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Database: PDB
Entry: 6AX8
LinkDB: 6AX8
Original site: 6AX8 
HEADER    LIGASE                                  06-SEP-17   6AX8              
TITLE     MYCOBACTERIUM TUBERCULOSIS METHIONYL-TRNA SYNTHETASE IN COMPLEX WITH  
TITLE    2 METHIONYL-ADENYLATE                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHIONINE-TRNA LIGASE;                                    
COMPND   3 CHAIN: A;                                                            
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 (STRAIN ATCC 25618 / 
SOURCE   3 H37RV);                                                              
SOURCE   4 ORGANISM_TAXID: 83332;                                               
SOURCE   5 STRAIN: ATCC 25618 / H37RV;                                          
SOURCE   6 GENE: METG, METS, RV1007C, MTCI237.24;                               
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SYNTHETASE, LIGASE, LIGASE-AMINOACYL ADENYLATE COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.BARROS-ALVAREZ,W.G.J.HOL                                            
REVDAT   4   11-DEC-19 6AX8    1       REMARK                                   
REVDAT   3   20-FEB-19 6AX8    1       REMARK                                   
REVDAT   2   31-OCT-18 6AX8    1       JRNL                                     
REVDAT   1   11-APR-18 6AX8    0                                                
JRNL        AUTH   X.BARROS-ALVAREZ,S.TURLEY,R.M.RANADE,J.R.GILLESPIE,          
JRNL        AUTH 2 N.A.DUSTER,C.L.M.J.VERLINDE,E.FAN,F.S.BUCKNER,W.G.J.HOL      
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE DRUG TARGET MYCOBACTERIUM       
JRNL        TITL 2 TUBERCULOSIS METHIONYL-TRNA SYNTHETASE IN COMPLEX WITH A     
JRNL        TITL 3 CATALYTIC INTERMEDIATE.                                      
JRNL        REF    ACTA CRYSTALLOGR F STRUCT     V.  74   245 2018              
JRNL        REF  2 BIOL COMMUN                                                  
JRNL        REFN                   ESSN 2053-230X                               
JRNL        PMID   29633973                                                     
JRNL        DOI    10.1107/S2053230X18003151                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 98.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 16441                          
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) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 948                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1205                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 62                           
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3980                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 38                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.17000                                             
REMARK   3    B22 (A**2) : -2.17000                                             
REMARK   3    B33 (A**2) : 7.05000                                              
REMARK   3    B12 (A**2) : -1.09000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 2.550         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.324         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.913                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4117 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3794 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5615 ; 1.290 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8660 ; 3.747 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   508 ; 5.633 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   198 ;35.394 ;22.727       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   605 ;15.680 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;15.607 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   617 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4724 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1026 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2035 ; 2.541 ; 5.907       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2036 ; 2.541 ; 5.908       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2543 ; 4.165 ; 8.862       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2543 ; 4.165 ; 8.863       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2082 ; 2.973 ; 6.166       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2083 ; 2.972 ; 6.167       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3073 ; 5.037 ; 9.150       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4611 ; 7.575 ;47.222       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4612 ; 7.574 ;47.232       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6AX8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229949.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-15                          
