GenomeNet

Database: PDB
Entry: 3EXY
LinkDB: 3EXY
Original site: 3EXY 
HEADER    ELECTRON TRANSPORT                      17-OCT-08   3EXY              
TITLE     CRYSTAL STRUCTURE OF THE 2[4FE-4S] FERREDOXIN V13G VARIANT            
TITLE    2 FROM ALLOCHROMATIUM VINOSUM                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERREDOXIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ALLOCHROMATIUM VINOSUM;                         
SOURCE   3 ORGANISM_COMMON: ALLOCHROMATIUM VINOSUM;                             
SOURCE   4 ORGANISM_TAXID: 1049;                                                
SOURCE   5 GENE: FDX;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ELECTRON TRANSPORT, FERREDOXIN, [4FE-4S] CLUSTERS, 4FE-4S,            
KEYWDS   2 IRON, IRON-SULFUR, METAL-BINDING, TRANSPORT                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.GIASTAS,E.SARIDAKIS,I.M.MAVRIDIS                                    
REVDAT   2   23-JUN-09 3EXY    1       JRNL                                     
REVDAT   1   05-MAY-09 3EXY    0                                                
JRNL        AUTH   E.SARIDAKIS,P.GIASTAS,G.EFTHYMIOU,V.THOMA,                   
JRNL        AUTH 2 J.M.MOULIS,P.KYRITSIS,I.M.MAVRIDIS                           
JRNL        TITL   INSIGHT INTO THE PROTEIN AND SOLVENT CONTRIBUTIONS           
JRNL        TITL 2 TO THE REDUCTION POTENTIALS OF [4FE-4S]2+/+                  
JRNL        TITL 3 CLUSTERS: CRYSTAL STRUCTURES OF THE ALLOCHROMATIUM           
JRNL        TITL 4 VINOSUM FERREDOXIN VARIANTS C57A AND V13G AND THE            
JRNL        TITL 5 HOMOLOGOUS ESCHERICHIA COLI FERREDOXIN.                      
JRNL        REF    J.BIOL.INORG.CHEM.            V.  14   783 2009              
JRNL        REFN                   ISSN 0949-8257                               
JRNL        PMID   19290553                                                     
JRNL        DOI    10.1007/S00775-009-0492-X                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.48 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.2                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : THIN SHELLS                    
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.170                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.162                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.218                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.600                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1017                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 18070                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.148                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.140                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.189                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.400                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 741                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 13726                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 627                                           
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 16                                            
REMARK   3   SOLVENT ATOMS      : 169                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 753.75                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 4                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 6375                    
REMARK   3   NUMBER OF RESTRAINTS                     : 7161                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.012                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.028                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL                    
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.016                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE       
REMARK   3  R (NO CUTOFF)                                                       
REMARK   4                                                                      
REMARK   4 3EXY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049906.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.81                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARREASEARCH                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18180                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1BLU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M AMMONIUM SULPHATE, 0.3 M            
REMARK 280  SODIUM CHLORIDE, 0.1 M TRIS , PH 8.0, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.47500            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       50.95000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       50.95000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       25.47500            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 151  LIES ON A SPECIAL POSITION.                          
