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Database: PDB
Entry: 1F4L
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Original site: 1F4L 
HEADER    HYDROLASE                               08-JUN-00   1F4L              
TITLE     CRYSTAL STRUCTURE OF THE E.COLI METHIONYL-TRNA SYNTHETASE COMPLEXED   
TITLE    2 WITH METHIONINE                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHIONYL-TRNA SYNTHETASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-551;                                            
COMPND   5 EC: 6.1.1.10;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: SYNTHETIC GENE;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ROSSMANN FOLD, ZINC DOMAIN, AMINO ACID, TRNA, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.SERRE,G.VERDON,T.CHONOWSKI,N.HERVOUET,C.ZELWER                      
REVDAT   6   04-OCT-17 1F4L    1       REMARK                                   
REVDAT   5   24-AUG-11 1F4L    1       KEYWDS VERSN                             
REVDAT   4   24-FEB-09 1F4L    1       VERSN                                    
REVDAT   3   07-JAN-03 1F4L    1       REMARK                                   
REVDAT   2   11-APR-01 1F4L    1       COMPND                                   
REVDAT   1   21-MAR-01 1F4L    0                                                
JRNL        AUTH   L.SERRE,G.VERDON,T.CHOINOWSKI,N.HERVOUET,J.L.RISLER,C.ZELWER 
JRNL        TITL   HOW METHIONYL-TRNA SYNTHETASE CREATES ITS AMINO ACID         
JRNL        TITL 2 RECOGNITION POCKET UPON L-METHIONINE BINDING.                
JRNL        REF    J.MOL.BIOL.                   V. 306   863 2001              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11243794                                                     
JRNL        DOI    10.1006/JMBI.2001.4408                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 40632                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4532                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4384                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 437                                     
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.010 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.028 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1F4L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JUN-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000011235.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : AUG-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45164                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4000                            
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: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM CITRATE, METHYL-PENTANEDIOL,    
REMARK 280  L-METHIONINE, MERCAPTOETHANOL, PHOSPHATE, PH 7.0, VAPOR             
REMARK 280  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       22.58000            
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 300 REMARK: THE BIOLOCICAL ASSEMBLY IS A DIMER FORMED WITH THE FULL      
REMARK 300 LENGTH MONOMER                                                       
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: DIMERIC                           
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 350   BIOMT1   2 -1.000000  0.000000  0.000000      -26.54228            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       22.58000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       82.12748            
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 A     0                                                      
REMARK 465     THR A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     GLU A   549                                                      
REMARK 465     VAL A   550                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  41   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A  41   NE  -  CZ  -  NH2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    TYR A  91   CB  -  CG  -  CD1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG A 103   CD  -  NE  -  CZ  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG A 139   CD  -  NE  -  CZ  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ARG A 206   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A 233   NE  -  CZ  -  NH2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ALA A 235   CA  -  C   -  O   ANGL. DEV. = -21.0 DEGREES          
REMARK 500    PRO A 236   CA  -  N   -  CD  ANGL. DEV. = -11.8 DEGREES          
REMARK 500    PRO A 236   N   -  CA  -  CB  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    VAL A 252   CB  -  CA  -  C   ANGL. DEV. = -15.8 DEGREES          
REMARK 500    LYS A 282   CA  -  CB  -  CG  ANGL. DEV. =  13.4 DEGREES          
REMARK 500    GLU A 375   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    GLN A 379   CB  -  CG  -  CD  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    ARG A 403   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A 435   CD  -  NE  -  CZ  ANGL. DEV. =  31.9 DEGREES          
REMARK 500    ARG A 435   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG A 435   NE  -  CZ  -  NH2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A 453   CD  -  NE  -  CZ  ANGL. DEV. =   8.4 DEGREES          
REMARK 500    GLU A 467   CB  -  CG  -  CD  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    VAL A 524   N   -  CA  -  CB  ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ARG A 533   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    LYS A 547   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  90       48.45    -81.20                                   
REMARK 500    HIS A  95     -143.62   -117.16                                   
REMARK 500    LEU A 303      -65.32   -120.90                                   
REMARK 500    GLU A 467      109.21    -13.52                                   
REMARK 500    LYS A 528      -91.05    -55.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A  235     PRO A  236                   55.87                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ALA A 235         30.69                                           
REMARK 500    GLU A 467        -10.96                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 145   SG                                                     
REMARK 620 2 CYS A 158   SG  105.5                                              
REMARK 620 3 CYS A 161   SG  109.5 114.2                                        
REMARK 620 4 CYS A 148   SG  109.8 106.3 111.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MET A 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QQT   RELATED DB: PDB                                   
REMARK 900 1QQT CONTAINS SAME PROTEIN.                                          
REMARK 900 RELATED ID: 1A8H   RELATED DB: PDB                                   
REMARK 900 1A8H CONTAINS METHIONYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS.   
