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Database: PDB
Entry: 5XET
LinkDB: 5XET
Original site: 5XET 
HEADER    LIGASE                                  06-APR-17   5XET              
TITLE     CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS METHIONYL-TRNA        
TITLE    2 SYNTHETASE BOUND BY METHIONYL-ADENYLATE (MET-AMP)                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHIONINE--TRNA LIGASE;                                   
COMPND   3 CHAIN: C;                                                            
COMPND   4 SYNONYM: METHIONYL-TRNA SYNTHETASE,METRS;                            
COMPND   5 EC: 6.1.1.10;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RA;               
SOURCE   3 ORGANISM_TAXID: 419947;                                              
SOURCE   4 STRAIN: ATCC 25177 / H37RA;                                          
SOURCE   5 GENE: METG, MRA_1016;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD(DE3)PLYSS AG                     
KEYWDS    SYNTHETASE, AMINOACYL-TRNA SYNTHETASE, COMPLEX, ATP, LIGASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.WANG,B.QIN,J.A.WOJDYLA,M.WANG,X.GAO,S.CUI                           
REVDAT   2   01-AUG-18 5XET    1       JRNL                                     
REVDAT   1   11-JUL-18 5XET    0                                                
JRNL        AUTH   W.WANG,B.QIN,J.A.WOJDYLA,M.WANG,X.GAO,S.CUI                  
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF FREE-STATE AND                
JRNL        TITL 2 PRODUCT-STATEMYCOBACTERIUM TUBERCULOSISMETHIONYL-TRNA        
JRNL        TITL 3 SYNTHETASE REVEALS AN INDUCED-FIT LIGAND-RECOGNITION         
JRNL        TITL 4 MECHANISM.                                                   
JRNL        REF    IUCRJ                         V.   5   478 2018              
JRNL        REFN                   ESSN 2052-2525                               
JRNL        PMID   30002848                                                     
JRNL        DOI    10.1107/S2052252518008217                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 2.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.42                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 22866                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1164                            
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 37.4263 -  4.7572    0.99     2683   160  0.1694 0.1996        
REMARK   3     2  4.7572 -  3.7771    0.99     2710   136  0.1561 0.1853        
REMARK   3     3  3.7771 -  3.3000    0.99     2709   129  0.1940 0.3045        
REMARK   3     4  3.3000 -  2.9984    1.00     2701   149  0.2228 0.2775        
REMARK   3     5  2.9984 -  2.7835    1.00     2716   151  0.2355 0.2990        
REMARK   3     6  2.7835 -  2.6195    1.00     2698   158  0.2460 0.2699        
REMARK   3     7  2.6195 -  2.4883    1.00     2776   121  0.2630 0.3433        
REMARK   3     8  2.4883 -  2.3800    1.00     2709   160  0.2738 0.3139        
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)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.080           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.55                          
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      :  0.008           4134                                  
REMARK   3   ANGLE     :  0.804           5631                                  
REMARK   3   CHIRALITY :  0.044            616                                  
REMARK   3   PLANARITY :  0.005            733                                  
REMARK   3   DIHEDRAL  : 13.456           2422                                  
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: THE STRUCTURE FACTOR FILE CONTAINS        
REMARK   3  FRIEDEL PAIRS IN F_PLUS/MINUS AND I_PLUS/MINUS COLUMNS              
REMARK   4                                                                      
REMARK   4 5XET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300002203.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL18U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.977760                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49191                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.380                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.420                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.15600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.7700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.13                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.610                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 2X1L                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULFATE MONOHYDRATE, 19%    