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     GLY A    82                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   81   CA    C     O     CB    CG    CD    OE1             
REMARK 480     GLU A   81   OE2                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  72   NE  -  CZ  -  NH1 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ARG A  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 225        DISTANCE =  6.31 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 83                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 84                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BLU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE ALLOCHROMATIUM VINOSUM                
REMARK 900 FERREDOXIN                                                           
REMARK 900 RELATED ID: 3EUN   RELATED DB: PDB                                   
REMARK 900 ATOMIC RESOLUTION CRYSTAL STRUCTURE OF C57A FERREDOXIN               
REMARK 900 VARIANT FROM ALLOCHROMATIUM VINOSUM                                  
REMARK 900 RELATED ID: 1FDN   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CLOSTRIDIUM ACIDURICI FERREDOXIN                
REMARK 900 RELATED ID: 2FDN   RELATED DB: PDB                                   
REMARK 900 ATOMIC RESOLUTION CRYSTAL STRUCTURE OF CLOSTRIDIUM                   
REMARK 900 ACIDURICI FERREDOXIN                                                 
REMARK 900 RELATED ID: 2FGO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA FERREDOXIN               
DBREF  3EXY A    1    82  UNP    P00208   FER_CHRVI        2     83             
SEQADV 3EXY GLY A   13  UNP  P00208    VAL    14 ENGINEERED                     
SEQRES   1 A   82  ALA LEU MET ILE THR ASP GLU CYS ILE ASN CYS ASP GLY          
SEQRES   2 A   82  CYS GLU PRO GLU CYS PRO ASN GLY ALA ILE SER GLN GLY          
SEQRES   3 A   82  ASP GLU THR TYR VAL ILE GLU PRO SER LEU CYS THR GLU          
SEQRES   4 A   82  CYS VAL GLY HIS TYR GLU THR SER GLN CYS VAL GLU VAL          
SEQRES   5 A   82  CYS PRO VAL ASP CYS ILE ILE LYS ASP PRO SER HIS GLU          
SEQRES   6 A   82  GLU THR GLU ASP GLU LEU ARG ALA LYS TYR GLU ARG ILE          
SEQRES   7 A   82  THR GLY GLU GLY                                              
HET    SF4  A  83       8                                                       
HET    SF4  A  84       8                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
FORMUL   2  SF4    2(FE4 S4)                                                    
FORMUL   4  HOH   *169(H2 O)                                                    
HELIX    1   1 CYS A   14  CYS A   18  5                                   5    
HELIX    2   2 PRO A   34  CYS A   37  5                                   4    
HELIX    3   3 SER A   47  CYS A   53  1                                   7    
HELIX    4   4 PRO A   62  GLU A   65  5                                   4    
HELIX    5   5 THR A   67  GLY A   80  1                                  14    
SHEET    1   A 2 LEU A   2  ILE A   4  0                                        
SHEET    2   A 2 ILE A  58  LYS A  60 -1  O  ILE A  59   N  MET A   3           
SHEET    1   B 2 ILE A  23  GLN A  25  0                                        
SHEET    2   B 2 TYR A  30  ILE A  32 -1  O  VAL A  31   N  SER A  24           
LINK         SG  CYS A   8                FE1  SF4 A  83     1555   1555  2.30  
LINK         SG  CYS A  11                FE2  SF4 A  83     1555   1555  2.28  
LINK         SG  CYS A  14                FE3  SF4 A  83     1555   1555  2.26  
LINK         SG  CYS A  18                FE4  SF4 A  84     1555   1555  2.30  
LINK         SG  CYS A  37                FE1  SF4 A  84     1555   1555  2.31  
LINK         SG  CYS A  40                FE2  SF4 A  84     1555   1555  2.28  
LINK         SG  CYS A  49                FE3  SF4 A  84     1555   1555  2.26  
LINK         SG  CYS A  53                FE4  SF4 A  83     1555   1555  2.28  
SITE     1 AC1 10 ILE A   4  CYS A   8  ILE A   9  CYS A  11                    
SITE     2 AC1 10 ASP A  12  CYS A  14  TYR A  30  CYS A  53                    
SITE     3 AC1 10 PRO A  54  CYS A  57                                          
SITE     1 AC2  8 LEU A   2  CYS A  18  CYS A  37  THR A  38                    
SITE     2 AC2  8 GLU A  39  CYS A  40  SER A  47  CYS A  49                    
CRYST1   51.425   51.425   76.425  90.00  90.00 120.00 P 31 2 1      6          
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      0.019446  0.011227  0.000000        0.00000                         
SCALE2      0.000000  0.022454  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013085        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system