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Database: PDB
Entry: 1PFY
LinkDB: 1PFY
Original site: 1PFY 
HEADER    LIGASE                                  27-MAY-03   1PFY              
TITLE     METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED             
TITLE    2 WITH METHIONYL SULPHAMOYL ADENOSINE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHIONYL-TRNA SYNTHETASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-551;                                            
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: 562;                                                 
SOURCE   4 GENE: METG;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM101TR;                                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBLUESCRIPT                               
KEYWDS    ROSSMANN FOLD, LIGASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.CREPIN,E.SCHMITT,Y.MECHULAM,P.B.SAMPSON,M.D.VAUGHAN,                
AUTHOR   2 J.F.HONEK,S.BLANQUET                                                 
REVDAT   4   24-FEB-09 1PFY    1       VERSN                                    
REVDAT   3   15-MAR-05 1PFY    1       FORMUL                                   
REVDAT   2   24-FEB-04 1PFY    1       AUTHOR                                   
REVDAT   1   17-FEB-04 1PFY    0                                                
JRNL        AUTH   T.CREPIN,E.SCHMITT,Y.MECHULAM,P.B.SAMPSON,                   
JRNL        AUTH 2 M.D.VAUGHAN,J.F.HONEK,S.BLANQUET                             
JRNL        TITL   USE OF ANALOGUES OF METHIONINE AND METHIONYL                 
JRNL        TITL 2 ADENYLATE TO SAMPLE CONFORMATIONAL CHANGES DURING            
JRNL        TITL 3 CATALYSIS IN ESCHERICHIA COLI METHIONYL-TRNA                 
JRNL        TITL 4 SYNTHETASE.                                                  
JRNL        REF    J.MOL.BIOL.                   V. 332    59 2003              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12946347                                                     
JRNL        DOI    10.1016/S0022-2836(03)00917-3                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.93 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.00                          
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)   (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 41999                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2106                            
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) : 1.93                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 39                           
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            : 4390                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 459                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.61000                                             
REMARK   3    B22 (A**2) : 0.39300                                              
REMARK   3    B33 (A**2) : 0.21800                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.31700                                             
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) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.18                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
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        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PFY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019300.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : LURE                               
REMARK 200  BEAMLINE                       : DW32                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.967                              
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41999                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.31700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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: 1QQT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM CITRATE, POTASSIUM              
REMARK 280  PHOSPHATE, PH 7, VAPOR DIFFUSION, TEMPERATURE 280K                  
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       22.59650            
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 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 465     LYS A   551                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 467    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 548    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 550    CG1  CG2                                            
