000  0.004255        0.00000                         
SCALE2      0.000000  0.019369  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013916        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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