REMARK 280  PEG 3350, BIS TRIS, PH 6.9, EVAPORATION, TEMPERATURE 293K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       99.00850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       57.16258            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       13.05367            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       99.00850            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       57.16258            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       13.05367            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       99.00850            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       57.16258            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       13.05367            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      114.32517            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       26.10733            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      114.32517            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       26.10733            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      114.32517            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       26.10733            
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: 460 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 20730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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     MET C    -7                                                      
REMARK 465     GLY C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C   297                                                      
REMARK 465     GLU C   298                                                      
REMARK 465     ARG C   509                                                      
REMARK 465     TYR C   510                                                      
REMARK 465     GLN C   511                                                      
REMARK 465     PRO C   512                                                      
REMARK 465     PRO C   513                                                      
REMARK 465     GLN C   514                                                      
REMARK 465     PRO C   515                                                      
REMARK 465     PRO C   516                                                      
REMARK 465     GLU C   517                                                      
REMARK 465     GLY C   518                                                      
REMARK 465     LYS C   519                                                      
REMARK 465     ARG C   520                                                      
REMARK 465     SER C   521                                                      
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   H    ALA C   385     O    HOH C   702              1.39            
REMARK 500  HH21  ARG C   109     O    HOH C   707              1.55            
REMARK 500   HE   ARG C   108     O    HOH C   725              1.58            
REMARK 500   OE1  GLU C    50     HG1  THR C    95              1.60            
REMARK 500   O    LYS C     2     H    ASP C    41              1.60            
REMARK 500   O    ARG C   251     O    HOH C   701              1.81            
REMARK 500   N    ALA C   385     O    HOH C   702              1.93            
REMARK 500   O    ALA C   381     O    HOH C   702              1.93            
REMARK 500   O    PRO C   501     O    HOH C   703              1.95            
REMARK 500   O    HOH C   751     O    HOH C   855              1.95            
REMARK 500   OD2  ASP C   309     O    HOH C   704              1.96            
REMARK 500   O    LEU C   500     O    HOH C   705              1.98            
REMARK 500   O    LEU C   363     O    HOH C   706              2.01            
REMARK 500   O    HOH C   841     O    HOH C   865              2.02            
REMARK 500   NH2  ARG C   109     O    HOH C   707              2.03            
