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Database: PDB
Entry: 3H99
LinkDB: 3H99
Original site: 3H99 
HEADER    LIGASE                                  30-APR-09   3H99              
TITLE     STRUCTURE OF A MUTANT METHIONYL-TRNA SYNTHETASE WITH MODIFIED         
TITLE    2 SPECIFICITY COMPLEXED WITH METHIONINE                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHIONYL-TRNA SYNTHETASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: M547 DOMAIN: UNP RESIDUES 2-548;                           
COMPND   5 SYNONYM: METHIONINE-TRNA LIGASE, METRS;                              
COMPND   6 EC: 6.1.1.10;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K-12;                                                        
SOURCE   5 GENE: B2114, JW2101, METG;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM101TR;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMTY21                                    
KEYWDS    ROSSMANN FOLD, AMINOACYL-TRNA SYNTHETASE, ATP-BINDING, LIGASE, METAL- 
KEYWDS   2 BINDING, NUCLEOTIDE-BINDING, PROTEIN BIOSYNTHESIS, RNA-BINDING,      
KEYWDS   3 TRNA-BINDING                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.SCHMITT,I.C.TANRIKULU,T.H.YOO,M.PANVERT,D.A.TIRRELL,Y.MECHULAM      
REVDAT   3   13-JUL-11 3H99    1       VERSN                                    
REVDAT   2   15-DEC-09 3H99    1       TITLE                                    
REVDAT   1   08-DEC-09 3H99    0                                                
JRNL        AUTH   E.SCHMITT,I.C.TANRIKULU,T.H.YOO,M.PANVERT,D.A.TIRRELL,       
JRNL        AUTH 2 Y.MECHULAM                                                   
JRNL        TITL   SWITCHING FROM AN INDUCED-FIT TO A LOCK-AND-KEY MECHANISM IN 
JRNL        TITL 2 AN AMINOACYL-TRNA SYNTHETASE WITH MODIFIED SPECIFICITY.      
JRNL        REF    J.MOL.BIOL.                   V. 394   843 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19837083                                                     
JRNL        DOI    10.1016/J.JMB.2009.10.016                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 111291                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.180                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6697                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4368                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 1047                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.62                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.09400                                             
REMARK   3    B22 (A**2) : -0.98900                                             
REMARK   3    B33 (A**2) : 1.08300                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.05300                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.004                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.22                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : 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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 35.60                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  3  : MAA.PAR                                        
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  5  : CIT.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3H99 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052852.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-SEP-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 111291                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.02500                            
REMARK 200  R SYM                      (I) : 0.02500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.07500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 11.700                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 3H97                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM CITRATE, PH 7.1, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 279K                           
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       22.64650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 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     MET A   -12                                                      
REMARK 465     ARG A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     THR A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     VAL A     3                                                      
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    HIS A  95     -151.15   -114.56                                   
REMARK 500    LYS A 528      -85.48    -57.95                                   
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 A1100        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH A1344        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH A1370        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH A1404        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH A1780        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH A1783        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH A1905        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A1911        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH A1948        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH A1954        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A1962        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A1985        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH A2006        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH A2010        DISTANCE =  6.96 ANGSTROMS                       
