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Database: PDB
Entry: 3H9C
LinkDB: 3H9C
Original site: 3H9C 
HEADER    LIGASE                                  30-APR-09   3H9C              
TITLE     STRUCTURE OF METHIONYL-TRNA SYNTHETASE: CRYSTAL FORM 2                
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                                                      
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: PBSM547                                   
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   4   24-JUL-19 3H9C    1       REMARK                                   
REVDAT   3   13-JUL-11 3H9C    1       VERSN                                    
REVDAT   2   15-DEC-09 3H9C    1       TITLE                                    
REVDAT   1   08-DEC-09 3H9C    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     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 109028                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6565                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.5470 -  4.3460    0.88     3315   212  0.1570 0.1820        
REMARK   3     2  4.3460 -  3.4510    0.91     3351   208  0.1390 0.1590        
REMARK   3     3  3.4510 -  3.0150    0.93     3375   221  0.1550 0.1810        
REMARK   3     4  3.0150 -  2.7400    0.94     3398   237  0.1690 0.1960        
REMARK   3     5  2.7400 -  2.5430    0.94     3372   235  0.1750 0.2100        
REMARK   3     6  2.5430 -  2.3940    0.95     3429   210  0.1650 0.1940        
REMARK   3     7  2.3940 -  2.2740    0.95     3447   216  0.1590 0.1920        
REMARK   3     8  2.2740 -  2.1750    0.95     3438   238  0.1630 0.1870        
REMARK   3     9  2.1750 -  2.0910    0.95     3484   202  0.1480 0.1770        
REMARK   3    10  2.0910 -  2.0190    0.96     3440   225  0.1490 0.1650        
REMARK   3    11  2.0190 -  1.9560    0.96     3444   210  0.1480 0.1670        
REMARK   3    12  1.9560 -  1.9000    0.96     3473   205  0.1550 0.1860        
REMARK   3    13  1.9000 -  1.8500    0.97     3480   235  0.1540 0.1790        
REMARK   3    14  1.8500 -  1.8050    0.97     3475   221  0.1530 0.1780        
REMARK   3    15  1.8050 -  1.7640    0.97     3470   232  0.1550 0.2030        
REMARK   3    16  1.7640 -  1.7260    0.98     3547   211  0.1570 0.1830        
REMARK   3    17  1.7260 -  1.6920    0.97     3455   205  0.1530 0.1820        
REMARK   3    18  1.6920 -  1.6600    0.97     3551   219  0.1610 0.1810        
REMARK   3    19  1.6600 -  1.6300    0.98     3490   208  0.1620 0.1930        
REMARK   3    20  1.6300 -  1.6030    0.98     3524   225  0.1630 0.1770        
REMARK   3    21  1.6030 -  1.5770    0.98     3504   249  0.1710 0.1980        
REMARK   3    22  1.5770 -  1.5530    0.98     3509   232  0.1740 0.1920        
REMARK   3    23  1.5530 -  1.5300    0.98     3525   219  0.1780 0.2090        
REMARK   3    24  1.5300 -  1.5080    0.98     3485   239  0.1780 0.2110        
REMARK   3    25  1.5080 -  1.4880    0.99     3526   220  0.1850 0.2250        
REMARK   3    26  1.4880 -  1.4680    0.96     3437   220  0.1930 0.1810        
REMARK   3    27  1.4680 -  1.4500    0.93     3331   233  0.2090 0.2270        
REMARK   3    28  1.4500 -  1.4330    0.89     3213   187  0.2180 0.2380        
REMARK   3    29  1.4330 -  1.4160    0.86     3032   210  0.2260 0.2590        
REMARK   3    30  1.4160 -  1.4000    0.81     2943   181  0.2370 0.2730        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 50.75                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.11                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.68900                                              
REMARK   3    B22 (A**2) : 0.27500                                              