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               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN-COOLED DOUBLE      
REMARK 200                                   CRYSTAL SI(111)                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AIMLESS                            
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17391                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 98.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1-0.2 M AMMONIUM SULFATE, 30-34 %      
REMARK 280  PEG 8K, 0.1 M SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION,           
REMARK 280  SITTING DROP, TEMPERATURE 298K                                      
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       98.47900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       56.85688            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       13.05900            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       98.47900            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       56.85688            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       13.05900            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       98.47900            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       56.85688            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       13.05900            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      113.71375            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       26.11800            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      113.71375            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       26.11800            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      113.71375            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       26.11800            
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 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     TYR A   510                                                      
REMARK 465     GLN A   511                                                      
REMARK 465     PRO A   512                                                      
REMARK 465     PRO A   513                                                      
REMARK 465     GLN A   514                                                      
REMARK 465     PRO A   515                                                      
REMARK 465     PRO A   516                                                      
REMARK 465     GLU A   517                                                      
REMARK 465     GLY A   518                                                      
REMARK 465     LYS A   519                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET A   1    SD   CE                                             
REMARK 470     LYS A   2    CG   CD   CE   NZ                                   
REMARK 470     VAL A 141    CG1  CG2                                            
REMARK 470     GLU A 247    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 296    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 298    CG   CD   OE1  OE2                                  
REMARK 470     MET A 300    CG   SD   CE                                        
REMARK 470     LYS A 302    CG   CD   CE   NZ                                   
REMARK 470     VAL A 304    CG1  CG2                                            
REMARK 470     GLU A 315    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 435    CG   CD   CE   NZ                                   
REMARK 470     GLU A 437    CG   CD   OE1  OE2                                  
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 A  13       32.14    -87.71                                   
REMARK 500    ASN A  85       38.86     70.74                                   
REMARK 500    SER A  87       54.32    -93.48                                   
REMARK 500    ARG A 131      145.01   -171.32                                   
