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Database: PDB
Entry: 1QNN
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HEADER    OXIDOREDUCTASE                          20-OCT-99   1QNN              
TITLE     CAMBIALISTIC SUPEROXIDE DISMUTASE FROM PORPHYROMONAS                  
TITLE    2 GINGIVALIS                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: FE/MN-SOD;                                                  
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: EACH CHAIN CONTAINS ONE METAL ION                     
COMPND   8  (FE3+\:MN3+=3\:1).;                                                 
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 SYNONYM: FE/MN-SOD;                                                  
COMPND  13 EC: 1.15.1.1;                                                        
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 OTHER_DETAILS: EACH CHAIN CONTAINS ONE METAL ION                     
COMPND  16  (FE3+\:MN3+=3\:1).                                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PORPHYROMONAS GINGIVALIS;                       
SOURCE   3 ORGANISM_TAXID: 837;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_CELL_LINE: QC774;                                  
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PKD210;                                   
SOURCE   8 EXPRESSION_SYSTEM_GENE: SOD;                                         
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: PORPHYROMONAS GINGIVALIS;                       
SOURCE  11 ORGANISM_TAXID: 837;                                                 
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_CELL_LINE: QC774;                                  
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PKD210;                                   
SOURCE  16 EXPRESSION_SYSTEM_GENE: SOD                                          
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SUGIO,B.Y.HIRAOKA,F.YAMAKURA                                        
REVDAT   2   24-FEB-09 1QNN    1       VERSN                                    
REVDAT   1   21-JUN-00 1QNN    0                                                
JRNL        AUTH   S.SUGIO,B.Y.HIRAOKA,F.YAMAKURA                               
JRNL        TITL   CRYSTAL STRUCTURE OF CAMBIALISTIC SUPEROXIDE                 
JRNL        TITL 2 DISMUTASE FROM PORPHYROMONAS GINGIVALIS                      
JRNL        REF    EUR.J.BIOCHEM.                V. 267  3487 2000              
JRNL        REFN                   ISSN 0014-2956                               
JRNL        PMID   10848964                                                     
JRNL        DOI    10.1046/J.1432-1327.2000.01373.X                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   F.YAMAKURA,R.L.RARDIN,G.A.PETSKO,D.RINGE,                    
REMARK   1  AUTH 2 B.Y.HIRAOKA,K.NAKAYAMA,T.FUJIMURA,H.TAKA,K.MURAYAMA          
REMARK   1  TITL   INACTIVATION AND DESTRUCTION OF CONSERVED TRP159             
REMARK   1  TITL 2 OF FE-SUPEROXIDE DISMUTASE FROM PORPHYROMONAS                
REMARK   1  TITL 3 GINGIVALIS BY HYDROGEN PEROXIDE                              
REMARK   1  REF    EUR.J.BIOCHEM.                V. 253    49 1998              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1  PMID   9578460                                                      
REMARK   1  DOI    10.1046/J.1432-1327.1998.2530049.X                           
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.AMANO,S.SHIZUKUISHI,A.TSUNEMITSU,K.MAEKAWA,                
REMARK   1  AUTH 2 S.TSUNEMITSU                                                 
REMARK   1  TITL   THE PRIMARY STRUCTURE OF SUPEROXIDE DISMUTASE                
REMARK   1  TITL 2 PURIFIED FROM ANAEROBICALLY MAINTAINED BACTEROIDES           
REMARK   1  TITL 3 GINGIVALIS                                                   
REMARK   1  REF    FEBS LETT.                    V. 272   217 1990              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1  PMID   2226833                                                      
REMARK   1  DOI    10.1016/0014-5793(90)80488-5                                 
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   A.AMANO,S.SHIZUKUISHI,H.TAMAGAWA,K.IWAKURA,                  
REMARK   1  AUTH 2 S.TSUNASAWA,S.TSUNEMITSU                                     
REMARK   1  TITL   CHARACTERIZATION OF SUPEROXIDE DISMUTASE PURIFIED            
REMARK   1  TITL 2 FROM EITHER ANAEROBICALLY MAINTAINED OR AERATED              
REMARK   1  TITL 3 BACTEROIDES GINGIVALIS                                       
REMARK   1  REF    J.BACTERIOL.                  V. 172  1457 1990              
REMARK   1  REFN                   ISSN 0021-9193                               
REMARK   1  PMID   2307656                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.8  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.0                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.001                          
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 63443                          
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) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1927                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.88                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.4                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5976                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.306                        
REMARK   3   BIN FREE R VALUE                    : 0.360                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.3                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 207                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6157                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 436                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.1                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.4                           
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) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.22                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.9                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.67                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.999 ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.572 ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.573 ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.337 ; 2.50                 
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : EXTRA.PAR                                      
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : EXTRA.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: A RESOLUTION-DEPENDENT WEIGHTS AND        
REMARK   3  BULK SOLVENT CORRECTION WERE APPLIED                                
REMARK   4                                                                      
REMARK   4 1QNN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-OCT-99.                  
