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Database: PDB
Entry: 3LJ9
LinkDB: 3LJ9
Original site: 3LJ9 
HEADER    OXIDOREDUCTASE                          26-JAN-10   3LJ9              
TITLE     X-RAY STRUCTURE OF THE IRON SUPEROXIDE DISMUTASE FROM                 
TITLE    2 PSEUDOALTEROMONAS HALOPLANKTIS IN COMPLEX WITH SODIUM AZIDE          
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 3LJ9    1       JRNL                                     
REVDAT   1   08-SEP-10 3LJ9    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 PSEUDOALTEROMONAS HALOPLANKTIS                               
REMARK   1  REF    PROTEIN AND PEPTIDE LETTERS   V.  15   415 2008              
REMARK   1  REFN                   ISSN 0929-8665                               
REMARK   1  PMID   18473957                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.44                          
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 19907                          
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) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2121                            
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          : 54                                      
REMARK   3   SOLVENT ATOMS            : 169                                     
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 3LJ9 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 RCSB057345.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-NOV-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24002                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.070                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.440                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.11700                            
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: 3LIO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULPHATE, 1.0M SODIUM      
REMARK 280  CHLORIDE, 0.1M HEPES PH 7.5. THE AZIDE COMPLEX WAS PREPARED BY      
REMARK 280  SOAKING OVERNIGHT IN 2.5M AMMONIUM SULPHATE, 0.1M TRIS/HCL PH       
REMARK 280  7.0., VAPOR DIFFUSION, HANGING DROP, 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       51.76350            
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: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  6175     O    HOH B  6192              2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    PRO B 172   C   -  N   -  CA  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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  29      -65.61   -102.87                                   
REMARK 500    PHE A  47        3.84    -62.79                                   
REMARK 500    SER A  58       26.65   -145.26                                   
REMARK 500    ASN A 140     -105.03     57.27                                   
REMARK 500    ARG A 168     -123.61     43.83                                   
REMARK 500    VAL A 182      121.09    -28.17                                   
REMARK 500    LYS B  46       16.24    -64.20                                   
REMARK 500    GLU B  48      -43.66    -28.98                                   
REMARK 500    ASP B 130        0.19    -69.51                                   
REMARK 500    ASN B 140     -111.08     58.61                                   
REMARK 500    TYR B 163      -11.70   -141.53                                   
REMARK 500    ARG B 168     -128.63     58.62                                   
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 B 204  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 157   OD2                                                    
REMARK 620 2 HIS B  73   NE2 100.8                                              
REMARK 620 3 HIS B  26   NE2  90.3  88.1                                        
REMARK 620 4 HIS B 161   NE2 108.8 150.1  95.2                                  
REMARK 620 5 AZI B 200   N1  174.2  78.9  95.4  71.2                            
REMARK 620 6 HOH B6195   O    88.1  91.8 178.4  85.7  86.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 203  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 AZI A 201   N1                                                     
REMARK 620 2 ASP A 157   OD2 173.7                                              
REMARK 620 3 HIS A  26   NE2  90.2  89.6                                        
REMARK 620 4 HIS A  73   NE2  75.6  98.2  97.4                                  
REMARK 620 5 HIS A 161   NE2  71.3 115.0  93.9 144.9                            
REMARK 620 6 AZI A 201   N2   20.4 153.9  80.4  59.7  89.9                      
REMARK 620 7 HOH A6181   O    93.6  86.6 176.2  83.3  87.6 103.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE A 1151                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI B 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE B 1152                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LIO   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURE OF THE IRON SUPEROXIDE DISMUTASE FROM                
REMARK 900 PSEUDOALTEROMONAS HALOPLANKTIS (CRYSTAL FORM I)                      
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  3LJ9 A    1   192  UNP    P84612   SODF_PSEHT       1    192             
DBREF  3LJ9 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    AZI  A 201       3                                                       
HET     FE  A 203       1                                                       
HET    TRE  A1151      23                                                       