REMARK 500    HIS A 220       71.01   -155.43                                   
REMARK 500    ASP A 243       80.69    -68.11                                   
REMARK 500    ASP A 245       44.47   -107.36                                   
REMARK 500    ARG A 296       -8.54     91.66                                   
REMARK 500    SER A 301     -111.73     59.18                                   
REMARK 500    ASN A 353      -66.39   -102.33                                   
REMARK 500    LEU A 355      -64.53    -92.50                                   
REMARK 500    ALA A 406       58.88   -117.46                                   
REMARK 500    GLN A 429       69.33     30.94                                   
REMARK 500    PHE A 507       71.20   -119.34                                   
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 A 938        DISTANCE =  8.05 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ME8 A 801                 
DBREF  6AX8 A    1   519  UNP    P9WFU5   SYM_MYCTU        1    519             
SEQRES   1 A  519  MET LYS PRO TYR TYR VAL THR THR ALA ILE ALA TYR PRO          
SEQRES   2 A  519  ASN ALA ALA PRO HIS VAL GLY HIS ALA TYR GLU TYR ILE          
SEQRES   3 A  519  ALA THR ASP ALA ILE ALA ARG PHE LYS ARG LEU ASP ARG          
SEQRES   4 A  519  TYR ASP VAL ARG PHE LEU THR GLY THR ASP GLU HIS GLY          
SEQRES   5 A  519  LEU LYS VAL ALA GLN ALA ALA ALA ALA ALA GLY VAL PRO          
SEQRES   6 A  519  THR ALA ALA LEU ALA ARG ARG ASN SER ASP VAL PHE GLN          
SEQRES   7 A  519  ARG MET GLN GLU ALA LEU ASN ILE SER PHE ASP ARG PHE          
SEQRES   8 A  519  ILE ARG THR THR ASP ALA ASP HIS HIS GLU ALA SER LYS          
SEQRES   9 A  519  GLU LEU TRP ARG ARG MET SER ALA ALA GLY ASP ILE TYR          
SEQRES  10 A  519  LEU ASP ASN TYR SER GLY TRP TYR SER VAL ARG ASP GLU          
SEQRES  11 A  519  ARG PHE PHE VAL GLU SER GLU THR GLN LEU VAL ASP GLY          
SEQRES  12 A  519  THR ARG LEU THR VAL GLU THR GLY THR PRO VAL THR TRP          
SEQRES  13 A  519  THR GLU GLU GLN THR TYR PHE PHE ARG LEU SER ALA TYR          
SEQRES  14 A  519  THR ASP LYS LEU LEU ALA HIS TYR HIS ALA ASN PRO ASP          
SEQRES  15 A  519  PHE ILE ALA PRO GLU THR ARG ARG ASN GLU VAL ILE SER          
SEQRES  16 A  519  PHE VAL SER GLY GLY LEU ASP ASP LEU SER ILE SER ARG          
SEQRES  17 A  519  THR SER PHE ASP TRP GLY VAL GLN VAL PRO GLU HIS PRO          
SEQRES  18 A  519  ASP HIS VAL MET TYR VAL TRP VAL ASP ALA LEU THR ASN          
SEQRES  19 A  519  TYR LEU THR GLY ALA GLY PHE PRO ASP THR ASP SER GLU          
SEQRES  20 A  519  LEU PHE ARG ARG TYR TRP PRO ALA ASP LEU HIS MET ILE          
SEQRES  21 A  519  GLY LYS ASP ILE ILE ARG PHE HIS ALA VAL TYR TRP PRO          
SEQRES  22 A  519  ALA PHE LEU MET SER ALA GLY ILE GLU LEU PRO ARG ARG          
SEQRES  23 A  519  ILE PHE ALA HIS GLY PHE LEU HIS ASN ARG GLY GLU LYS          
SEQRES  24 A  519  MET SER LYS SER VAL GLY ASN ILE VAL ASP PRO VAL ALA          
SEQRES  25 A  519  LEU ALA GLU ALA LEU GLY VAL ASP GLN VAL ARG TYR PHE          
SEQRES  26 A  519  LEU LEU ARG GLU VAL PRO PHE GLY GLN ASP GLY SER TYR          
SEQRES  27 A  519  SER ASP GLU ALA ILE VAL THR ARG ILE ASN THR ASP LEU          
SEQRES  28 A  519  ALA ASN GLU LEU GLY ASN LEU ALA GLN ARG SER LEU SER          
SEQRES  29 A  519  MET VAL ALA LYS ASN LEU ASP GLY ARG VAL PRO ASN PRO          
SEQRES  30 A  519  GLY GLU PHE ALA ASP ALA ASP ALA ALA LEU LEU ALA THR          
SEQRES  31 A  519  ALA ASP GLY LEU LEU GLU ARG VAL ARG GLY HIS PHE ASP          
SEQRES  32 A  519  ALA GLN ALA MET HIS LEU ALA LEU GLU ALA ILE TRP LEU          
SEQRES  33 A  519  MET LEU GLY ASP ALA ASN LYS TYR PHE SER VAL GLN GLN          
SEQRES  34 A  519  PRO TRP VAL LEU ARG LYS SER GLU SER GLU ALA ASP GLN          
SEQRES  35 A  519  ALA ARG PHE ARG THR THR LEU TYR VAL THR CYS GLU VAL          
SEQRES  36 A  519  VAL ARG ILE ALA ALA LEU LEU ILE GLN PRO VAL MET PRO          
SEQRES  37 A  519  GLU SER ALA GLY LYS ILE LEU ASP LEU LEU GLY GLN ALA          
SEQRES  38 A  519  PRO ASN GLN ARG SER PHE ALA ALA VAL GLY VAL ARG LEU          
SEQRES  39 A  519  THR PRO GLY THR ALA LEU PRO PRO PRO THR GLY VAL PHE          
SEQRES  40 A  519  PRO ARG TYR GLN PRO PRO GLN PRO PRO GLU GLY LYS              
HET    ME8  A 801      31                                                       
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                                      
HETSYN     ME8 L-METHIONINE-AMP; METHIONYL-ADENYLATE                            