REMARK   3    B33 (A**2) : -1.96300                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.20700                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           4499                                  
REMARK   3   ANGLE     :  1.055           6091                                  
REMARK   3   CHIRALITY :  0.072            638                                  
REMARK   3   PLANARITY :  0.005            795                                  
REMARK   3   DIHEDRAL  : 17.681           1627                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3H9C 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 DEPOSITION ID IS D_1000052855.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-09                          
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               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980                              
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   : 109028                             
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     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
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     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.30000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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   (%): 47.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
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       22.70000            
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     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    SER A  90       51.59    -91.37                                   
REMARK 500    HIS A  95     -146.16   -116.71                                   
REMARK 500    VAL A 160      -61.80    -97.95                                   
REMARK 500    LEU A 303      -66.91   -122.68                                   
REMARK 500    LYS A 528      -89.60    -71.93                                   
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 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 145   SG                                                     
REMARK 620 2 CYS A 148   SG  111.0                                              
REMARK 620 3 CYS A 158   SG  106.9 106.4                                        
REMARK 620 4 CYS A 161   SG  109.6 111.0 111.8                                  
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 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 602                 
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: 3H99   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H9B   RELATED DB: PDB                                   
DBREF  3H9C A    1   547  UNP    P00959   SYM_ECOLI        2    548             
SEQRES   1 A  547  THR GLN VAL ALA LYS LYS ILE LEU VAL THR CYS ALA LEU          
SEQRES   2 A  547  PRO TYR ALA ASN GLY SER ILE HIS LEU GLY HIS MET LEU          
SEQRES   3 A  547  GLU HIS ILE GLN ALA ASP VAL TRP VAL ARG TYR GLN ARG          
SEQRES   4 A  547  MET ARG GLY HIS GLU VAL ASN PHE ILE CYS ALA ASP ASP          
SEQRES   5 A  547  ALA HIS GLY THR PRO ILE MET LEU LYS ALA GLN GLN LEU          
SEQRES   6 A  547  GLY ILE THR PRO GLU GLN MET ILE GLY GLU MET SER GLN          
SEQRES   7 A  547  GLU HIS GLN THR ASP PHE ALA GLY PHE ASN ILE SER TYR          
SEQRES   8 A  547  ASP ASN TYR HIS SER THR HIS SER GLU GLU ASN ARG GLN          
SEQRES   9 A  547  LEU SER GLU LEU ILE TYR SER ARG LEU LYS GLU ASN GLY          
SEQRES  10 A  547  PHE ILE LYS ASN ARG THR ILE SER GLN LEU TYR ASP PRO          
SEQRES  11 A  547  GLU LYS GLY MET PHE LEU PRO ASP ARG PHE VAL LYS GLY          
SEQRES  12 A  547  THR CYS PRO LYS CYS LYS SER PRO ASP GLN TYR GLY ASP          
SEQRES  13 A  547  ASN CYS GLU VAL CYS GLY ALA THR TYR SER PRO THR GLU          
SEQRES  14 A  547  LEU ILE GLU PRO LYS SER VAL VAL SER GLY ALA THR PRO          
SEQRES  15 A  547  VAL MET ARG ASP SER GLU HIS PHE PHE PHE ASP LEU PRO          