HET    AZI  B 200       3                                                       
HET     FE  B 204       1                                                       
HET    TRE  B1152      23                                                       
HETNAM     AZI AZIDE ION                                                        
HETNAM      FE FE (III) ION                                                     
HETNAM     TRE TREHALOSE                                                        
HETSYN     TRE ALPHA-D-GLUCOPYRANOSYL-ALPHA-D-GLUCOPYRANOSIDE                   
FORMUL   3  AZI    2(N3 1-)                                                     
FORMUL   4   FE    2(FE 3+)                                                     
FORMUL   5  TRE    2(C12 H22 O11)                                               
FORMUL   9  HOH   *169(H2 O)                                                    
HELIX    1   1 SER A   19  HIS A   27  1                                   9    
HELIX    2   2 LYS A   29  GLY A   40  1                                  12    
HELIX    3   3 THR A   45  LYS A   50  5                                   6    
HELIX    4   4 SER A   51  CYS A   57  1                                   7    
HELIX    5   5 ASP A   60  SER A   79  1                                  20    
HELIX    6   6 THR A   89  GLY A  101  1                                  13    
HELIX    7   7 SER A  102  ASN A  116  1                                  15    
HELIX    8   8 THR A  143  ASP A  147  5                                   5    
HELIX    9   9 TRP A  159  ALA A  162  5                                   4    
HELIX   10  10 TYR A  163  ARG A  168  1                                   6    
HELIX   11  11 VAL A  170  VAL A  182  1                                  13    
HELIX   12  12 ASN A  183  ALA A  192  1                                  10    
HELIX   13  13 SER B   19  HIS B   27  1                                   9    
HELIX   14  14 LYS B   29  ILE B   42  1                                  14    
HELIX   15  15 SER B   51  SER B   59  1                                   9    
HELIX   16  16 ASP B   60  SER B   79  1                                  20    
HELIX   17  17 THR B   89  GLY B  101  1                                  13    
HELIX   18  18 SER B  102  ASN B  116  1                                  15    
HELIX   19  19 THR B  143  ASP B  147  5                                   5    
HELIX   20  20 TRP B  159  ALA B  162  5                                   4    
HELIX   21  21 TYR B  163  ARG B  168  1                                   6    
HELIX   22  22 VAL B  170  VAL B  182  1                                  13    
HELIX   23  23 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  THR A 151   N  LYS A 127           
SHEET    1   B 3 LEU B 133  SER B 139  0                                        
SHEET    2   B 3 SER B 121  LYS B 127 -1  N  TRP B 124   O  VAL B 136           
SHEET    3   B 3 THR B 151  ASP B 157 -1  O  THR B 151   N  LYS B 127           
LINK         OD2 ASP B 157                FE    FE B 204     1555   1555  1.96  
LINK         N1  AZI A 201                FE    FE A 203     1555   1555  2.00  
LINK         OD2 ASP A 157                FE    FE A 203     1555   1555  2.05  
LINK         NE2 HIS B  73                FE    FE B 204     1555   1555  2.06  
LINK         NE2 HIS B  26                FE    FE B 204     1555   1555  2.14  
LINK         NE2 HIS A  26                FE    FE A 203     1555   1555  2.14  
LINK         NE2 HIS A  73                FE    FE A 203     1555   1555  2.18  
LINK         NE2 HIS A 161                FE    FE A 203     1555   1555  2.21  
LINK         NE2 HIS B 161                FE    FE B 204     1555   1555  2.23  
LINK         N1  AZI B 200                FE    FE B 204     1555   1555  2.53  
LINK         N2  AZI A 201                FE    FE A 203     1555   1555  2.75  
LINK        FE    FE A 203                 O   HOH A6181     1555   1555  2.29  
LINK        FE    FE B 204                 O   HOH B6195     1555   1555  2.30  
CISPEP   1 GLU A   15    PRO A   16          0        -0.61                     
CISPEP   2 GLU B   15    PRO B   16          0        -0.19                     
SITE     1 AC1  7 HIS A  26  HIS A  30  HIS A  31  TYR A  34                    
SITE     2 AC1  7 HIS A  73  HIS A 161   FE A 203                               
SITE     1 AC2  6 HIS A  26  HIS A  73  ASP A 157  HIS A 161                    
SITE     2 AC2  6 AZI A 201  HOH A6181                                          
SITE     1 AC3 10 ASN A 116  ASN A 117  PHE A 118  ASN A 137                    
SITE     2 AC3 10 SER A 139  HOH A6125  HOH A6164  GLY B  61                    
SITE     3 AC3 10 GLY B  62  ASN B  65                                          
SITE     1 AC4  7 HIS B  26  HIS B  30  HIS B  31  TYR B  34                    
SITE     2 AC4  7 HIS B  73  HIS B 161   FE B 204                               
SITE     1 AC5  6 HIS B  26  HIS B  73  ASP B 157  HIS B 161                    
SITE     2 AC5  6 AZI B 200  HOH B6195                                          
SITE     1 AC6  8 GLY A  61  GLY A  62  ASN B 116  ASN B 117                    
SITE     2 AC6  8 PHE B 118  ASN B 137  HOH B6064  HOH B6142                    
CRYST1   46.134  103.527   50.586  90.00 108.29  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      0.021676  0.000000  0.007164        0.00000                         
SCALE2      0.000000  0.009659  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020820        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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