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Database: PDB
Entry: 3SDP
LinkDB: 3SDP
Original site: 3SDP 
HEADER    OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)    06-MAY-91   3SDP              
TITLE     THE 2.1 ANGSTROMS RESOLUTION STRUCTURE OF IRON SUPEROXIDE             
TITLE    2 DISMUTASE FROM PSEUDOMONAS OVALIS                                    
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: PSEUDOMONAS PUTIDA;                             
SOURCE   3 ORGANISM_TAXID: 303                                                  
KEYWDS    OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.L.STODDARD,D.RINGE,G.A.PETSKO                                       
REVDAT   3   24-FEB-09 3SDP    1       VERSN                                    
REVDAT   2   01-APR-03 3SDP    1       JRNL                                     
REVDAT   1   15-APR-93 3SDP    0                                                
JRNL        AUTH   B.L.STODDARD,P.L.HOWELL,D.RINGE,G.A.PETSKO                   
JRNL        TITL   THE 2.1-A RESOLUTION STRUCTURE OF IRON SUPEROXIDE            
JRNL        TITL 2 DISMUTASE FROM PSEUDOMONAS OVALIS.                           
JRNL        REF    BIOCHEMISTRY                  V.  29  8885 1990              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   2271564                                                      
JRNL        DOI    10.1021/BI00490A002                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.L.STODDARD,D.RINGE,G.A.PETSKO                              
REMARK   1  TITL   THE STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM              
REMARK   1  TITL 2 PSEUDOMONAS OVALIS BOUND TO THE INHIBITOR AZIDE:             
REMARK   1  TITL 3 COORDINATION CHANGES AND DYNAMICS DURING CATALYSIS           
REMARK   1  REF    PROTEIN ENG.                  V.   4   113 1990              
REMARK   1  REFN                   ISSN 0269-2139                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ, X-PLOR                                       
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2910                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 180                                     
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.033 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3SDP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       24.55000            
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: 1990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 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     ALA A     1                                                      
REMARK 465     PHE A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     LYS A   191                                                      
REMARK 465     THR A   192                                                      
REMARK 465     PHE A   193                                                      
REMARK 465     LYS A   194                                                      
REMARK 465     ALA A   195                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     PHE B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     LYS B   191                                                      
REMARK 465     THR B   192                                                      
REMARK 465     PHE B   193                                                      
REMARK 465     LYS B   194                                                      
REMARK 465     ALA B   195                                                      
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 B 704        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH B 709        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH B 710        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A 615        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH A 617        DISTANCE =  7.71 ANGSTROMS                       
REMARK 525    HOH A 621        DISTANCE =  7.77 ANGSTROMS                       
REMARK 525    HOH B 721        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH B 722        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH A 624        DISTANCE =  7.02 ANGSTROMS                       
REMARK 525    HOH B 725        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH A 627        DISTANCE =  7.00 ANGSTROMS                       