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    ALA A  50      165.64    174.04                                   
REMARK 500    HIS A  95     -142.35   -109.90                                   
REMARK 500    LYS A 147      -74.06    -79.02                                   
REMARK 500    VAL A 160      -60.05   -100.17                                   
REMARK 500    LEU A 495       76.04   -119.96                                   
REMARK 500    ALA A 529      125.46    -34.38                                   
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 A1399        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A1409        DISTANCE =  5.76 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 552  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 145   SG                                                     
REMARK 620 2 CYS A 148   SG  115.5                                              
REMARK 620 3 CYS A 158   SG  106.7 104.7                                        
REMARK 620 4 CYS A 161   SG  105.9 114.0 109.8                                  
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 552                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MSP A 553                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1P7P   RELATED DB: PDB                                   
REMARK 900 METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED            
REMARK 900 WITH METHIONINE PHOSPHINATE                                          
REMARK 900 RELATED ID: 1PFU   RELATED DB: PDB                                   
REMARK 900 METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED            
REMARK 900 WITH METHIONINE PHOSPHINATE                                          
REMARK 900 RELATED ID: 1PFV   RELATED DB: PDB                                   
REMARK 900 METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED            
REMARK 900 WITH METHIONINE PHOSPHINATE                                          
REMARK 900 RELATED ID: 1PFW   RELATED DB: PDB                                   
REMARK 900 METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED            
REMARK 900 WITH METHIONINE PHOSPHINATE                                          
REMARK 900 RELATED ID: 1PG0   RELATED DB: PDB                                   
REMARK 900 METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED            
REMARK 900 WITH METHIONINE PHOSPHINATE                                          
REMARK 900 RELATED ID: 1PG2   RELATED DB: PDB                                   
REMARK 900 METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED            
REMARK 900 WITH METHIONINE PHOSPHINATE                                          
DBREF  1PFY A    1   551  UNP    P00959   SYM_ECOLI        1    551             
SEQRES   1 A  551  THR GLN VAL ALA LYS LYS ILE LEU VAL THR CYS ALA LEU          
SEQRES   2 A  551  PRO TYR ALA ASN GLY SER ILE HIS LEU GLY HIS MET LEU          
SEQRES   3 A  551  GLU HIS ILE GLN ALA ASP VAL TRP VAL ARG TYR GLN ARG          
SEQRES   4 A  551  MET ARG GLY HIS GLU VAL ASN PHE ILE CYS ALA ASP ASP          
SEQRES   5 A  551  ALA HIS GLY THR PRO ILE MET LEU LYS ALA GLN GLN LEU          
SEQRES   6 A  551  GLY ILE THR PRO GLU GLN MET ILE GLY GLU MET SER GLN          
SEQRES   7 A  551  GLU HIS GLN THR ASP PHE ALA GLY PHE ASN ILE SER TYR          
SEQRES   8 A  551  ASP ASN TYR HIS SER THR HIS SER GLU GLU ASN ARG GLN          
SEQRES   9 A  551  LEU SER GLU LEU ILE TYR SER ARG LEU LYS GLU ASN GLY          
SEQRES  10 A  551  PHE ILE LYS ASN ARG THR ILE SER GLN LEU TYR ASP PRO          
SEQRES  11 A  551  GLU LYS GLY MET PHE LEU PRO ASP ARG PHE VAL LYS GLY          
SEQRES  12 A  551  THR CYS PRO LYS CYS LYS SER PRO ASP GLN TYR GLY ASP          
SEQRES  13 A  551  ASN CYS GLU VAL CYS GLY ALA THR TYR SER PRO THR GLU          
SEQRES  14 A  551  LEU ILE GLU PRO LYS SER VAL VAL SER GLY ALA THR PRO          
SEQRES  15 A  551  VAL MET ARG ASP SER GLU HIS PHE PHE PHE ASP LEU PRO          
SEQRES  16 A  551  SER PHE SER GLU MET LEU GLN ALA TRP THR ARG SER GLY          
SEQRES  17 A  551  ALA LEU GLN GLU GLN VAL ALA ASN LYS MET GLN GLU TRP          
SEQRES  18 A  551  PHE GLU SER GLY LEU GLN GLN TRP ASP ILE SER ARG ASP          
SEQRES  19 A  551  ALA PRO TYR PHE GLY PHE GLU ILE PRO ASN ALA PRO GLY          
SEQRES  20 A  551  LYS TYR PHE TYR VAL TRP LEU ASP ALA PRO ILE GLY TYR          
