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Database: PDB
Entry: 3LJF
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Original site: 3LJF 
HEADER    OXIDOREDUCTASE                          26-JAN-10   3LJF              
TITLE     THE X-RAY STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM                 
TITLE    2 PSEUDOALTEROMONAS HALOPLANKTIS (CRYSTAL FORM II)                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IRON SUPEROXIDE DISMUTASE;                                 
COMPND   3 CHAIN: A, C, B, D;                                                   
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: SODB, PSHAA1215;                                               
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 3LJF    1       JRNL                                     
REVDAT   1   08-SEP-10 3LJF    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) : 30.00                          
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             : 47141                          
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) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4727                            
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            : 6044                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 532                                     
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 3LJF 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 RCSB057351.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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                         : NULL                               
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   : 51958                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.09200                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 1ISA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF PROTEIN WERE OBTAINED        
REMARK 280  USING 2.3-2.5M AMMONIUM SULPHATE, 10 MM FECL3, 100 MM HEPES PH      
REMARK 280  7.0, 3% (V/V) ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP            
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       51.89250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 1900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 B  5292     O    HOH B  5330              2.13            
REMARK 500   O    HOH B  5411     O    HOH B  5459              2.15            
REMARK 500   O    LYS D    46     O    HOH D  5178              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU C 108   CG    GLU C 108   CD      0.103                       
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    LEU A 110   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    LEU A 154   CA  -  CB  -  CG  ANGL. DEV. =  16.4 DEGREES          
REMARK 500    ASP B  60   CB  -  CG  -  OD1 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    VAL B 182   CB  -  CA  -  C   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    LEU D 154   CA  -  CB  -  CG  ANGL. DEV. =  15.6 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    ASN A 140     -106.02     56.19                                   
REMARK 500    ARG A 168     -124.24     49.31                                   
REMARK 500    LYS C  29      -65.03   -105.62                                   
REMARK 500    PHE C  47      -39.07    -32.17                                   
REMARK 500    SER C  81      143.91   -176.86                                   
REMARK 500    ASN C  83       25.24     49.00                                   
REMARK 500    ASN C 140     -103.13     53.41                                   
REMARK 500    TYR C 163       -3.56   -141.48                                   
REMARK 500    ARG C 168     -125.62     49.46                                   
REMARK 500    LYS B  29      -65.59   -105.07                                   
REMARK 500    ASN B 140     -107.67     60.83                                   
REMARK 500    TYR B 163       -5.79   -141.76                                   
REMARK 500    ARG B 168     -128.61     48.96                                   
REMARK 500    ASN D 140     -109.83     54.31                                   
REMARK 500    ARG D 168     -131.61     51.91                                   
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    PRO C  82        45.9      L          L   OUTSIDE RANGE           
REMARK 500    ASN C  83        24.5      L          L   OUTSIDE RANGE           
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 A5000  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 157   OD2                                                    
REMARK 620 2 HIS A  73   NE2 110.9                                              