REMARK 100 THE PDBE ID CODE IS EBI-4187.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-AUG-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 5.80                               
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/MSC RU-H2R                  
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : YALE MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROCESS                            
REMARK 200  DATA SCALING SOFTWARE          : PROCESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64134                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY                : 5.640                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: PDB ENTRY 1ISA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 46                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS:                                          
REMARK 280 SOLUTION CONTAINING 6-9MG/ML PROTEIN AND 10MM TRIS/HCL               
REMARK 280 (PH7.8) WERE USED FOR CRYSTALLIZATION.  CRYSTALS WERE                
REMARK 280 GROWN FROM HANGING DROPS SUSPENDED OVER A RESERVOIR                  
REMARK 280 SOLUTION CONTAINING 100MM POTASSIUM PHOSPHATE (PH5.8)                
REMARK 280 AND 26-31% PEG4000 AT 293K WITHIN A FEW WEEKS.                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       37.73500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.79500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.33000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.79500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.73500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.33000            
REMARK 290   SMTRY3   4  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 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 5020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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     MET D     1                                                      
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 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 141     -109.09     54.48                                   
REMARK 500    GLN A 168     -122.78     54.32                                   
REMARK 500    PRO B   9       23.96    -78.52                                   
REMARK 500    LYS B  99      -74.72    -64.22                                   
REMARK 500    ASN B 141     -104.36     51.91                                   
REMARK 500    TYR B 163       -8.06   -140.56                                   
REMARK 500    GLN B 168     -128.10     53.00                                   
REMARK 500    ASN C 141     -114.07     55.30                                   
REMARK 500    TYR C 163       -7.09   -142.92                                   
REMARK 500    GLN C 168     -119.35     55.34                                   
REMARK 500    ILE D   6      153.32    -46.17                                   
REMARK 500    LYS D  30      -56.15   -122.64                                   
REMARK 500    ASN D 141     -106.48     50.63                                   
REMARK 500    TYR D 163      -11.60   -141.41                                   
REMARK 500    GLN D 168     -119.27     50.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 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 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 161   NE2                                                    
REMARK 620 2 ASP A 157   OD2 111.6                                              
REMARK 620 3 HOH A2085   O    92.2  86.6                                        
REMARK 620 4 HIS A  27   NE2  93.2  94.1 173.8                                  
REMARK 620 5 HIS A  74   NE2 134.4 114.0  89.8  84.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  74   NE2                                                    