SEQRES  21 A  551  MET GLY SER PHE LYS ASN LEU CYS ASP LYS ARG GLY ASP          
SEQRES  22 A  551  SER VAL SER PHE ASP GLU TYR TRP LYS LYS ASP SER THR          
SEQRES  23 A  551  ALA GLU LEU TYR HIS PHE ILE GLY LYS ASP ILE VAL TYR          
SEQRES  24 A  551  PHE HIS SER LEU PHE TRP PRO ALA MET LEU GLU GLY SER          
SEQRES  25 A  551  ASN PHE ARG LYS PRO SER ASN LEU PHE VAL HIS GLY TYR          
SEQRES  26 A  551  VAL THR VAL ASN GLY ALA LYS MET SER LYS SER ARG GLY          
SEQRES  27 A  551  THR PHE ILE LYS ALA SER THR TRP LEU ASN HIS PHE ASP          
SEQRES  28 A  551  ALA ASP SER LEU ARG TYR TYR TYR THR ALA LYS LEU SER          
SEQRES  29 A  551  SER ARG ILE ASP ASP ILE ASP LEU ASN LEU GLU ASP PHE          
SEQRES  30 A  551  VAL GLN ARG VAL ASN ALA ASP ILE VAL ASN LYS VAL VAL          
SEQRES  31 A  551  ASN LEU ALA SER ARG ASN ALA GLY PHE ILE ASN LYS ARG          
SEQRES  32 A  551  PHE ASP GLY VAL LEU ALA SER GLU LEU ALA ASP PRO GLN          
SEQRES  33 A  551  LEU TYR LYS THR PHE THR ASP ALA ALA GLU VAL ILE GLY          
SEQRES  34 A  551  GLU ALA TRP GLU SER ARG GLU PHE GLY LYS ALA VAL ARG          
SEQRES  35 A  551  GLU ILE MET ALA LEU ALA ASP LEU ALA ASN ARG TYR VAL          
SEQRES  36 A  551  ASP GLU GLN ALA PRO TRP VAL VAL ALA LYS GLN GLU GLY          
SEQRES  37 A  551  ARG ASP ALA ASP LEU GLN ALA ILE CYS SER MET GLY ILE          
SEQRES  38 A  551  ASN LEU PHE ARG VAL LEU MET THR TYR LEU LYS PRO VAL          
SEQRES  39 A  551  LEU PRO LYS LEU THR GLU ARG ALA GLU ALA PHE LEU ASN          
SEQRES  40 A  551  THR GLU LEU THR TRP ASP GLY ILE GLN GLN PRO LEU LEU          
SEQRES  41 A  551  GLY HIS LYS VAL ASN PRO PHE LYS ALA LEU TYR ASN ARG          
SEQRES  42 A  551  ILE ASP MET ARG GLN VAL GLU ALA LEU VAL GLU ALA SER          
SEQRES  43 A  551  LYS GLU GLU VAL LYS                                          
HET     ZN  A 552       1                                                       
HET    MSP  A 553      31                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     MSP 5'-O-[(L-METHIONYL)-SULPHAMOYL]ADENOSINE                         
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  MSP    C15 H25 N7 O7 S2                                             
FORMUL   4  HOH   *459(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  ARG A  206  1                                  10    
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  PHE A  404  1                                  17    
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  LYS A  492  1                                  24    
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  VAL A  550  1                                  16    
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  VAL A   9   O  ILE A  48           
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  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  HIS A 189   N  ARG A 122           
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  ILE A 171   N  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  LEU A 372   N  THR A 327           
LINK        ZN    ZN A 552                 SG  CYS A 145     1555   1555  2.47  
LINK        ZN    ZN A 552                 SG  CYS A 148     1555   1555  2.31  
LINK        ZN    ZN A 552                 SG  CYS A 158     1555   1555  2.44  
LINK        ZN    ZN A 552                 SG  CYS A 161     1555   1555  2.36  
CISPEP   1 ALA A  235    PRO A  236          0        -0.20                     
SITE     1 AC1  4 CYS A 145  CYS A 148  CYS A 158  CYS A 161                    
SITE     1 AC2 25 ALA A  12  LEU A  13  PRO A  14  TYR A  15                    
SITE     2 AC2 25 HIS A  21  GLY A  23  HIS A  24  GLU A  27                    
SITE     3 AC2 25 ASP A  52  TRP A 253  ALA A 256  PRO A 257                    
SITE     4 AC2 25 TYR A 260  GLY A 294  ASP A 296  ILE A 297                    
SITE     5 AC2 25 HIS A 301  HIS A 323  GLY A 324  TYR A 325                    
SITE     6 AC2 25 VAL A 326  HOH A1132  HOH A1420  HOH A1424                    
SITE     7 AC2 25 HOH A1435                                                     
CRYST1   78.803   45.193   86.412  90.00 107.31  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      0.012690  0.000000  0.003955        0.00000                         
SCALE2      0.000000  0.022127  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012121        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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