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Database: PDB
Entry: 3CEI
LinkDB: 3CEI
Original site: 3CEI 
HEADER    OXIDOREDUCTASE                          29-FEB-08   3CEI              
TITLE     CRYSTAL STRUCTURE OF SUPEROXIDE DISMUTASE FROM HELICOBACTER           
TITLE    2 PYLORI                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;                            
SOURCE   3 ORGANISM_COMMON: CAMPYLOBACTER PYLORI;                               
SOURCE   4 ORGANISM_TAXID: 210;                                                 
SOURCE   5 STRAIN: CCUG17874;                                                   
SOURCE   6 GENE: SOD;                                                           
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET-28B                                   
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.ESPOSITO,A.SEYDEL,R.AIELLO,G.SORRENTINO,L.CENDRON,                  
AUTHOR   2 G.ZANOTTI,A.ZAGARI                                                   
REVDAT   3   24-FEB-09 3CEI    1       VERSN                                    
REVDAT   2   11-NOV-08 3CEI    1       JRNL                                     
REVDAT   1   10-JUN-08 3CEI    0                                                
JRNL        AUTH   L.ESPOSITO,A.SEYDEL,R.AIELLO,G.SORRENTINO,                   
JRNL        AUTH 2 L.CENDRON,G.ZANOTTI,A.ZAGARI                                 
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE SUPEROXIDE DISMUTASE            
JRNL        TITL 2 FROM HELICOBACTER PYLORI REVEALS A STRUCTURED                
JRNL        TITL 3 C-TERMINAL EXTENSION                                         
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1784  1601 2008              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   18502213                                                     
JRNL        DOI    10.1016/J.BBAPAP.2008.04.024                                 
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 80.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2205746.280                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 22256                          
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) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1051                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3442                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE                    : 0.3170                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 171                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.024                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3453                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 206                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.03000                                              
REMARK   3    B22 (A**2) : 5.03000                                              
REMARK   3    B33 (A**2) : -10.06000                                            
REMARK   3    B12 (A**2) : 7.27000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
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) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.78                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.190 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.960 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.950 ; 2.500                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.910 ; 3.000                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 50.15                                                
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 3CEI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-MAR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046678.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAR-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               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22256                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 18.300                             
REMARK 200  R MERGE                    (I) : 0.11200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 19.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.39500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1ISB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9M AMMONIUM SULFATE, 0.1M TRIS,        
REMARK 280  PH8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296.0K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       79.01550            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       79.01550            
