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Database: PDB
Entry: 3LIO
LinkDB: 3LIO
Original site: 3LIO 
HEADER    OXIDOREDUCTASE                          25-JAN-10   3LIO              
TITLE     X-RAY STRUCTURE OF THE IRON SUPEROXIDE DISMUTASE FROM                 
TITLE    2 PSEUDOALTEROMONAS HALOPLANKTIS (CRYSTAL FORM I)                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IRON 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: PSEUDOALTEROMONAS HALOPLANKTIS;                 
SOURCE   3 ORGANISM_TAXID: 326442;                                              
SOURCE   4 STRAIN: TAC 125;                                                     
SOURCE   5 GENE: PSHAA1215, SODB;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    COLD ADAPTATION, SUPEROXIDE DISMUTASE, FLEXIBILITY, THERMAL           
KEYWDS   2 STABILITY, PSYCHROPHILIC PROTEIN, METAL-BINDING, OXIDOREDUCTASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.MERLINO,I.RUSSO KRAUSS,B.ROSSI,M.CONTE,A.VERGARA,F.SICA             
REVDAT   2   24-NOV-10 3LIO    1       JRNL                                     
REVDAT   1   08-SEP-10 3LIO    0                                                
JRNL        AUTH   A.MERLINO,I.RUSSO KRAUSS,I.CASTELLANO,E.DE VENDITTIS,        
JRNL        AUTH 2 B.ROSSI,M.CONTE,A.VERGARA,F.SICA                             
JRNL        TITL   STRUCTURE AND FLEXIBILITY IN COLD-ADAPTED IRON SUPEROXIDE    
JRNL        TITL 2 DISMUTASES: THE CASE OF THE ENZYME ISOLATED FROM             
JRNL        TITL 3 PSEUDOALTEROMONAS HALOPLANKTIS.                              
JRNL        REF    J.STRUCT.BIOL.                V. 172   343 2010              
JRNL        REFN                   ISSN 1047-8477                               
JRNL        PMID   20732427                                                     
JRNL        DOI    10.1016/J.JSB.2010.08.008                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.MERLINO,I.RUSSO KRAUSS,I.CASTELLANO,E.DE VENDITTIS,        
REMARK   1  AUTH 2 A.VERGARA,F.SICA                                             
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF 
REMARK   1  TITL 2 A PSYCHROPHILIC IRON SUPEROXIDE DISMUTASE FROM               
REMARK   1  TITL 3 PSEUDOLATEROMONAS HALOPLANKTIS                               
REMARK   1  REF    PROTEIN AND PEPTIDE LETTERS   V.  15   415 2008              
REMARK   1  REFN                   ISSN 0929-8665                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 54954                          
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) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2773                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3022                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 461                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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 3LIO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057325.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66818                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06000                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
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: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1ISA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULPHATE, 1.0M SODIUM      
REMARK 280  CHLORIDE, 0.1M HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 293K                                                    
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       51.85700            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 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    LYS A  46       11.37    -68.94                                   
REMARK 500    ASN A 140     -111.17     60.96                                   
REMARK 500    ASP A 148      123.86    -38.59                                   
REMARK 500    ARG A 168     -127.20     53.40                                   
REMARK 500    LYS B  46       27.70    -75.29                                   
REMARK 500    ASN B 140     -108.34     59.30                                   
REMARK 500    ARG B 168     -126.27     52.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ILE A  42        22.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE B  42        24.4      L          L   OUTSIDE RANGE           
REMARK 500    GLU B  48        24.9      L          L   OUTSIDE RANGE           
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 B1066        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH B1070        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH B1085        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH A1138        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH B1171        DISTANCE =  5.16 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                              FE B5001  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 157   OD2                                                    