DBREF  1F4L A    0   550  UNP    P00959   SYM_ECOLI        1    551             
SEQRES   1 A  551  MET THR GLN VAL ALA LYS LYS ILE LEU VAL THR CYS ALA          
SEQRES   2 A  551  LEU PRO TYR ALA ASN GLY SER ILE HIS LEU GLY HIS MET          
SEQRES   3 A  551  LEU GLU HIS ILE GLN ALA ASP VAL TRP VAL ARG TYR GLN          
SEQRES   4 A  551  ARG MET ARG GLY HIS GLU VAL ASN PHE ILE CYS ALA ASP          
SEQRES   5 A  551  ASP ALA HIS GLY THR PRO ILE MET LEU LYS ALA GLN GLN          
SEQRES   6 A  551  LEU GLY ILE THR PRO GLU GLN MET ILE GLY GLU MET SER          
SEQRES   7 A  551  GLN GLU HIS GLN THR ASP PHE ALA GLY PHE ASN ILE SER          
SEQRES   8 A  551  TYR ASP ASN TYR HIS SER THR HIS SER GLU GLU ASN ARG          
SEQRES   9 A  551  GLN LEU SER GLU LEU ILE TYR SER ARG LEU LYS GLU ASN          
SEQRES  10 A  551  GLY PHE ILE LYS ASN ARG THR ILE SER GLN LEU TYR ASP          
SEQRES  11 A  551  PRO GLU LYS GLY MET PHE LEU PRO ASP ARG PHE VAL LYS          
SEQRES  12 A  551  GLY THR CYS PRO LYS CYS LYS SER PRO ASP GLN TYR GLY          
SEQRES  13 A  551  ASP ASN CYS GLU VAL CYS GLY ALA THR TYR SER PRO THR          
SEQRES  14 A  551  GLU LEU ILE GLU PRO LYS SER VAL VAL SER GLY ALA THR          
SEQRES  15 A  551  PRO VAL MET ARG ASP SER GLU HIS PHE PHE PHE ASP LEU          
SEQRES  16 A  551  PRO SER PHE SER GLU MET LEU GLN ALA TRP THR ARG SER          
SEQRES  17 A  551  GLY ALA LEU GLN GLU GLN VAL ALA ASN LYS MET GLN GLU          
SEQRES  18 A  551  TRP PHE GLU SER GLY LEU GLN GLN TRP ASP ILE SER ARG          
SEQRES  19 A  551  ASP ALA PRO TYR PHE GLY PHE GLU ILE PRO ASN ALA PRO          
SEQRES  20 A  551  GLY LYS TYR PHE TYR VAL TRP LEU ASP ALA PRO ILE GLY          
SEQRES  21 A  551  TYR MET GLY SER PHE LYS ASN LEU CYS ASP LYS ARG GLY          
SEQRES  22 A  551  ASP SER VAL SER PHE ASP GLU TYR TRP LYS LYS ASP SER          
SEQRES  23 A  551  THR ALA GLU LEU TYR HIS PHE ILE GLY LYS ASP ILE VAL          
SEQRES  24 A  551  TYR PHE HIS SER LEU PHE TRP PRO ALA MET LEU GLU GLY          
SEQRES  25 A  551  SER ASN PHE ARG LYS PRO SER ASN LEU PHE VAL HIS GLY          
SEQRES  26 A  551  TYR VAL THR VAL ASN GLY ALA LYS MET SER LYS SER ARG          
SEQRES  27 A  551  GLY THR PHE ILE LYS ALA SER THR TRP LEU ASN HIS PHE          
SEQRES  28 A  551  ASP ALA ASP SER LEU ARG TYR TYR TYR THR ALA LYS LEU          
SEQRES  29 A  551  SER SER ARG ILE ASP ASP ILE ASP LEU ASN LEU GLU ASP          
SEQRES  30 A  551  PHE VAL GLN ARG VAL ASN ALA ASP ILE VAL ASN LYS VAL          
SEQRES  31 A  551  VAL ASN LEU ALA SER ARG ASN ALA GLY PHE ILE ASN LYS          
SEQRES  32 A  551  ARG PHE ASP GLY VAL LEU ALA SER GLU LEU ALA ASP PRO          
SEQRES  33 A  551  GLN LEU TYR LYS THR PHE THR ASP ALA ALA GLU VAL ILE          
SEQRES  34 A  551  GLY GLU ALA TRP GLU SER ARG GLU PHE GLY LYS ALA VAL          
SEQRES  35 A  551  ARG GLU ILE MET ALA LEU ALA ASP LEU ALA ASN ARG TYR          
SEQRES  36 A  551  VAL ASP GLU GLN ALA PRO TRP VAL VAL ALA LYS GLN GLU          
SEQRES  37 A  551  GLY ARG ASP ALA ASP LEU GLN ALA ILE CYS SER MET GLY          
SEQRES  38 A  551  ILE ASN LEU PHE ARG VAL LEU MET THR TYR LEU LYS PRO          
SEQRES  39 A  551  VAL LEU PRO LYS LEU THR GLU ARG ALA GLU ALA PHE LEU          
SEQRES  40 A  551  ASN THR GLU LEU THR TRP ASP GLY ILE GLN GLN PRO LEU          
SEQRES  41 A  551  LEU GLY HIS LYS VAL ASN PRO PHE LYS ALA LEU TYR ASN          
SEQRES  42 A  551  ARG ILE ASP MET ARG GLN VAL GLU ALA LEU VAL GLU ALA          
SEQRES  43 A  551  SER LYS GLU GLU VAL                                          
HET     ZN  A 701       1                                                       
HET    MET  A 601       9                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     MET METHIONINE                                                       
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  MET    C5 H11 N O2 S                                                
FORMUL   4  HOH   *437(H2 O)                                                    
HELIX    1   1 HIS A   21  ARG A   41  1                                  21    
HELIX    2   2 GLY A   55  GLY A   66  1                                  12    