REMARK 620 2 HOH B2088   O    91.9                                              
REMARK 620 3 HIS B  27   NE2  86.5 178.4                                        
REMARK 620 4 ASP B 157   OD2 109.7  92.6  88.0                                  
REMARK 620 5 HIS B 161   NE2 133.6  90.8  90.3 116.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 161   NE2                                                    
REMARK 620 2 HIS C  74   NE2 130.1                                              
REMARK 620 3 ASP C 157   OD2 117.2 112.5                                        
REMARK 620 4 HOH C2117   O    87.0  98.1  88.8                                  
REMARK 620 5 HIS C  27   NE2  93.3  84.3  87.9 176.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  27   NE2                                                    
REMARK 620 2 ASP D 157   OD2  84.7                                              
REMARK 620 3 HIS D  74   NE2  88.0 104.6                                        
REMARK 620 4 HOH D2056   O   171.6  89.0  88.2                                  
REMARK 620 5 HIS D 161   NE2  95.7 117.3 138.1  92.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE D 201                 
DBREF  1QNN A    1   191  UNP    P19665   SODF_PORGI       1    191             
DBREF  1QNN B    1   191  UNP    P19665   SODF_PORGI       1    191             
DBREF  1QNN C    1   191  UNP    P19665   SODF_PORGI       1    191             
DBREF  1QNN D    1   191  UNP    P19665   SODF_PORGI       1    191             
SEQRES   1 A  191  MET THR HIS GLU LEU ILE SER LEU PRO TYR ALA VAL ASP          
SEQRES   2 A  191  ALA LEU ALA PRO VAL ILE SER LYS GLU THR VAL GLU PHE          
SEQRES   3 A  191  HIS HIS GLY LYS HIS LEU LYS THR TYR VAL ASP ASN LEU          
SEQRES   4 A  191  ASN LYS LEU ILE ILE GLY THR GLU PHE GLU ASN ALA ASP          
SEQRES   5 A  191  LEU ASN THR ILE VAL GLN LYS SER GLU GLY GLY ILE PHE          
SEQRES   6 A  191  ASN ASN ALA GLY GLN THR LEU ASN HIS ASN LEU TYR PHE          
SEQRES   7 A  191  THR GLN PHE ARG PRO GLY LYS GLY GLY ALA PRO LYS GLY          
SEQRES   8 A  191  LYS LEU GLY GLU ALA ILE ASP LYS GLN PHE GLY SER PHE          
SEQRES   9 A  191  GLU LYS PHE LYS GLU GLU PHE ASN THR ALA GLY THR THR          
SEQRES  10 A  191  LEU PHE GLY SER GLY TRP VAL TRP LEU ALA SER ASP ALA          
SEQRES  11 A  191  ASN GLY LYS LEU SER ILE GLU LYS GLU PRO ASN ALA GLY          
SEQRES  12 A  191  ASN PRO VAL ARG LYS GLY LEU ASN PRO LEU LEU GLY PHE          
SEQRES  13 A  191  ASP VAL TRP GLU HIS ALA TYR TYR LEU THR TYR GLN ASN          
SEQRES  14 A  191  ARG ARG ALA ASP HIS LEU LYS ASP LEU TRP SER ILE VAL          
SEQRES  15 A  191  ASP TRP ASP ILE VAL GLU SER ARG TYR                          
SEQRES   1 B  191  MET THR HIS GLU LEU ILE SER LEU PRO TYR ALA VAL ASP          
SEQRES   2 B  191  ALA LEU ALA PRO VAL ILE SER LYS GLU THR VAL GLU PHE          
SEQRES   3 B  191  HIS HIS GLY LYS HIS LEU LYS THR TYR VAL ASP ASN LEU          
SEQRES   4 B  191  ASN LYS LEU ILE ILE GLY THR GLU PHE GLU ASN ALA ASP          
SEQRES   5 B  191  LEU ASN THR ILE VAL GLN LYS SER GLU GLY GLY ILE PHE          
SEQRES   6 B  191  ASN ASN ALA GLY GLN THR LEU ASN HIS ASN LEU TYR PHE          
SEQRES   7 B  191  THR GLN PHE ARG PRO GLY LYS GLY GLY ALA PRO LYS GLY          
SEQRES   8 B  191  LYS LEU GLY GLU ALA ILE ASP LYS GLN PHE GLY SER PHE          
SEQRES   9 B  191  GLU LYS PHE LYS GLU GLU PHE ASN THR ALA GLY THR THR          
SEQRES  10 B  191  LEU PHE GLY SER GLY TRP VAL TRP LEU ALA SER ASP ALA          
SEQRES  11 B  191  ASN GLY LYS LEU SER ILE GLU LYS GLU PRO ASN ALA GLY          
SEQRES  12 B  191  ASN PRO VAL ARG LYS GLY LEU ASN PRO LEU LEU GLY PHE          