REMARK 620 2 HIS B 161   NE2 123.1                                              
REMARK 620 3 HIS B  26   NE2  88.3  88.8                                        
REMARK 620 4 HIS B  73   NE2 112.1 124.8  94.9                                  
REMARK 620 5 HOH B1054   O    87.6  94.1 175.8  86.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A5000  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 157   OD2                                                    
REMARK 620 2 HIS A 161   NE2 122.7                                              
REMARK 620 3 HIS A  73   NE2 113.6 123.7                                        
REMARK 620 4 HIS A  26   NE2  86.1  89.8  96.3                                  
REMARK 620 5 HOH A1039   O    88.1  92.6  87.0 174.1                            
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 TRE A 8000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 5000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE B 8001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 5001                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LJ9   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURE OF THE IRON SUPEROXIDE DISMUTASE FROM                
REMARK 900 PSEUDOALTEROMONAS HALOPLANKTIS IN COMPLEX WITH SODIUM AZIDE          
REMARK 900 RELATED ID: 3LJF   RELATED DB: PDB                                   
REMARK 900 THE X-RAY STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM                
REMARK 900 PSEUDOALTEROMONAS HALOPLANKTIS (CRYSTAL FORM II)                     
DBREF  3LIO A    1   192  UNP    P84612   SODF_PSEHT       1    192             
DBREF  3LIO B    1   192  UNP    P84612   SODF_PSEHT       1    192             
SEQRES   1 A  192  ALA PHE GLU LEU PRO SER LEU PRO TYR ALA ILE ASP ALA          
SEQRES   2 A  192  LEU GLU PRO HIS ILE SER LYS GLU THR LEU GLU PHE HIS          
SEQRES   3 A  192  HIS GLY LYS HIS HIS ASN THR TYR VAL VAL LYS LEU ASN          
SEQRES   4 A  192  GLY LEU ILE PRO GLY THR LYS PHE GLU ASN LYS SER LEU          
SEQRES   5 A  192  GLU GLU ILE VAL CYS SER SER ASP GLY GLY VAL PHE ASN          
SEQRES   6 A  192  ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 A  192  SER LEU SER PRO ASN GLY GLY GLY ALA PRO THR GLY ALA          
SEQRES   8 A  192  VAL ALA ASP ALA ILE ASN ALA LYS TRP GLY SER PHE ASP          
SEQRES   9 A  192  ALA PHE LYS GLU ALA LEU ASN ASP LYS ALA VAL ASN ASN          
SEQRES  10 A  192  PHE GLY SER SER TRP THR TRP LEU VAL LYS LEU ALA ASP          
SEQRES  11 A  192  GLY SER LEU ASP ILE VAL ASN THR SER ASN ALA ALA THR          
SEQRES  12 A  192  PRO LEU THR ASP ASP GLY VAL THR PRO ILE LEU THR VAL          
SEQRES  13 A  192  ASP LEU TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN          
SEQRES  14 A  192  VAL ARG PRO ASP TYR LEU LYS GLY PHE TRP SER LEU VAL          
SEQRES  15 A  192  ASN TRP GLU PHE ALA ASN ALA ASN PHE ALA                      
SEQRES   1 B  192  ALA PHE GLU LEU PRO SER LEU PRO TYR ALA ILE ASP ALA          
SEQRES   2 B  192  LEU GLU PRO HIS ILE SER LYS GLU THR LEU GLU PHE HIS          
SEQRES   3 B  192  HIS GLY LYS HIS HIS ASN THR TYR VAL VAL LYS LEU ASN          
SEQRES   4 B  192  GLY LEU ILE PRO GLY THR LYS PHE GLU ASN LYS SER LEU          
SEQRES   5 B  192  GLU GLU ILE VAL CYS SER SER ASP GLY GLY VAL PHE ASN          
SEQRES   6 B  192  ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 B  192  SER LEU SER PRO ASN GLY GLY GLY ALA PRO THR GLY ALA          
SEQRES   8 B  192  VAL ALA ASP ALA ILE ASN ALA LYS TRP GLY SER PHE ASP          
SEQRES   9 B  192  ALA PHE LYS GLU ALA LEU ASN ASP LYS ALA VAL ASN ASN          
SEQRES  10 B  192  PHE GLY SER SER TRP THR TRP LEU VAL LYS LEU ALA ASP          
SEQRES  11 B  192  GLY SER LEU ASP ILE VAL ASN THR SER ASN ALA ALA THR          
SEQRES  12 B  192  PRO LEU THR ASP ASP GLY VAL THR PRO ILE LEU THR VAL          
SEQRES  13 B  192  ASP LEU TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN          
SEQRES  14 B  192  VAL ARG PRO ASP TYR LEU LYS GLY PHE TRP SER LEU VAL          
SEQRES  15 B  192  ASN TRP GLU PHE ALA ASN ALA ASN PHE ALA                      
HET    TRE  A8000      23                                                       
HET     FE  A5000       1                                                       
HET    TRE  B8001      23                                                       
HET     FE  B5001       1                                                       
HETNAM     TRE TREHALOSE                                                        
HETNAM      FE FE (III) ION                                                     
HETSYN     TRE ALPHA-D-GLUCOPYRANOSYL-ALPHA-D-GLUCOPYRANOSIDE                   
FORMUL   3  TRE    2(C12 H22 O11)                                               