REMARK 620 3 HIS A  26   NE2  98.4  91.1                                        
REMARK 620 4 HIS A 161   NE2 124.5 124.1  88.2                                  
REMARK 620 5 HOH A5004   O    79.0  90.5 177.3  92.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D5003  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 157   OD2                                                    
REMARK 620 2 HIS D  73   NE2 110.4                                              
REMARK 620 3 HIS D  26   NE2  87.5 100.2                                        
REMARK 620 4 HIS D 161   NE2 121.3 126.6  94.8                                  
REMARK 620 5 HOH D1699   O    85.0  87.9 170.5  84.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C5002  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 157   OD2                                                    
REMARK 620 2 HIS C 161   NE2 123.4                                              
REMARK 620 3 HIS C  73   NE2 112.5 124.0                                        
REMARK 620 4 HIS C  26   NE2  90.7  87.6  95.8                                  
REMARK 620 5 HOH C5006   O    84.9  95.4  85.3 175.5                            
REMARK 620 N                    1     2     3     4                             
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 116.8                                              
REMARK 620 3 HIS B  73   NE2 120.6 121.5                                        
REMARK 620 4 HIS B  26   NE2  87.8  95.3  97.3                                  
REMARK 620 5 HOH B5005   O    83.5  91.5  84.5 170.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 5000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE A 193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 5002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE C 195                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 5001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE B 194                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 5003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRE D 196                 
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: 3LJ9   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURE OF THE IRON SUPEROXIDE DISMUTASE FROM                
REMARK 900 PSEUDOALTEROMONAS HALOPLANKTIS IN COMPLEX WITH SODIUM AZIDE          
DBREF  3LJF A    1   192  UNP    P84612   SODF_PSEHT       1    192             
DBREF  3LJF C    1   192  UNP    P84612   SODF_PSEHT       1    192             
DBREF  3LJF B    1   192  UNP    P84612   SODF_PSEHT       1    192             
DBREF  3LJF D    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 C  192  ALA PHE GLU LEU PRO SER LEU PRO TYR ALA ILE ASP ALA          
SEQRES   2 C  192  LEU GLU PRO HIS ILE SER LYS GLU THR LEU GLU PHE HIS          
SEQRES   3 C  192  HIS GLY LYS HIS HIS ASN THR TYR VAL VAL LYS LEU ASN          
SEQRES   4 C  192  GLY LEU ILE PRO GLY THR LYS PHE GLU ASN LYS SER LEU          
SEQRES   5 C  192  GLU GLU ILE VAL CYS SER SER ASP GLY GLY VAL PHE ASN          
SEQRES   6 C  192  ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 C  192  SER LEU SER PRO ASN GLY GLY GLY ALA PRO THR GLY ALA          
SEQRES   8 C  192  VAL ALA ASP ALA ILE ASN ALA LYS TRP GLY SER PHE ASP          
SEQRES   9 C  192  ALA PHE LYS GLU ALA LEU ASN ASP LYS ALA VAL ASN ASN          
SEQRES  10 C  192  PHE GLY SER SER TRP THR TRP LEU VAL LYS LEU ALA ASP          
SEQRES  11 C  192  GLY SER LEU ASP ILE VAL ASN THR SER ASN ALA ALA THR          
SEQRES  12 C  192  PRO LEU THR ASP ASP GLY VAL THR PRO ILE LEU THR VAL          
SEQRES  13 C  192  ASP LEU TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN          
SEQRES  14 C  192  VAL ARG PRO ASP TYR LEU LYS GLY PHE TRP SER LEU VAL          
SEQRES  15 C  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                      
SEQRES   1 D  192  ALA PHE GLU LEU PRO SER LEU PRO TYR ALA ILE ASP ALA          
SEQRES   2 D  192  LEU GLU PRO HIS ILE SER LYS GLU THR LEU GLU PHE HIS          
SEQRES   3 D  192  HIS GLY LYS HIS HIS ASN THR TYR VAL VAL LYS LEU ASN          
SEQRES   4 D  192  GLY LEU ILE PRO GLY THR LYS PHE GLU ASN LYS SER LEU          
SEQRES   5 D  192  GLU GLU ILE VAL CYS SER SER ASP GLY GLY VAL PHE ASN          
SEQRES   6 D  192  ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 D  192  SER LEU SER PRO ASN GLY GLY GLY ALA PRO THR GLY ALA          
SEQRES   8 D  192  VAL ALA ASP ALA ILE ASN ALA LYS TRP GLY SER PHE ASP          
SEQRES   9 D  192  ALA PHE LYS GLU ALA LEU ASN ASP LYS ALA VAL ASN ASN          
SEQRES  10 D  192  PHE GLY SER SER TRP THR TRP LEU VAL LYS LEU ALA ASP          
SEQRES  11 D  192  GLY SER LEU ASP ILE VAL ASN THR SER ASN ALA ALA THR          