REMARK 500   N    SER C   301     O    HOH C   708              2.06            
REMARK 500   OD1  ASP C   222     O    HOH C   709              2.12            
REMARK 500   O    PRO C   242     O    HOH C   710              2.14            
REMARK 500   O    HOH C   779     O    HOH C   858              2.15            
REMARK 500   O    HOH C   748     O    HOH C   806              2.17            
REMARK 500   NH1  ARG C   131     O    HOH C   711              2.18            
REMARK 500   O    ASP C   142     O    HOH C   712              2.18            
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 C   832     O    HOH C   847     1556     2.03            
REMARK 500   O    HOH C   845     O    HOH C   852     1554     2.06            
REMARK 500   O    HOH C   843     O    HOH C   872     2555     2.09            
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    PRO C  13       45.41    -80.29                                   
REMARK 500    SER C  87       44.62    -83.72                                   
REMARK 500    GLU C 130       39.97     74.04                                   
REMARK 500    GLU C 137       38.19    -81.71                                   
REMARK 500    HIS C 220       68.48   -155.00                                   
REMARK 500    TYR C 226      126.83    -35.01                                   
REMARK 500    VAL C 270      -58.10   -121.21                                   
REMARK 500    LEU C 317       -5.95   -140.87                                   
REMARK 500    ASN C 353      -69.16    -94.16                                   
REMARK 500    ALA C 406       58.95   -108.79                                   
REMARK 500    GLN C 429       57.89     38.98                                   
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 C 880        DISTANCE =  6.44 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 C 605  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C  23   OH                                                     
REMARK 620 2 LEU C 326   O   109.0                                              
REMARK 620 3 VAL C 330   O   112.8 103.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 606  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 751   O                                                      
REMARK 620 2 HOH C 855   O    54.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ME8 C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 607                  
DBREF  5XET C    1   519  UNP    A5U150   A5U150_MYCTA     1    519             
SEQADV 5XET MET C   -7  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XET GLY C   -6  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XET HIS C   -5  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XET HIS C   -4  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XET HIS C   -3  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XET HIS C   -2  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XET HIS C   -1  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XET HIS C    0  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XET ARG C  520  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XET SER C  521  UNP  A5U150              EXPRESSION TAG                 
SEQRES   1 C  529  MET GLY HIS HIS HIS HIS HIS HIS MET LYS PRO TYR TYR          
SEQRES   2 C  529  VAL THR THR ALA ILE ALA TYR PRO ASN ALA ALA PRO HIS          
SEQRES   3 C  529  VAL GLY HIS ALA TYR GLU TYR ILE ALA THR ASP ALA ILE          
SEQRES   4 C  529  ALA ARG PHE LYS ARG LEU ASP ARG TYR ASP VAL ARG PHE          
SEQRES   5 C  529  LEU THR GLY THR ASP GLU HIS GLY LEU LYS VAL ALA GLN          
SEQRES   6 C  529  ALA ALA ALA ALA ALA GLY VAL PRO THR ALA ALA LEU ALA          
SEQRES   7 C  529  ARG ARG ASN SER ASP VAL PHE GLN ARG MET GLN GLU ALA          
SEQRES   8 C  529  LEU ASN ILE SER PHE ASP ARG PHE ILE ARG THR THR ASP          
SEQRES   9 C  529  ALA ASP HIS HIS GLU ALA SER LYS GLU LEU TRP ARG ARG          
SEQRES  10 C  529  MET SER ALA ALA GLY ASP ILE TYR LEU ASP ASN TYR SER          
SEQRES  11 C  529  GLY TRP TYR SER VAL ARG ASP GLU ARG PHE PHE VAL GLU          
SEQRES  12 C  529  SER GLU THR GLN LEU VAL ASP GLY THR ARG LEU THR VAL          
SEQRES  13 C  529  GLU THR GLY THR PRO VAL THR TRP THR GLU GLU GLN THR          
SEQRES  14 C  529  TYR PHE PHE ARG LEU SER ALA TYR THR ASP LYS LEU LEU          
SEQRES  15 C  529  ALA HIS TYR HIS ALA ASN PRO ASP PHE ILE ALA PRO GLU          