REMARK 525    HOH A2030        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH A2031        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A2032        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH A2033        DISTANCE =  5.01 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                              ZN A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 145   SG                                                     
REMARK 620 2 CYS A 148   SG  111.6                                              
REMARK 620 3 CYS A 158   SG  107.0 106.2                                        
REMARK 620 4 CYS A 161   SG  109.6 110.2 112.2                                  
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 MET A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 604                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QQT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H97   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H9B   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H9C   RELATED DB: PDB                                   
DBREF  3H99 A    0   547  UNP    P00959   SYM_ECOLI        1    548             
SEQADV 3H99 MET A  -12  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 ARG A  -11  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 GLY A  -10  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 SER A   -9  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 HIS A   -8  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 HIS A   -7  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 HIS A   -6  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 HIS A   -5  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 HIS A   -4  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 HIS A   -3  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 GLY A   -2  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 SER A   -1  UNP  P00959              EXPRESSION TAG                 
SEQADV 3H99 SER A   13  UNP  P00959    LEU    14 ENGINEERED                     
SEQADV 3H99 LEU A  260  UNP  P00959    TYR   261 ENGINEERED                     
SEQADV 3H99 LEU A  301  UNP  P00959    HIS   302 ENGINEERED                     
SEQRES   1 A  560  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET          
SEQRES   2 A  560  THR GLN VAL ALA LYS LYS ILE LEU VAL THR CYS ALA SER          
SEQRES   3 A  560  PRO TYR ALA ASN GLY SER ILE HIS LEU GLY HIS MET LEU          
SEQRES   4 A  560  GLU HIS ILE GLN ALA ASP VAL TRP VAL ARG TYR GLN ARG          
SEQRES   5 A  560  MET ARG GLY HIS GLU VAL ASN PHE ILE CYS ALA ASP ASP          
SEQRES   6 A  560  ALA HIS GLY THR PRO ILE MET LEU LYS ALA GLN GLN LEU          
SEQRES   7 A  560  GLY ILE THR PRO GLU GLN MET ILE GLY GLU MET SER GLN          
SEQRES   8 A  560  GLU HIS GLN THR ASP PHE ALA GLY PHE ASN ILE SER TYR          
SEQRES   9 A  560  ASP ASN TYR HIS SER THR HIS SER GLU GLU ASN ARG GLN          
SEQRES  10 A  560  LEU SER GLU LEU ILE TYR SER ARG LEU LYS GLU ASN GLY          
SEQRES  11 A  560  PHE ILE LYS ASN ARG THR ILE SER GLN LEU TYR ASP PRO          
SEQRES  12 A  560  GLU LYS GLY MET PHE LEU PRO ASP ARG PHE VAL LYS GLY          
SEQRES  13 A  560  THR CYS PRO LYS CYS LYS SER PRO ASP GLN TYR GLY ASP          
SEQRES  14 A  560  ASN CYS GLU VAL CYS GLY ALA THR TYR SER PRO THR GLU          
SEQRES  15 A  560  LEU ILE GLU PRO LYS SER VAL VAL SER GLY ALA THR PRO          
SEQRES  16 A  560  VAL MET ARG ASP SER GLU HIS PHE PHE PHE ASP LEU PRO          
SEQRES  17 A  560  SER PHE SER GLU MET LEU GLN ALA TRP THR ARG SER GLY          
SEQRES  18 A  560  ALA LEU GLN GLU GLN VAL ALA ASN LYS MET GLN GLU TRP          
SEQRES  19 A  560  PHE GLU SER GLY LEU GLN GLN TRP ASP ILE SER ARG ASP          
SEQRES  20 A  560  ALA PRO TYR PHE GLY PHE GLU ILE PRO ASN ALA PRO GLY          
SEQRES  21 A  560  LYS TYR PHE TYR VAL TRP LEU ASP ALA PRO ILE GLY LEU          
SEQRES  22 A  560  MET GLY SER PHE LYS ASN LEU CYS ASP LYS ARG GLY ASP          
SEQRES  23 A  560  SER VAL SER PHE ASP GLU TYR TRP LYS LYS ASP SER THR          
SEQRES  24 A  560  ALA GLU LEU TYR HIS PHE ILE GLY LYS ASP ILE VAL TYR          
SEQRES  25 A  560  PHE LEU SER LEU PHE TRP PRO ALA MET LEU GLU GLY SER          
SEQRES  26 A  560  ASN PHE ARG LYS PRO SER ASN LEU PHE VAL HIS GLY TYR          
SEQRES  27 A  560  VAL THR VAL ASN GLY ALA LYS MET SER LYS SER ARG GLY          
SEQRES  28 A  560  THR PHE ILE LYS ALA SER THR TRP LEU ASN HIS PHE ASP          
SEQRES  29 A  560  ALA ASP SER LEU ARG TYR TYR TYR THR ALA LYS LEU SER          
SEQRES  30 A  560  SER ARG ILE ASP ASP ILE ASP LEU ASN LEU GLU ASP PHE          
SEQRES  31 A  560  VAL GLN ARG VAL ASN ALA ASP ILE VAL ASN LYS VAL VAL          
SEQRES  32 A  560  ASN LEU ALA SER ARG ASN ALA GLY PHE ILE ASN LYS ARG          