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       79.01550            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       79.01550            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       79.01550            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       79.01550            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     LYS B   211                                                      
REMARK 465     LYS B   212                                                      
REMARK 465     LEU B   213                                                      
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    MET A  14       32.92    -98.43                                   
REMARK 500    LYS A  29      -56.07   -120.01                                   
REMARK 500    ASN A 140     -107.55     50.51                                   
REMARK 500    TYR A 162       -1.83   -140.74                                   
REMARK 500    LYS A 167     -130.94     53.68                                   
REMARK 500    HIS A 210       40.74   -105.76                                   
REMARK 500    LYS A 212      100.85    -58.29                                   
REMARK 500    PHE B  17      -60.12   -123.77                                   
REMARK 500    ASN B 140     -109.27     47.50                                   
REMARK 500    LYS B 167     -130.61     48.33                                   
REMARK 500    VAL B 209      -73.76   -134.04                                   
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                              FE A 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  73   NE2  85.6                                              
REMARK 620 3 ASP A 156   OD2  89.5 107.6                                        
REMARK 620 4 HIS A 160   NE2  90.5 127.5 124.7                                  
REMARK 620 5 HOH A 600   O   178.3  93.6  89.3  91.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 500  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 HIS B  73   NE2  91.3                                              
REMARK 620 3 ASP B 156   OD2  88.1 106.7                                        
REMARK 620 4 HIS B 160   NE2  90.1 126.8 126.5                                  
REMARK 620 5 HOH B 600   O   172.7  90.1  84.7  94.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 500                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 500                  
DBREF  3CEI A    1   213  UNP    B1VJF0   B1VJF0_HELPY     1    213             
DBREF  3CEI B    1   213  UNP    B1VJF0   B1VJF0_HELPY     1    213             
SEQRES   1 A  213  MET PHE THR LEU ARG GLU LEU PRO PHE ALA LYS ASP SER          
SEQRES   2 A  213  MET GLY ASP PHE LEU SER PRO VAL ALA PHE ASP PHE HIS          
SEQRES   3 A  213  HIS GLY LYS HIS HIS GLN THR TYR VAL ASN ASN LEU ASN          
SEQRES   4 A  213  ASN LEU ILE LYS GLY THR ASP PHE GLU LYS SER SER LEU          
SEQRES   5 A  213  PHE ALA ILE LEU THR LYS SER SER GLY GLY VAL PHE ASN          
SEQRES   6 A  213  ASN ALA ALA GLN ILE TYR ASN HIS ASP PHE TYR TRP ASP          
SEQRES   7 A  213  CYS LEU SER PRO LYS ALA THR ALA LEU SER ASP GLU LEU          
SEQRES   8 A  213  LYS GLY ALA LEU GLU LYS ASP PHE GLY SER LEU GLU LYS          
SEQRES   9 A  213  PHE LYS GLU ASP PHE ILE LYS SER ALA THR THR LEU PHE          
SEQRES  10 A  213  GLY SER GLY TRP ASN TRP ALA ALA TYR ASN LEU ASP THR          
SEQRES  11 A  213  GLN LYS ILE GLU ILE ILE GLN THR SER ASN ALA GLN THR          
SEQRES  12 A  213  PRO VAL THR ASP LYS LYS VAL PRO LEU LEU VAL VAL ASP          
SEQRES  13 A  213  VAL TRP GLU HIS ALA TYR TYR ILE ASP HIS LYS ASN ALA          
SEQRES  14 A  213  ARG PRO VAL TYR LEU GLU LYS PHE TYR GLY HIS ILE ASN          
SEQRES  15 A  213  TRP HIS PHE VAL SER GLN CYS TYR GLU TRP ALA LYS LYS          
SEQRES  16 A  213  GLU GLY LEU GLY SER VAL ASP TYR TYR ILE ASN GLU LEU          
SEQRES  17 A  213  VAL HIS LYS LYS LEU                                          
SEQRES   1 B  213  MET PHE THR LEU ARG GLU LEU PRO PHE ALA LYS ASP SER          
SEQRES   2 B  213  MET GLY ASP PHE LEU SER PRO VAL ALA PHE ASP PHE HIS          
SEQRES   3 B  213  HIS GLY LYS HIS HIS GLN THR TYR VAL ASN ASN LEU ASN          
SEQRES   4 B  213  ASN LEU ILE LYS GLY THR ASP PHE GLU LYS SER SER LEU          
SEQRES   5 B  213  PHE ALA ILE LEU THR LYS SER SER GLY GLY VAL PHE ASN          
SEQRES   6 B  213  ASN ALA ALA GLN ILE TYR ASN HIS ASP PHE TYR TRP ASP          
SEQRES   7 B  213  CYS LEU SER PRO LYS ALA THR ALA LEU SER ASP GLU LEU          
SEQRES   8 B  213  LYS GLY ALA LEU GLU LYS ASP PHE GLY SER LEU GLU LYS          
SEQRES   9 B  213  PHE LYS GLU ASP PHE ILE LYS SER ALA THR THR LEU PHE          
SEQRES  10 B  213  GLY SER GLY TRP ASN TRP ALA ALA TYR ASN LEU ASP THR          