SEQRES  16 A  547  SER PHE SER GLU MET LEU GLN ALA TRP THR ARG SER GLY          
SEQRES  17 A  547  ALA LEU GLN GLU GLN VAL ALA ASN LYS MET GLN GLU TRP          
SEQRES  18 A  547  PHE GLU SER GLY LEU GLN GLN TRP ASP ILE SER ARG ASP          
SEQRES  19 A  547  ALA PRO TYR PHE GLY PHE GLU ILE PRO ASN ALA PRO GLY          
SEQRES  20 A  547  LYS TYR PHE TYR VAL TRP LEU ASP ALA PRO ILE GLY TYR          
SEQRES  21 A  547  MET GLY SER PHE LYS ASN LEU CYS ASP LYS ARG GLY ASP          
SEQRES  22 A  547  SER VAL SER PHE ASP GLU TYR TRP LYS LYS ASP SER THR          
SEQRES  23 A  547  ALA GLU LEU TYR HIS PHE ILE GLY LYS ASP ILE VAL TYR          
SEQRES  24 A  547  PHE HIS SER LEU PHE TRP PRO ALA MET LEU GLU GLY SER          
SEQRES  25 A  547  ASN PHE ARG LYS PRO SER ASN LEU PHE VAL HIS GLY TYR          
SEQRES  26 A  547  VAL THR VAL ASN GLY ALA LYS MET SER LYS SER ARG GLY          
SEQRES  27 A  547  THR PHE ILE LYS ALA SER THR TRP LEU ASN HIS PHE ASP          
SEQRES  28 A  547  ALA ASP SER LEU ARG TYR TYR TYR THR ALA LYS LEU SER          
SEQRES  29 A  547  SER ARG ILE ASP ASP ILE ASP LEU ASN LEU GLU ASP PHE          
SEQRES  30 A  547  VAL GLN ARG VAL ASN ALA ASP ILE VAL ASN LYS VAL VAL          
SEQRES  31 A  547  ASN LEU ALA SER ARG ASN ALA GLY PHE ILE ASN LYS ARG          
SEQRES  32 A  547  PHE ASP GLY VAL LEU ALA SER GLU LEU ALA ASP PRO GLN          
SEQRES  33 A  547  LEU TYR LYS THR PHE THR ASP ALA ALA GLU VAL ILE GLY          
SEQRES  34 A  547  GLU ALA TRP GLU SER ARG GLU PHE GLY LYS ALA VAL ARG          
SEQRES  35 A  547  GLU ILE MET ALA LEU ALA ASP LEU ALA ASN ARG TYR VAL          
SEQRES  36 A  547  ASP GLU GLN ALA PRO TRP VAL VAL ALA LYS GLN GLU GLY          
SEQRES  37 A  547  ARG ASP ALA ASP LEU GLN ALA ILE CYS SER MET GLY ILE          
SEQRES  38 A  547  ASN LEU PHE ARG VAL LEU MET THR TYR LEU LYS PRO VAL          
SEQRES  39 A  547  LEU PRO LYS LEU THR GLU ARG ALA GLU ALA PHE LEU ASN          
SEQRES  40 A  547  THR GLU LEU THR TRP ASP GLY ILE GLN GLN PRO LEU LEU          
SEQRES  41 A  547  GLY HIS LYS VAL ASN PRO PHE LYS ALA LEU TYR ASN ARG          
SEQRES  42 A  547  ILE ASP MET ARG GLN VAL GLU ALA LEU VAL GLU ALA SER          
SEQRES  43 A  547  LYS                                                          
HET     ZN  A 601       1                                                       
HET    CIT  A 602      13                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     CIT CITRIC ACID                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  CIT    C6 H8 O7                                                     
FORMUL   4  HOH   *1048(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 LYS A  388  ARG A  395  1                                   8    
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  LEU A  491  1                                  23    
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 2 VAL A 326  VAL A 328  0                                        
SHEET    2   E 2 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  2.36  
LINK         SG  CYS A 158                ZN    ZN A 601     1555   1555  2.36  
LINK         SG  CYS A 161                ZN    ZN A 601     1555   1555  2.31  
CISPEP   1 ALA A  235    PRO A  236          0         0.48                     
SITE     1 AC1  4 CYS A 145  CYS A 148  CYS A 158  CYS A 161                    
SITE     1 AC2  8 GLN A  63  LYS A 132  LYS A 465  HOH A 675                    
SITE     2 AC2  8 HOH A1143  HOH A1211  HOH A1296  HOH A1485                    
CRYST1   78.890   45.400   86.210  90.00 107.30  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      0.012676  0.000000  0.003948        0.00000                         
SCALE2      0.000000  0.022026  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012149        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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