REMARK 525    HOH A 628        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH B 732        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH B 735        DISTANCE =  7.85 ANGSTROMS                       
REMARK 525    HOH A 635        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH B 737        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH B 739        DISTANCE =  7.17 ANGSTROMS                       
REMARK 525    HOH B 740        DISTANCE =  8.14 ANGSTROMS                       
REMARK 525    HOH B 741        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH B 742        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 642        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A 643        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH A 645        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH A 647        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH B 749        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH B 750        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH A 652        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH A 656        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH A 657        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH A 661        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A 662        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH B 765        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH A 667        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH B 775        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH A 689        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH A 690        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH A 692        DISTANCE =  7.48 ANGSTROMS                       
REMARK 525    HOH A 693        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH A 703        DISTANCE =  5.26 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 A 196  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  74   NE2  99.6                                              
REMARK 620 3 ASP A 156   OD2  97.8 120.0                                        
REMARK 620 4 HIS A 160   NE2  93.7 128.1 107.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 196  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  74   NE2                                                    
REMARK 620 2 HIS B 160   NE2 136.3                                              
REMARK 620 3 ASP B 156   OD2 102.7 105.7                                        
REMARK 620 4 HIS B  26   NE2 104.3  90.7 118.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: FEA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: FEB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 196                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 196                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 RESIDUE 85 OF EACH CHAIN IS IDENTIFIED AS ALA IN THIS                
REMARK 999 ENTRY.  NOTE THAT THIS RESIDUE IS IDENTIFIED AS GLY IN               
REMARK 999 SWISSPROT ENTRY SODF_PSEOV.                                          
DBREF  3SDP A    1   195  UNP    P09223   SODF_PSEPU       1    195             
DBREF  3SDP B    1   195  UNP    P09223   SODF_PSEPU       1    195             
SEQADV 3SDP ALA A   85  UNP  P09223    GLY    85 CONFLICT                       
SEQADV 3SDP ALA B   85  UNP  P09223    GLY    85 CONFLICT                       
SEQRES   1 A  195  ALA PHE GLU LEU PRO PRO LEU PRO TYR ALA HIS ASP ALA          
SEQRES   2 A  195  LEU GLN PRO HIS ILE SER LYS GLU THR LEU GLU TYR HIS          
SEQRES   3 A  195  HIS ASP LYS HIS HIS ASN THR TYR VAL VAL ASN LEU ASN          
SEQRES   4 A  195  ASN LEU VAL PRO GLY THR PRO GLU PHE GLU GLY LYS THR          
SEQRES   5 A  195  LEU GLU GLU ILE VAL LYS SER SER SER GLY GLY ILE PHE          
SEQRES   6 A  195  ASN ASN ALA ALA GLN VAL TRP ASN HIS THR PHE TYR TRP          
SEQRES   7 A  195  ASN CYS LEU SER PRO ASP ALA GLY GLY GLN PRO THR GLY          
SEQRES   8 A  195  ALA LEU ALA ASP ALA ILE ASN ALA ALA PHE GLY SER PHE          
SEQRES   9 A  195  ASP LYS PHE LYS GLU GLU PHE THR LYS THR SER VAL GLY          
SEQRES  10 A  195  THR PHE GLY SER GLY TRP ALA TRP LEU VAL LYS ALA ASP          
SEQRES  11 A  195  GLY SER LEU ALA LEU CYS SER THR ILE GLY ALA GLY ALA          
SEQRES  12 A  195  PRO LEU THR SER GLY ASP THR PRO LEU LEU THR CYS ASP          
SEQRES  13 A  195  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN LEU          