FORMUL   4   FE    2(FE 3+)                                                     
FORMUL   7  HOH   *461(H2 O)                                                    
HELIX    1   1 SER A   19  HIS A   27  1                                   9    
HELIX    2   2 LYS A   29  ILE A   42  1                                  14    
HELIX    3   3 SER A   51  CYS A   57  1                                   7    
HELIX    4   4 ASP A   60  SER A   79  1                                  20    
HELIX    5   5 THR A   89  GLY A  101  1                                  13    
HELIX    6   6 SER A  102  ASN A  116  1                                  15    
HELIX    7   7 THR A  143  ASP A  147  5                                   5    
HELIX    8   8 TRP A  159  ALA A  162  5                                   4    
HELIX    9   9 TYR A  163  ARG A  168  1                                   6    
HELIX   10  10 VAL A  170  VAL A  182  1                                  13    
HELIX   11  11 ASN A  183  ALA A  192  1                                  10    
HELIX   12  12 SER B   19  HIS B   27  1                                   9    
HELIX   13  13 LYS B   29  ILE B   42  1                                  14    
HELIX   14  14 SER B   51  SER B   59  1                                   9    
HELIX   15  15 ASP B   60  SER B   79  1                                  20    
HELIX   16  16 THR B   89  GLY B  101  1                                  13    
HELIX   17  17 SER B  102  ASN B  116  1                                  15    
HELIX   18  18 THR B  143  ASP B  147  5                                   5    
HELIX   19  19 TRP B  159  ALA B  162  5                                   4    
HELIX   20  20 TYR B  163  ARG B  168  1                                   6    
HELIX   21  21 VAL B  170  VAL B  182  1                                  13    
HELIX   22  22 ASN B  183  ALA B  192  1                                  10    
SHEET    1   A 3 LEU A 133  SER A 139  0                                        
SHEET    2   A 3 SER A 121  LYS A 127 -1  N  TRP A 122   O  THR A 138           
SHEET    3   A 3 THR A 151  ASP A 157 -1  O  ILE A 153   N  LEU A 125           
SHEET    1   B 3 LEU B 133  SER B 139  0                                        
SHEET    2   B 3 SER B 121  LYS B 127 -1  N  VAL B 126   O  ASP B 134           
SHEET    3   B 3 THR B 151  ASP B 157 -1  O  ILE B 153   N  LEU B 125           
LINK         OD2 ASP B 157                FE    FE B5001     1555   1555  1.94  
LINK         OD2 ASP A 157                FE    FE A5000     1555   1555  1.96  
LINK         NE2 HIS B 161                FE    FE B5001     1555   1555  2.04  
LINK         NE2 HIS A 161                FE    FE A5000     1555   1555  2.05  
LINK         NE2 HIS B  26                FE    FE B5001     1555   1555  2.07  
LINK         NE2 HIS A  73                FE    FE A5000     1555   1555  2.10  
LINK         NE2 HIS A  26                FE    FE A5000     1555   1555  2.10  
LINK         NE2 HIS B  73                FE    FE B5001     1555   1555  2.13  
LINK        FE    FE B5001                 O   HOH B1054     1555   1555  2.16  
LINK        FE    FE A5000                 O   HOH A1039     1555   1555  2.26  
CISPEP   1 GLU A   15    PRO A   16          0         0.14                     
CISPEP   2 GLU B   15    PRO B   16          0         0.03                     
SITE     1 AC1 15 ASN A 116  ASN A 117  PHE A 118  ASN A 137                    
SITE     2 AC1 15 SER A 139  HOH A1052  HOH A1120  HOH A1169                    
SITE     3 AC1 15 HOH A1170  HOH A1179  HOH A1197  HOH A1205                    
SITE     4 AC1 15 GLY B  61  GLY B  62  HOH B1135                               
SITE     1 AC2  5 HIS A  26  HIS A  73  ASP A 157  HIS A 161                    
SITE     2 AC2  5 HOH A1039                                                     
SITE     1 AC3 17 GLY A  61  GLY A  62  ASN A  65  ASN B 116                    
SITE     2 AC3 17 ASN B 117  PHE B 118  ASN B 137  SER B 139                    
SITE     3 AC3 17 HOH B1003  HOH B1044  HOH B1050  HOH B1051                    
SITE     4 AC3 17 HOH B1052  HOH B1063  HOH B1122  HOH B1146                    
SITE     5 AC3 17 HOH B1189                                                     
SITE     1 AC4  5 HIS B  26  HIS B  73  ASP B 157  HIS B 161                    
SITE     2 AC4  5 HOH B1054                                                     
CRYST1   44.866  103.714   50.242  90.00 108.63  90.00 P 1 21 1      4          
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      0.022289 -0.000001  0.007513        0.00000                         
SCALE2      0.000000  0.009642  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021004        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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