HELIX    3   3 THR A   68  PHE A   87  1                                  20    
HELIX    4   4 SER A   99  ASN A  116  1                                  18    
HELIX    5   5 PRO A  137  ARG A  139  5                                   3    
HELIX    6   6 SER A  166  LEU A  170  5                                   5    
HELIX    7   7 LEU A  194  SER A  196  5                                   3    
HELIX    8   8 PHE A  197  SER A  207  1                                  11    
HELIX    9   9 GLN A  211  GLY A  225  1                                  15    
HELIX   10  10 TYR A  251  GLY A  272  1                                  22    
HELIX   11  11 VAL A  275  LYS A  282  1                                   8    
HELIX   12  12 ILE A  297  LEU A  303  1                                   7    
HELIX   13  13 LEU A  303  SER A  312  1                                  10    
HELIX   14  14 LYS A  342  PHE A  350  1                                   9    
HELIX   15  15 ASP A  351  LEU A  363  1                                  13    
HELIX   16  16 ASN A  373  ILE A  385  1                                  13    
HELIX   17  17 VAL A  389  PHE A  404  1                                  16    
HELIX   18  18 ASP A  414  ALA A  424  1                                  11    
HELIX   19  19 ALA A  424  SER A  434  1                                  11    
HELIX   20  20 GLU A  436  ALA A  459  1                                  24    
HELIX   21  21 ALA A  459  ALA A  464  1                                   6    
HELIX   22  22 ARG A  469  LEU A  491  1                                  23    
HELIX   23  23 LEU A  495  ASN A  507  1                                  13    
HELIX   24  24 TRP A  512  GLN A  517  5                                   6    
HELIX   25  25 ASP A  535  GLU A  548  1                                  14    
SHEET    1   A 5 ASN A  93  SER A  96  0                                        
SHEET    2   A 5 GLU A  44  ASP A  51  1  O  PHE A  47   N  ASN A  93           
SHEET    3   A 5 LYS A   6  CYS A  11  1  N  ILE A   7   O  GLU A  44           
SHEET    4   A 5 GLU A 288  GLY A 294  1  O  GLU A 288   N  LEU A   8           
SHEET    5   A 5 ASN A 319  HIS A 323  1  N  ASN A 319   O  LEU A 289           
SHEET    1   B 4 MET A 134  PHE A 135  0                                        
SHEET    2   B 4 ILE A 119  ASP A 129 -1  N  ASP A 129   O  MET A 134           
SHEET    3   B 4 VAL A 183  PHE A 192 -1  O  VAL A 183   N  TYR A 128           
SHEET    4   B 4 TRP A 229  ASP A 230 -1  O  TRP A 229   N  PHE A 192           
SHEET    1   C 3 GLN A 153  TYR A 154  0                                        
SHEET    2   C 3 VAL A 141  THR A 144 -1  O  GLY A 143   N  GLN A 153           
SHEET    3   C 3 ILE A 171  SER A 175 -1  N  ILE A 171   O  THR A 144           
SHEET    1   D 2 SER A 232  ASP A 234  0                                        
SHEET    2   D 2 LYS A 248  PHE A 250 -1  O  TYR A 249   N  ARG A 233           
SHEET    1   E 2 VAL A 326  VAL A 328  0                                        
SHEET    2   E 2 ILE A 370  LEU A 372  1  O  ILE A 370   N  THR A 327           
LINK        ZN    ZN A 701                 SG  CYS A 145     1555   1555  2.54  
LINK        ZN    ZN A 701                 SG  CYS A 158     1555   1555  2.61  
LINK        ZN    ZN A 701                 SG  CYS A 161     1555   1555  2.54  
LINK        ZN    ZN A 701                 SG  CYS A 148     1555   1555  2.52  
SITE     1 AC1  4 CYS A 145  CYS A 148  CYS A 158  CYS A 161                    
SITE     1 AC2  9 LEU A  13  TYR A  15  ASP A  52  TRP A 253                    
SITE     2 AC2  9 ALA A 256  PRO A 257  TYR A 260  ILE A 297                    
SITE     3 AC2  9 HOH A 744                                                     
CRYST1   78.400   45.160   86.310  90.00 107.91  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      0.012760  0.000000  0.004120        0.00000                         
SCALE2      0.000000  0.022140  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012180        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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