SEQRES  14 A  195  ARG PRO LYS TYR VAL GLU ALA PHE TRP ASN LEU VAL ASN          
SEQRES  15 A  195  TRP ALA PHE VAL ALA GLU GLU GLY LYS THR PHE LYS ALA          
SEQRES   1 B  195  ALA PHE GLU LEU PRO PRO LEU PRO TYR ALA HIS ASP ALA          
SEQRES   2 B  195  LEU GLN PRO HIS ILE SER LYS GLU THR LEU GLU TYR HIS          
SEQRES   3 B  195  HIS ASP LYS HIS HIS ASN THR TYR VAL VAL ASN LEU ASN          
SEQRES   4 B  195  ASN LEU VAL PRO GLY THR PRO GLU PHE GLU GLY LYS THR          
SEQRES   5 B  195  LEU GLU GLU ILE VAL LYS SER SER SER GLY GLY ILE PHE          
SEQRES   6 B  195  ASN ASN ALA ALA GLN VAL TRP ASN HIS THR PHE TYR TRP          
SEQRES   7 B  195  ASN CYS LEU SER PRO ASP ALA GLY GLY GLN PRO THR GLY          
SEQRES   8 B  195  ALA LEU ALA ASP ALA ILE ASN ALA ALA PHE GLY SER PHE          
SEQRES   9 B  195  ASP LYS PHE LYS GLU GLU PHE THR LYS THR SER VAL GLY          
SEQRES  10 B  195  THR PHE GLY SER GLY TRP ALA TRP LEU VAL LYS ALA ASP          
SEQRES  11 B  195  GLY SER LEU ALA LEU CYS SER THR ILE GLY ALA GLY ALA          
SEQRES  12 B  195  PRO LEU THR SER GLY ASP THR PRO LEU LEU THR CYS ASP          
SEQRES  13 B  195  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN LEU          
SEQRES  14 B  195  ARG PRO LYS TYR VAL GLU ALA PHE TRP ASN LEU VAL ASN          
SEQRES  15 B  195  TRP ALA PHE VAL ALA GLU GLU GLY LYS THR PHE LYS ALA          
HET     FE  A 196       1                                                       
HET     FE  B 196       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   5  HOH   *180(H2 O)                                                    
HELIX    1  AA LYS A   20  ASN A   40  1HIS 26 IS A LIGAND TO FE          21    
HELIX    2  BA ILE A   64  ASN A   79  1HIS 74 IS A LIGAND TO FE          16    
HELIX    3  CA GLY A   91  PHE A  101  1                                  11    
HELIX    4  DA SER A  103  THR A  112  1                                  10    
HELIX    5  EA ARG A  167  ASN A  179  1                                  13    
HELIX    6  FA TRP A  183  GLY A  190  1                                   8    
HELIX    7  AB LYS B   20  ASN B   40  1HIS 26 IS A LIGAND TO FE          21    
HELIX    8  BB ILE B   64  ASN B   79  1HIS 74 IS A LIGAND TO FE          16    
HELIX    9  CB GLY B   91  PHE B  101  1                                  11    
HELIX   10  DB SER B  103  THR B  112  1                                  10    
HELIX   11  EB ARG B  167  ASN B  179  1                                  13    
HELIX   12  FB TRP B  183  GLY B  190  1                                   8    
SHEET    1  AA 3 SER A 132  ILE A 139  0                                        
SHEET    2  AA 3 TRP A 123  ASP A 130 -1  N  VAL A 127   O  LEU A 133           
SHEET    3  AA 3 ASP A 149  VAL A 157 -1  N  THR A 150   O  LYS A 128           
SHEET    1  AB 3 SER B 132  ILE B 139  0                                        
SHEET    2  AB 3 TRP B 123  ASP B 130 -1  N  VAL B 127   O  LEU B 133           
SHEET    3  AB 3 ASP B 149  VAL B 157 -1  N  THR B 150   O  LYS B 128           
LINK        FE    FE A 196                 NE2 HIS A  26     1555   1555  2.57  
LINK        FE    FE A 196                 NE2 HIS A  74     1555   1555  2.29  
LINK        FE    FE A 196                 OD2 ASP A 156     1555   1555  2.37  
LINK        FE    FE A 196                 NE2 HIS A 160     1555   1555  2.39  
LINK        FE    FE B 196                 NE2 HIS B  74     1555   1555  2.30  
LINK        FE    FE B 196                 NE2 HIS B 160     1555   1555  2.58  
LINK        FE    FE B 196                 OD2 ASP B 156     1555   1555  2.25  
LINK        FE    FE B 196                 NE2 HIS B  26     1555   1555  2.58  
SITE     1 FEA  5 HIS A  26  HIS A  74  ASP A 156  HIS A 160                    
SITE     2 FEA  5  FE A 196                                                     
SITE     1 FEB  5 HIS B  26  HIS B  74  ASP B 156  HIS B 160                    
SITE     2 FEB  5  FE B 196                                                     
SITE     1 AC1  4 HIS A  26  HIS A  74  ASP A 156  HIS A 160                    
SITE     1 AC2  4 HIS B  26  HIS B  74  ASP B 156  HIS B 160                    
CRYST1   81.900   49.100   61.700  90.00 106.80  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      0.012210  0.000000  0.003686        0.00000                         
SCALE2      0.000000  0.020367  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016930        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system