SEQRES  16 C  529  THR ARG ARG ASN GLU VAL ILE SER PHE VAL SER GLY GLY          
SEQRES  17 C  529  LEU ASP ASP LEU SER ILE SER ARG THR SER PHE ASP TRP          
SEQRES  18 C  529  GLY VAL GLN VAL PRO GLU HIS PRO ASP HIS VAL MET TYR          
SEQRES  19 C  529  VAL TRP VAL ASP ALA LEU THR ASN TYR LEU THR GLY ALA          
SEQRES  20 C  529  GLY PHE PRO ASP THR ASP SER GLU LEU PHE ARG ARG TYR          
SEQRES  21 C  529  TRP PRO ALA ASP LEU HIS MET ILE GLY LYS ASP ILE ILE          
SEQRES  22 C  529  ARG PHE HIS ALA VAL TYR TRP PRO ALA PHE LEU MET SER          
SEQRES  23 C  529  ALA GLY ILE GLU LEU PRO ARG ARG ILE PHE ALA HIS GLY          
SEQRES  24 C  529  PHE LEU HIS ASN ARG GLY GLU LYS MET SER LYS SER VAL          
SEQRES  25 C  529  GLY ASN ILE VAL ASP PRO VAL ALA LEU ALA GLU ALA LEU          
SEQRES  26 C  529  GLY VAL ASP GLN VAL ARG TYR PHE LEU LEU ARG GLU VAL          
SEQRES  27 C  529  PRO PHE GLY GLN ASP GLY SER TYR SER ASP GLU ALA ILE          
SEQRES  28 C  529  VAL THR ARG ILE ASN THR ASP LEU ALA ASN GLU LEU GLY          
SEQRES  29 C  529  ASN LEU ALA GLN ARG SER LEU SER MET VAL ALA LYS ASN          
SEQRES  30 C  529  LEU ASP GLY ARG VAL PRO ASN PRO GLY GLU PHE ALA ASP          
SEQRES  31 C  529  ALA ASP ALA ALA LEU LEU ALA THR ALA ASP GLY LEU LEU          
SEQRES  32 C  529  GLU ARG VAL ARG GLY HIS PHE ASP ALA GLN ALA MET HIS          
SEQRES  33 C  529  LEU ALA LEU GLU ALA ILE TRP LEU MET LEU GLY ASP ALA          
SEQRES  34 C  529  ASN LYS TYR PHE SER VAL GLN GLN PRO TRP VAL LEU ARG          
SEQRES  35 C  529  LYS SER GLU SER GLU ALA ASP GLN ALA ARG PHE ARG THR          
SEQRES  36 C  529  THR LEU TYR VAL THR CYS GLU VAL VAL ARG ILE ALA ALA          
SEQRES  37 C  529  LEU LEU ILE GLN PRO VAL MET PRO GLU SER ALA GLY LYS          
SEQRES  38 C  529  ILE LEU ASP LEU LEU GLY GLN ALA PRO ASN GLN ARG SER          
SEQRES  39 C  529  PHE ALA ALA VAL GLY VAL ARG LEU THR PRO GLY THR ALA          
SEQRES  40 C  529  LEU PRO PRO PRO THR GLY VAL PHE PRO ARG TYR GLN PRO          
SEQRES  41 C  529  PRO GLN PRO PRO GLU GLY LYS ARG SER                          
HET    ME8  C 601      53                                                       
HET    EDO  C 602      10                                                       
HET     MG  C 603       1                                                       
HET     MG  C 604       1                                                       
HET     MG  C 605       1                                                       
HET     MG  C 606       1                                                       
HET     MG  C 607       1                                                       
HETNAM     ME8 [[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-             
HETNAM   2 ME8  OXOLAN-2-YL]METHOXY-HYDROXY-PHOSPHORYL] (2S)-2-AZANYL-          
HETNAM   3 ME8  4-METHYLSULFANYL-BUTANOATE                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     ME8 L-METHIONINE-AMP; METHIONYL-ADENYLATE                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  ME8    C15 H23 N6 O8 P S                                            
FORMUL   3  EDO    C2 H6 O2                                                     
FORMUL   4   MG    5(MG 2+)                                                     
FORMUL   9  HOH   *180(H2 O)                                                    
HELIX    1 AA1 HIS C   18  ASP C   38  1                                  21    
HELIX    2 AA2 GLY C   52  ALA C   60  1                                   9    
HELIX    3 AA3 PRO C   65  LEU C   84  1                                  20    
HELIX    4 AA4 ASP C   96  ALA C  113  1                                  18    
HELIX    5 AA5 VAL C  134  SER C  136  5                                   3    
HELIX    6 AA6 LEU C  166  ALA C  168  5                                   3    
HELIX    7 AA7 TYR C  169  ASN C  180  1                                  12    
HELIX    8 AA8 PRO C  186  GLY C  199  1                                  14    
HELIX    9 AA9 TYR C  226  THR C  233  1                                   8    
HELIX   10 AB1 THR C  233  GLY C  238  1                                   6    
HELIX   11 AB2 SER C  246  TRP C  253  1                                   8    
HELIX   12 AB3 ILE C  264  VAL C  270  1                                   7    
HELIX   13 AB4 VAL C  270  ALA C  279  1                                  10    