SEQRES  33 A  560  PHE ASP GLY VAL LEU ALA SER GLU LEU ALA ASP PRO GLN          
SEQRES  34 A  560  LEU TYR LYS THR PHE THR ASP ALA ALA GLU VAL ILE GLY          
SEQRES  35 A  560  GLU ALA TRP GLU SER ARG GLU PHE GLY LYS ALA VAL ARG          
SEQRES  36 A  560  GLU ILE MET ALA LEU ALA ASP LEU ALA ASN ARG TYR VAL          
SEQRES  37 A  560  ASP GLU GLN ALA PRO TRP VAL VAL ALA LYS GLN GLU GLY          
SEQRES  38 A  560  ARG ASP ALA ASP LEU GLN ALA ILE CYS SER MET GLY ILE          
SEQRES  39 A  560  ASN LEU PHE ARG VAL LEU MET THR TYR LEU LYS PRO VAL          
SEQRES  40 A  560  LEU PRO LYS LEU THR GLU ARG ALA GLU ALA PHE LEU ASN          
SEQRES  41 A  560  THR GLU LEU THR TRP ASP GLY ILE GLN GLN PRO LEU LEU          
SEQRES  42 A  560  GLY HIS LYS VAL ASN PRO PHE LYS ALA LEU TYR ASN ARG          
SEQRES  43 A  560  ILE ASP MET ARG GLN VAL GLU ALA LEU VAL GLU ALA SER          
SEQRES  44 A  560  LYS                                                          
HET    MET  A 602       9                                                       
HET     ZN  A 601       1                                                       
HET    CIT  A 603      13                                                       
HET    CIT  A 604      13                                                       
HETNAM     MET METHIONINE                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     CIT CITRIC ACID                                                      
FORMUL   2  MET    C5 H11 N O2 S                                                
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  CIT    2(C6 H8 O7)                                                  
FORMUL   6  HOH   *1047(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  390  ARG A  395  1                                   6    
HELIX   18  18 ASN A  396  PHE A  404  1                                   9    
HELIX   19  19 ASP A  414  ALA A  424  1                                  11    
HELIX   20  20 ALA A  424  SER A  434  1                                  11    
HELIX   21  21 GLU A  436  ALA A  459  1                                  24    
HELIX   22  22 ALA A  459  ALA A  464  1                                   6    
HELIX   23  23 ARG A  469  LYS A  492  1                                  24    
HELIX   24  24 LEU A  495  ASN A  507  1                                  13    
HELIX   25  25 TRP A  512  GLN A  517  5                                   6    
HELIX   26  26 ASP A  535  LYS A  547  1                                  13    
SHEET    1   A 5 ASN A  93  SER A  96  0                                        
SHEET    2   A 5 GLU A  44  ASP A  51  1  N  CYS A  49   O  HIS A  95           
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  LYS A   6           
SHEET    5   A 5 ASN A 319  HIS A 323  1  O  PHE A 321   N  HIS A 291           
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  PHE A 191   N  LYS A 120           
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  N  GLY A 143   O  GLN A 153           
SHEET    3   C 3 ILE A 171  SER A 175 -1  O  LYS A 174   N  LYS A 142           
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 3 ALA A 331  LYS A 332  0                                        
SHEET    2   E 3 VAL A 326  VAL A 328 -1  N  VAL A 328   O  ALA A 331           
SHEET    3   E 3 ILE A 370  LEU A 372  1  O  LEU A 372   N  THR A 327           
LINK         SG  CYS A 145                ZN    ZN A 601     1555   1555  2.33  
LINK         SG  CYS A 148                ZN    ZN A 601     1555   1555  2.35  
LINK         SG  CYS A 158                ZN    ZN A 601     1555   1555  2.36  
LINK         SG  CYS A 161                ZN    ZN A 601     1555   1555  2.34  
CISPEP   1 ALA A  235    PRO A  236          0         0.08                     
SITE     1 AC1 13 SER A  13  TYR A  15  ASP A  52  TRP A 253                    
SITE     2 AC1 13 ALA A 256  PRO A 257  ILE A 297  HOH A1442                    
SITE     3 AC1 13 HOH A1462  HOH A1469  HOH A1489  HOH A1506                    
SITE     4 AC1 13 HOH A1938                                                     
SITE     1 AC2  5 CYS A 145  CYS A 148  CYS A 158  VAL A 160                    
SITE     2 AC2  5 CYS A 161                                                     
SITE     1 AC3 13 PRO A 137  ASP A 138  ARG A 233  HOH A1436                    
SITE     2 AC3 13 HOH A1463  HOH A1480  HOH A1495  HOH A1520                    
SITE     3 AC3 13 HOH A1536  HOH A1589  HOH A1929  HOH A1932                    
SITE     4 AC3 13 HOH A1940                                                     
SITE     1 AC4 10 GLN A  63  LYS A 132  HOH A1568  HOH A1586                    
SITE     2 AC4 10 HOH A1596  HOH A1606  HOH A1662  HOH A1663                    
SITE     3 AC4 10 HOH A1978  HOH A2012                                          
CRYST1   78.172   45.293   85.967  90.00 107.25  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      0.012792  0.000000  0.003972        0.00000                         
SCALE2      0.000000  0.022078  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012180        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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