SEQRES  12 D  192  PRO LEU THR ASP ASP GLY VAL THR PRO ILE LEU THR VAL          
SEQRES  13 D  192  ASP LEU TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN          
SEQRES  14 D  192  VAL ARG PRO ASP TYR LEU LYS GLY PHE TRP SER LEU VAL          
SEQRES  15 D  192  ASN TRP GLU PHE ALA ASN ALA ASN PHE ALA                      
HET     FE  A5000       1                                                       
HET    TRE  A 193      23                                                       
HET     FE  C5002       1                                                       
HET    TRE  C 195      23                                                       
HET     FE  B5001       1                                                       
HET    TRE  B 194      23                                                       
HET     FE  D5003       1                                                       
HET    TRE  D 196      23                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     TRE TREHALOSE                                                        
HETSYN     TRE ALPHA-D-GLUCOPYRANOSYL-ALPHA-D-GLUCOPYRANOSIDE                   
FORMUL   5   FE    4(FE 3+)                                                     
FORMUL   6  TRE    4(C12 H22 O11)                                               
FORMUL  13  HOH   *532(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 THR A   45  ASN A   49  5                                   5    
HELIX    4   4 SER A   51  SER A   59  1                                   9    
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 C   19  HIS C   27  1                                   9    
HELIX   14  14 LYS C   29  ILE C   42  1                                  14    
HELIX   15  15 THR C   45  ASN C   49  5                                   5    
HELIX   16  16 SER C   51  SER C   59  1                                   9    
HELIX   17  17 ASP C   60  SER C   79  1                                  20    
HELIX   18  18 THR C   89  GLY C  101  1                                  13    
HELIX   19  19 SER C  102  ASN C  116  1                                  15    
HELIX   20  20 THR C  143  ASP C  147  5                                   5    
HELIX   21  21 TRP C  159  ALA C  162  5                                   4    
HELIX   22  22 TYR C  163  ARG C  168  1                                   6    
HELIX   23  23 VAL C  170  VAL C  182  1                                  13    
HELIX   24  24 ASN C  183  ALA C  192  1                                  10    
HELIX   25  25 SER B   19  HIS B   27  1                                   9    
HELIX   26  26 LYS B   29  ILE B   42  1                                  14    
HELIX   27  27 THR B   45  LYS B   50  5                                   6    
HELIX   28  28 SER B   51  CYS B   57  1                                   7    
HELIX   29  29 ASP B   60  SER B   79  1                                  20    
HELIX   30  30 THR B   89  GLY B  101  1                                  13    
HELIX   31  31 SER B  102  ASN B  116  1                                  15    
HELIX   32  32 THR B  143  ASP B  147  5                                   5    
HELIX   33  33 TRP B  159  ALA B  162  5                                   4    
HELIX   34  34 TYR B  163  ARG B  168  1                                   6    
HELIX   35  35 VAL B  170  VAL B  182  1                                  13    
HELIX   36  36 ASN B  183  ALA B  192  1                                  10    
HELIX   37  37 SER D   19  HIS D   27  1                                   9    
HELIX   38  38 LYS D   29  ILE D   42  1                                  14    
HELIX   39  39 THR D   45  LYS D   50  5                                   6    
HELIX   40  40 SER D   51  SER D   58  1                                   8    
HELIX   41  41 ASP D   60  SER D   79  1                                  20    
HELIX   42  42 THR D   89  GLY D  101  1                                  13    
HELIX   43  43 SER D  102  ASN D  116  1                                  15    
HELIX   44  44 THR D  143  ASP D  147  5                                   5    
HELIX   45  45 TRP D  159  ALA D  162  5                                   4    
HELIX   46  46 TYR D  163  ARG D  168  1                                   6    
HELIX   47  47 VAL D  170  VAL D  182  1                                  13    
HELIX   48  48 ASN D  183  ALA D  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 124   O  VAL A 136           
SHEET    3   A 3 THR A 151  ASP A 157 -1  O  THR A 151   N  LYS A 127           
SHEET    1   B 3 LEU C 133  SER C 139  0                                        