SEQRES  13 B  191  ASP VAL TRP GLU HIS ALA TYR TYR LEU THR TYR GLN ASN          
SEQRES  14 B  191  ARG ARG ALA ASP HIS LEU LYS ASP LEU TRP SER ILE VAL          
SEQRES  15 B  191  ASP TRP ASP ILE VAL GLU SER ARG TYR                          
SEQRES   1 C  191  MET THR HIS GLU LEU ILE SER LEU PRO TYR ALA VAL ASP          
SEQRES   2 C  191  ALA LEU ALA PRO VAL ILE SER LYS GLU THR VAL GLU PHE          
SEQRES   3 C  191  HIS HIS GLY LYS HIS LEU LYS THR TYR VAL ASP ASN LEU          
SEQRES   4 C  191  ASN LYS LEU ILE ILE GLY THR GLU PHE GLU ASN ALA ASP          
SEQRES   5 C  191  LEU ASN THR ILE VAL GLN LYS SER GLU GLY GLY ILE PHE          
SEQRES   6 C  191  ASN ASN ALA GLY GLN THR LEU ASN HIS ASN LEU TYR PHE          
SEQRES   7 C  191  THR GLN PHE ARG PRO GLY LYS GLY GLY ALA PRO LYS GLY          
SEQRES   8 C  191  LYS LEU GLY GLU ALA ILE ASP LYS GLN PHE GLY SER PHE          
SEQRES   9 C  191  GLU LYS PHE LYS GLU GLU PHE ASN THR ALA GLY THR THR          
SEQRES  10 C  191  LEU PHE GLY SER GLY TRP VAL TRP LEU ALA SER ASP ALA          
SEQRES  11 C  191  ASN GLY LYS LEU SER ILE GLU LYS GLU PRO ASN ALA GLY          
SEQRES  12 C  191  ASN PRO VAL ARG LYS GLY LEU ASN PRO LEU LEU GLY PHE          
SEQRES  13 C  191  ASP VAL TRP GLU HIS ALA TYR TYR LEU THR TYR GLN ASN          
SEQRES  14 C  191  ARG ARG ALA ASP HIS LEU LYS ASP LEU TRP SER ILE VAL          
SEQRES  15 C  191  ASP TRP ASP ILE VAL GLU SER ARG TYR                          
SEQRES   1 D  191  MET THR HIS GLU LEU ILE SER LEU PRO TYR ALA VAL ASP          
SEQRES   2 D  191  ALA LEU ALA PRO VAL ILE SER LYS GLU THR VAL GLU PHE          
SEQRES   3 D  191  HIS HIS GLY LYS HIS LEU LYS THR TYR VAL ASP ASN LEU          
SEQRES   4 D  191  ASN LYS LEU ILE ILE GLY THR GLU PHE GLU ASN ALA ASP          
SEQRES   5 D  191  LEU ASN THR ILE VAL GLN LYS SER GLU GLY GLY ILE PHE          
SEQRES   6 D  191  ASN ASN ALA GLY GLN THR LEU ASN HIS ASN LEU TYR PHE          
SEQRES   7 D  191  THR GLN PHE ARG PRO GLY LYS GLY GLY ALA PRO LYS GLY          
SEQRES   8 D  191  LYS LEU GLY GLU ALA ILE ASP LYS GLN PHE GLY SER PHE          
SEQRES   9 D  191  GLU LYS PHE LYS GLU GLU PHE ASN THR ALA GLY THR THR          
SEQRES  10 D  191  LEU PHE GLY SER GLY TRP VAL TRP LEU ALA SER ASP ALA          
SEQRES  11 D  191  ASN GLY LYS LEU SER ILE GLU LYS GLU PRO ASN ALA GLY          
SEQRES  12 D  191  ASN PRO VAL ARG LYS GLY LEU ASN PRO LEU LEU GLY PHE          
SEQRES  13 D  191  ASP VAL TRP GLU HIS ALA TYR TYR LEU THR TYR GLN ASN          
SEQRES  14 D  191  ARG ARG ALA ASP HIS LEU LYS ASP LEU TRP SER ILE VAL          
SEQRES  15 D  191  ASP TRP ASP ILE VAL GLU SER ARG TYR                          
HET     FE  A 201       1                                                       
HET     FE  B 201       1                                                       
HET     FE  C 201       1                                                       
HET     FE  D 201       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   5   FE    4(FE 3+)                                                     
FORMUL   9  HOH   *436(H2 O1)                                                   
HELIX    1   1 SER A   20  LYS A   30  1                                  11    
HELIX    2   2 LYS A   30  ILE A   43  1                                  14    
HELIX    3   3 ASP A   52  SER A   60  1                                   9    
HELIX    4   4 GLU A   61  GLN A   80  1                                  20    
HELIX    5   5 LYS A   90  GLY A  102  1                                  13    
HELIX    6   6 SER A  103  LEU A  118  1                                  16    
HELIX    7   7 ASN A  144  GLY A  149  5                                   6    
HELIX    8   8 TRP A  159  ALA A  162  5                                   4    