FORMUL   2  ME8    C15 H23 N6 O8 P S                                            
FORMUL   3  HOH   *38(H2 O)                                                     
HELIX    1 AA1 HIS A   18  ASP A   38  1                                  21    
HELIX    2 AA2 GLY A   52  GLY A   63  1                                  12    
HELIX    3 AA3 PRO A   65  LEU A   84  1                                  20    
HELIX    4 AA4 ASP A   96  ALA A  113  1                                  18    
HELIX    5 AA5 VAL A  134  SER A  136  5                                   3    
HELIX    6 AA6 LEU A  166  ALA A  168  5                                   3    
HELIX    7 AA7 TYR A  169  ASN A  180  1                                  12    
HELIX    8 AA8 PRO A  186  GLY A  199  1                                  14    
HELIX    9 AA9 TYR A  226  THR A  233  1                                   8    
HELIX   10 AB1 THR A  233  GLY A  238  1                                   6    
HELIX   11 AB2 SER A  246  TRP A  253  1                                   8    
HELIX   12 AB3 ILE A  264  VAL A  270  1                                   7    
HELIX   13 AB4 VAL A  270  ALA A  279  1                                  10    
HELIX   14 AB5 ASP A  309  GLY A  318  1                                  10    
HELIX   15 AB6 GLY A  318  VAL A  330  1                                  13    
HELIX   16 AB7 SER A  339  LEU A  351  1                                  13    
HELIX   17 AB8 LEU A  355  LEU A  370  1                                  16    
HELIX   18 AB9 ALA A  381  GLY A  393  1                                  13    
HELIX   19 AC1 GLY A  393  ALA A  404  1                                  12    
HELIX   20 AC2 ALA A  406  GLN A  429  1                                  24    
HELIX   21 AC3 GLN A  429  ARG A  434  1                                   6    
HELIX   22 AC4 SER A  438  GLN A  464  1                                  27    
HELIX   23 AC5 MET A  467  LEU A  478  1                                  12    
HELIX   24 AC6 ALA A  488  VAL A  492  5                                   5    
SHEET    1 AA1 6 ARG A  90  ARG A  93  0                                        
SHEET    2 AA1 6 ASP A  41  THR A  48  1  N  THR A  46   O  ILE A  92           
SHEET    3 AA1 6 PRO A   3  THR A   8  1  N  TYR A   4   O  ARG A  43           
SHEET    4 AA1 6 LEU A 257  GLY A 261  1  O  MET A 259   N  THR A   7           
SHEET    5 AA1 6 ILE A 287  HIS A 290  1  O  HIS A 290   N  ILE A 260           
SHEET    6 AA1 6 ILE A 184  ALA A 185  1  N  ALA A 185   O  ILE A 287           
SHEET    1 AA2 4 ARG A 131  PHE A 133  0                                        
SHEET    2 AA2 4 ILE A 116  SER A 126 -1  N  SER A 126   O  ARG A 131           
SHEET    3 AA2 4 THR A 155  PHE A 164 -1  O  GLU A 159   N  TYR A 121           
SHEET    4 AA2 4 LEU A 204  SER A 205 -1  O  LEU A 204   N  PHE A 164           
SHEET    1 AA3 2 THR A 138  LEU A 140  0                                        
SHEET    2 AA3 2 ARG A 145  THR A 147 -1  O  LEU A 146   N  GLN A 139           
SHEET    1 AA4 3 SER A 207  ARG A 208  0                                        
SHEET    2 AA4 3 HIS A 220  MET A 225 -1  O  VAL A 224   N  ARG A 208           
SHEET    3 AA4 3 GLN A 216  VAL A 217 -1  N  VAL A 217   O  HIS A 223           
SHEET    1 AA5 2 LEU A 293  HIS A 294  0                                        
SHEET    2 AA5 2 GLY A 336  SER A 337  1  O  GLY A 336   N  HIS A 294           
CISPEP   1 ALA A  185    PRO A  186          0        -3.45                     
CISPEP   2 PHE A  241    PRO A  242          0        12.07                     
CISPEP   3 TRP A  253    PRO A  254          0         4.86                     
SITE     1 AC1 18 ILE A  10  ALA A  11  TYR A  12  HIS A  18                    
SITE     2 AC1 18 GLY A  20  HIS A  21  GLU A  24  ASP A  49                    
SITE     3 AC1 18 TRP A 228  GLY A 261  ASP A 263  ILE A 264                    
SITE     4 AC1 18 HIS A 268  HIS A 290  GLY A 291  PHE A 292                    
SITE     5 AC1 18 LEU A 293  HOH A 901                                          
CRYST1  196.958  196.958   39.177  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      0.005077  0.002931  0.000000        0.00000                         
SCALE2      0.000000  0.005863  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025525        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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