HELIX   14 AB5 ASP C  309  GLY C  318  1                                  10    
HELIX   15 AB6 GLY C  318  VAL C  330  1                                  13    
HELIX   16 AB7 SER C  339  LEU C  351  1                                  13    
HELIX   17 AB8 LEU C  355  LEU C  370  1                                  16    
HELIX   18 AB9 ALA C  381  GLY C  393  1                                  13    
HELIX   19 AC1 GLY C  393  ALA C  404  1                                  12    
HELIX   20 AC2 ALA C  406  GLN C  429  1                                  24    
HELIX   21 AC3 GLN C  429  ARG C  434  1                                   6    
HELIX   22 AC4 SER C  438  GLN C  464  1                                  27    
HELIX   23 AC5 MET C  467  LEU C  478  1                                  12    
HELIX   24 AC6 ALA C  481  ARG C  485  5                                   5    
HELIX   25 AC7 SER C  486  VAL C  492  5                                   7    
SHEET    1 AA1 6 ARG C  90  ARG C  93  0                                        
SHEET    2 AA1 6 ASP C  41  THR C  48  1  N  THR C  46   O  ILE C  92           
SHEET    3 AA1 6 PRO C   3  THR C   8  1  N  TYR C   4   O  ASP C  41           
SHEET    4 AA1 6 LEU C 257  GLY C 261  1  O  MET C 259   N  THR C   7           
SHEET    5 AA1 6 ILE C 287  HIS C 290  1  O  HIS C 290   N  ILE C 260           
SHEET    6 AA1 6 ILE C 184  ALA C 185  1  N  ALA C 185   O  ALA C 289           
SHEET    1 AA2 4 ARG C 131  PHE C 133  0                                        
SHEET    2 AA2 4 ILE C 116  SER C 126 -1  N  TRP C 124   O  PHE C 133           
SHEET    3 AA2 4 THR C 155  PHE C 164 -1  O  GLU C 159   N  TYR C 121           
SHEET    4 AA2 4 LEU C 204  SER C 205 -1  O  LEU C 204   N  PHE C 164           
SHEET    1 AA3 2 THR C 138  VAL C 141  0                                        
SHEET    2 AA3 2 THR C 144  THR C 147 -1  O  THR C 144   N  VAL C 141           
SHEET    1 AA4 2 SER C 207  ARG C 208  0                                        
SHEET    2 AA4 2 VAL C 224  MET C 225 -1  O  VAL C 224   N  ARG C 208           
SHEET    1 AA5 2 LEU C 293  ASN C 295  0                                        
SHEET    2 AA5 2 GLY C 336  TYR C 338  1  O  TYR C 338   N  HIS C 294           
LINK         OH  TYR C  23                MG    MG C 605     1555   1555  2.39  
LINK         OG  SER C 301                MG    MG C 603     1555   1555  1.78  
LINK         O   LEU C 326                MG    MG C 605     1555   1555  2.94  
LINK         O   VAL C 330                MG    MG C 605     1555   1555  2.64  
LINK        MG    MG C 604                 O   HOH C 788     1555   1555  1.88  
LINK        MG    MG C 606                 O   HOH C 751     1555   1555  2.14  
LINK        MG    MG C 606                 O   HOH C 855     1555   1555  2.13  
CISPEP   1 ALA C  185    PRO C  186          0         3.06                     
CISPEP   2 PHE C  241    PRO C  242          0         8.10                     
CISPEP   3 TRP C  253    PRO C  254          0         6.28                     
SITE     1 AC1 22 ALA C   9  ILE C  10  ALA C  11  TYR C  12                    
SITE     2 AC1 22 HIS C  18  GLY C  20  HIS C  21  GLU C  24                    
SITE     3 AC1 22 ASP C  49  TRP C 228  ALA C 231  TYR C 235                    
SITE     4 AC1 22 GLY C 261  ASP C 263  ILE C 264  HIS C 290                    
SITE     5 AC1 22 GLY C 291  PHE C 292  LEU C 293  HOH C 721                    
SITE     6 AC1 22 HOH C 762  HOH C 811                                          
SITE     1 AC2  4 ARG C  33  ASN C  85  HOH C 789  HOH C 816                    
SITE     1 AC3  3 VAL C  19  SER C 301  VAL C 308                               
SITE     1 AC4  2 ARG C 397  HOH C 788                                          
SITE     1 AC5  4 TYR C  23  LEU C 326  VAL C 330  PHE C 332                    
SITE     1 AC6  3 ARG C 328  HOH C 751  HOH C 855                               
SITE     1 AC7  1 ARG C 446                                                     
CRYST1  198.017  198.017   39.161  90.00  90.00 120.00 H 3           9          
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      0.005050  0.002916  0.000000        0.00000                         
SCALE2      0.000000  0.005831  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025536        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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