SEQRES  11 B  213  GLN LYS ILE GLU ILE ILE GLN THR SER ASN ALA GLN THR          
SEQRES  12 B  213  PRO VAL THR ASP LYS LYS VAL PRO LEU LEU VAL VAL ASP          
SEQRES  13 B  213  VAL TRP GLU HIS ALA TYR TYR ILE ASP HIS LYS ASN ALA          
SEQRES  14 B  213  ARG PRO VAL TYR LEU GLU LYS PHE TYR GLY HIS ILE ASN          
SEQRES  15 B  213  TRP HIS PHE VAL SER GLN CYS TYR GLU TRP ALA LYS LYS          
SEQRES  16 B  213  GLU GLY LEU GLY SER VAL ASP TYR TYR ILE ASN GLU LEU          
SEQRES  17 B  213  VAL HIS LYS LYS LEU                                          
HET     FE  A 500       1                                                       
HET    SO4  A 700       5                                                       
HET     FE  B 500       1                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *206(H2 O)                                                    
HELIX    1   1 SER A   19  HIS A   27  1                                   9    
HELIX    2   2 LYS A   29  LYS A   43  1                                  15    
HELIX    3   3 SER A   51  SER A   59  1                                   9    
HELIX    4   4 SER A   60  CYS A   79  1                                  20    
HELIX    5   5 SER A   88  GLY A  100  1                                  13    
HELIX    6   6 SER A  101  LEU A  116  1                                  16    
HELIX    7   7 THR A  143  LYS A  148  5                                   6    
HELIX    8   8 TRP A  158  ALA A  161  5                                   4    
HELIX    9   9 TYR A  162  LYS A  167  1                                   6    
HELIX   10  10 ALA A  169  HIS A  180  1                                  12    
HELIX   11  11 ASN A  182  GLY A  197  1                                  16    
HELIX   12  12 LEU A  198  VAL A  209  1                                  12    
HELIX   13  13 SER B   19  HIS B   27  1                                   9    
HELIX   14  14 LYS B   29  LYS B   43  1                                  15    
HELIX   15  15 SER B   51  SER B   59  1                                   9    
HELIX   16  16 SER B   60  CYS B   79  1                                  20    
HELIX   17  17 SER B   88  GLY B  100  1                                  13    
HELIX   18  18 SER B  101  LEU B  116  1                                  16    
HELIX   19  19 THR B  143  ASP B  147  5                                   5    
HELIX   20  20 TRP B  158  ALA B  161  5                                   4    
HELIX   21  21 TYR B  162  LYS B  167  1                                   6    
HELIX   22  22 ALA B  169  HIS B  180  1                                  12    
HELIX   23  23 ASN B  182  GLY B  197  1                                  16    
HELIX   24  24 LEU B  198  LEU B  208  1                                  11    
SHEET    1   A 3 ILE A 133  SER A 139  0                                        
SHEET    2   A 3 GLY A 120  TYR A 126 -1  N  TRP A 123   O  ILE A 136           
SHEET    3   A 3 VAL A 150  ASP A 156 -1  O  LEU A 152   N  ALA A 124           
SHEET    1   B 3 ILE B 133  SER B 139  0                                        
SHEET    2   B 3 GLY B 120  ASN B 127 -1  N  TRP B 123   O  ILE B 136           
SHEET    3   B 3 LYS B 149  ASP B 156 -1  O  VAL B 150   N  TYR B 126           
LINK         NE2 HIS A  26                FE    FE A 500     1555   1555  2.10  
LINK         NE2 HIS A  73                FE    FE A 500     1555   1555  2.09  
LINK         OD2 ASP A 156                FE    FE A 500     1555   1555  1.91  
LINK         NE2 HIS A 160                FE    FE A 500     1555   1555  2.10  
LINK         NE2 HIS B  26                FE    FE B 500     1555   1555  2.11  
LINK         NE2 HIS B  73                FE    FE B 500     1555   1555  2.12  
LINK         OD2 ASP B 156                FE    FE B 500     1555   1555  1.92  
LINK         NE2 HIS B 160                FE    FE B 500     1555   1555  2.10  
LINK        FE    FE A 500                 O   HOH A 600     1555   1555  2.00  
LINK        FE    FE B 500                 O   HOH B 600     1555   1555  2.04  
SITE     1 AC1  4 HIS A  26  HIS A  73  ASP A 156  HIS A 160                    
SITE     1 AC2  4 HIS B  26  HIS B  73  ASP B 156  HIS B 160                    
CRYST1  108.716  108.716  158.031  90.00  90.00 120.00 P 63 2 2     24          
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      0.009198  0.005311  0.000000        0.00000                         
SCALE2      0.000000  0.010621  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006328        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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