HELIX    9   9 TYR A  163  GLN A  168  1                                   6    
HELIX   10  10 ARG A  170  TRP A  179  1                                  10    
HELIX   11  11 ASP A  183  SER A  189  1                                   7    
HELIX   12  12 SER B   20  HIS B   28  1                                   9    
HELIX   13  13 LYS B   30  ILE B   43  1                                  14    
HELIX   14  14 ASP B   52  SER B   60  1                                   9    
HELIX   15  15 GLU B   61  GLN B   80  1                                  20    
HELIX   16  16 LYS B   90  GLY B  102  1                                  13    
HELIX   17  17 SER B  103  LEU B  118  1                                  16    
HELIX   18  18 ASN B  144  GLY B  149  5                                   6    
HELIX   19  19 TRP B  159  ALA B  162  5                                   4    
HELIX   20  20 TYR B  163  GLN B  168  1                                   6    
HELIX   21  21 ARG B  170  TRP B  179  1                                  10    
HELIX   22  22 ASP B  183  SER B  189  1                                   7    
HELIX   23  23 SER C   20  HIS C   28  1                                   9    
HELIX   24  24 LYS C   30  ILE C   43  1                                  14    
HELIX   25  25 ASP C   52  SER C   60  1                                   9    
HELIX   26  26 GLU C   61  GLN C   80  1                                  20    
HELIX   27  27 LYS C   90  GLY C  102  1                                  13    
HELIX   28  28 SER C  103  LEU C  118  1                                  16    
HELIX   29  29 ASN C  144  GLY C  149  5                                   6    
HELIX   30  30 TRP C  159  ALA C  162  5                                   4    
HELIX   31  31 TYR C  163  GLN C  168  1                                   6    
HELIX   32  32 ARG C  170  TRP C  179  1                                  10    
HELIX   33  33 ASP C  183  TYR C  191  1                                   9    
HELIX   34  34 SER D   20  LYS D   30  1                                  11    
HELIX   35  35 LYS D   30  ILE D   44  1                                  15    
HELIX   36  36 ASP D   52  SER D   60  1                                   9    
HELIX   37  37 GLU D   61  THR D   79  1                                  19    
HELIX   38  38 LYS D   90  GLY D  102  1                                  13    
HELIX   39  39 SER D  103  LEU D  118  1                                  16    
HELIX   40  40 ASN D  144  GLY D  149  5                                   6    
HELIX   41  41 TRP D  159  ALA D  162  5                                   4    
HELIX   42  42 TYR D  163  GLN D  168  1                                   6    
HELIX   43  43 ARG D  170  TRP D  179  1                                  10    
HELIX   44  44 ASP D  183  SER D  189  1                                   7    
SHEET    1   A 3 LEU A 134  PRO A 140  0                                        
SHEET    2   A 3 GLY A 122  SER A 128 -1  N  ALA A 127   O  SER A 135           
SHEET    3   A 3 ASN A 151  ASP A 157 -1  N  PHE A 156   O  VAL A 124           
SHEET    1   B 3 LEU B 134  PRO B 140  0                                        
SHEET    2   B 3 GLY B 122  SER B 128 -1  N  ALA B 127   O  SER B 135           
SHEET    3   B 3 ASN B 151  ASP B 157 -1  N  PHE B 156   O  VAL B 124           
SHEET    1   C 3 LEU C 134  PRO C 140  0                                        
SHEET    2   C 3 GLY C 122  SER C 128 -1  N  ALA C 127   O  SER C 135           
SHEET    3   C 3 ASN C 151  ASP C 157 -1  N  PHE C 156   O  VAL C 124           
SHEET    1   D 3 LEU D 134  PRO D 140  0                                        
SHEET    2   D 3 GLY D 122  SER D 128 -1  N  ALA D 127   O  SER D 135           