SHEET    2   B 3 SER C 121  LYS C 127 -1  N  TRP C 124   O  VAL C 136           
SHEET    3   B 3 THR C 151  ASP C 157 -1  O  THR C 151   N  LYS C 127           
SHEET    1   C 3 LEU B 133  SER B 139  0                                        
SHEET    2   C 3 SER B 121  LYS B 127 -1  N  TRP B 124   O  VAL B 136           
SHEET    3   C 3 THR B 151  ASP B 157 -1  O  THR B 151   N  LYS B 127           
SHEET    1   D 3 LEU D 133  SER D 139  0                                        
SHEET    2   D 3 SER D 121  LYS D 127 -1  N  TRP D 124   O  VAL D 136           
SHEET    3   D 3 THR D 151  ASP D 157 -1  O  THR D 151   N  LYS D 127           
LINK         OD2 ASP A 157                FE    FE A5000     1555   1555  1.87  
LINK         OD2 ASP D 157                FE    FE D5003     1555   1555  1.95  
LINK         OD2 ASP C 157                FE    FE C5002     1555   1555  1.96  
LINK         NE2 HIS A  73                FE    FE A5000     1555   1555  2.01  
LINK         OD2 ASP B 157                FE    FE B5001     1555   1555  2.02  
LINK         NE2 HIS C 161                FE    FE C5002     1555   1555  2.02  
LINK         NE2 HIS B 161                FE    FE B5001     1555   1555  2.03  
LINK         NE2 HIS A  26                FE    FE A5000     1555   1555  2.06  
LINK         NE2 HIS C  73                FE    FE C5002     1555   1555  2.06  
LINK         NE2 HIS D  73                FE    FE D5003     1555   1555  2.08  
LINK         NE2 HIS D  26                FE    FE D5003     1555   1555  2.12  
LINK         NE2 HIS B  73                FE    FE B5001     1555   1555  2.13  
LINK         NE2 HIS D 161                FE    FE D5003     1555   1555  2.14  
LINK         NE2 HIS B  26                FE    FE B5001     1555   1555  2.17  
LINK         NE2 HIS C  26                FE    FE C5002     1555   1555  2.18  
LINK         NE2 HIS A 161                FE    FE A5000     1555   1555  2.21  
LINK        FE    FE B5001                 O   HOH B5005     1555   1555  2.08  
LINK        FE    FE D5003                 O   HOH D1699     1555   1555  2.19  
LINK        FE    FE A5000                 O   HOH A5004     1555   1555  2.20  
LINK        FE    FE C5002                 O   HOH C5006     1555   1555  2.39  
CISPEP   1 GLU A   15    PRO A   16          0        -0.52                     
CISPEP   2 GLU C   15    PRO C   16          0        -0.84                     
CISPEP   3 GLU B   15    PRO B   16          0         0.72                     
CISPEP   4 GLU D   15    PRO D   16          0        -0.31                     
SITE     1 AC1  5 HIS A  26  HIS A  73  ASP A 157  HIS A 161                    
SITE     2 AC1  5 HOH A5004                                                     
SITE     1 AC2 12 ASN A 116  ASN A 117  PHE A 118  ASN A 137                    
SITE     2 AC2 12 SER A 139  HOH A5130  HOH A5179  HOH A5340                    
SITE     3 AC2 12 HOH A5376  GLY B  61  GLY B  62  HOH B5366                    
SITE     1 AC3  5 HIS C  26  HIS C  73  ASP C 157  HIS C 161                    
SITE     2 AC3  5 HOH C5006                                                     
SITE     1 AC4 10 ASN C 116  ASN C 117  PHE C 118  ASN C 137                    
SITE     2 AC4 10 SER C 139  HOH C1720  HOH C1727  HOH C5191                    
SITE     3 AC4 10 GLY D  61  GLY D  62                                          
SITE     1 AC5  5 HIS B  26  HIS B  73  ASP B 157  HIS B 161                    
SITE     2 AC5  5 HOH B5005                                                     
SITE     1 AC6 13 GLY A  61  GLY A  62  LYS B 113  ASN B 116                    
SITE     2 AC6 13 ASN B 117  PHE B 118  ASN B 137  HOH B1736                    
SITE     3 AC6 13 HOH B5180  HOH B5252  HOH B5269  HOH B5337                    
SITE     4 AC6 13 HOH B5379                                                     
SITE     1 AC7  5 HIS D  26  HIS D  73  ASP D 157  HIS D 161                    
SITE     2 AC7  5 HOH D1699                                                     
SITE     1 AC8 14 GLY C  61  GLY C  62  ASN C  65  LYS D 113                    
SITE     2 AC8 14 ASN D 116  ASN D 117  PHE D 118  ASN D 137                    
SITE     3 AC8 14 HOH D1723  HOH D1745  HOH D5314  HOH D5394                    
SITE     4 AC8 14 HOH D5408  HOH D5414                                          
CRYST1   50.476  103.785   90.251  90.00 103.81  90.00 P 1 21 1      8          
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      0.019811  0.000000  0.004870        0.00000                         
SCALE2      0.000000  0.009635  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011410        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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