SHEET    3   D 3 ASN D 151  ASP D 157 -1  N  PHE D 156   O  VAL D 124           
LINK        FE    FE A 201                 NE2 HIS A 161     1555   1555  2.12  
LINK        FE    FE A 201                 OD2 ASP A 157     1555   1555  1.88  
LINK        FE    FE A 201                 O   HOH A2085     1555   1555  2.11  
LINK        FE    FE A 201                 NE2 HIS A  27     1555   1555  2.14  
LINK        FE    FE A 201                 NE2 HIS A  74     1555   1555  2.13  
LINK        FE    FE B 201                 NE2 HIS B  74     1555   1555  2.15  
LINK        FE    FE B 201                 O   HOH B2088     1555   1555  2.06  
LINK        FE    FE B 201                 NE2 HIS B  27     1555   1555  2.23  
LINK        FE    FE B 201                 OD2 ASP B 157     1555   1555  1.84  
LINK        FE    FE B 201                 NE2 HIS B 161     1555   1555  2.13  
LINK        FE    FE C 201                 NE2 HIS C  74     1555   1555  2.11  
LINK        FE    FE C 201                 OD2 ASP C 157     1555   1555  1.79  
LINK        FE    FE C 201                 O   HOH C2117     1555   1555  2.05  
LINK        FE    FE C 201                 NE2 HIS C  27     1555   1555  2.24  
LINK        FE    FE C 201                 NE2 HIS C 161     1555   1555  2.20  
LINK        FE    FE D 201                 OD2 ASP D 157     1555   1555  1.90  
LINK        FE    FE D 201                 NE2 HIS D  74     1555   1555  2.20  
LINK        FE    FE D 201                 O   HOH D2056     1555   1555  2.18  
LINK        FE    FE D 201                 NE2 HIS D 161     1555   1555  2.16  
LINK        FE    FE D 201                 NE2 HIS D  27     1555   1555  2.24  
CISPEP   1 ALA A   16    PRO A   17          0         0.14                     
CISPEP   2 ALA B   16    PRO B   17          0         0.68                     
CISPEP   3 ALA C   16    PRO C   17          0         0.49                     
CISPEP   4 ALA D   16    PRO D   17          0         0.31                     
SITE     1 AC1  5 HIS A  27  HIS A  74  ASP A 157  HIS A 161                    
SITE     2 AC1  5 HOH A2085                                                     
SITE     1 AC2  5 HIS B  27  HIS B  74  ASP B 157  HIS B 161                    
SITE     2 AC2  5 HOH B2088                                                     
SITE     1 AC3  5 HIS C  27  HIS C  74  ASP C 157  HIS C 161                    
SITE     2 AC3  5 HOH C2117                                                     
SITE     1 AC4  5 HIS D  27  HIS D  74  ASP D 157  HIS D 161                    
SITE     2 AC4  5 HOH D2056                                                     
CRYST1   75.470  102.660   99.590  90.00  90.00  90.00 P 21 21 21   16          
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      0.013250  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009741  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010041        0.00000                         
MTRIX1   1  0.256110 -0.146860 -0.955430       89.17615    1                    
MTRIX2   1 -0.148060 -0.982690  0.111360      112.99615    1                    
MTRIX3   1 -0.955240  0.112940 -0.273420      100.25890    1                    
MTRIX1   2 -0.102620 -0.140210  0.984790        2.85580    1                    
MTRIX2   2 -0.137380 -0.978530 -0.153630      103.85100    1                    
MTRIX3   2  0.985190 -0.151060  0.081150       18.22559    1                    
MTRIX1   3 -0.943880  0.270760  0.189160       57.08716    1                    
MTRIX2   3  0.269120  0.962480 -0.034820       14.43610    1                    
MTRIX3   3 -0.191490  0.018040 -0.981330      106.03601    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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