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Database: PDB
Entry: 3MM8
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HEADER    OXIDOREDUCTASE                          19-APR-10   3MM8              
TITLE     DISSIMILATORY SULFITE REDUCTASE NITRATE COMPLEX                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SULFITE REDUCTASE, DISSIMILATORY-TYPE SUBUNIT ALPHA;       
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: HYDROGENSULFITE REDUCTASE SUBUNIT ALPHA;                    
COMPND   5 EC: 1.8.99.3;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SULFITE REDUCTASE, DISSIMILATORY-TYPE SUBUNIT BETA;        
COMPND   8 CHAIN: B, E;                                                         
COMPND   9 SYNONYM: HYDROGENSULFITE REDUCTASE SUBUNIT BETA;                     
COMPND  10 EC: 1.8.99.3                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   3 ORGANISM_TAXID: 2234;                                                
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   6 ORGANISM_TAXID: 2234                                                 
KEYWDS    ALPHA-BETA-PROTEIN, OXIDOREDUCTASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.PAREY,E.WARKENTIN,P.M.H.KRONECK,U.ERMLER                            
REVDAT   3   08-NOV-17 3MM8    1       REMARK                                   
REVDAT   2   06-JUL-11 3MM8    1       JRNL                                     
REVDAT   1   21-JUL-10 3MM8    0                                                
JRNL        AUTH   K.PAREY,E.WARKENTIN,P.M.KRONECK,U.ERMLER                     
JRNL        TITL   REACTION CYCLE OF THE DISSIMILATORY SULFITE REDUCTASE FROM   
JRNL        TITL 2 ARCHAEOGLOBUS FULGIDUS.                                      
JRNL        REF    BIOCHEMISTRY                  V.  49  8912 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   20822098                                                     
JRNL        DOI    10.1021/BI100781F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.28 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0046                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 75008                          
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 + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3947                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.28                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3894                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 205                          
REMARK   3   BIN FREE R VALUE                    : 0.3570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12458                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 320                                     
REMARK   3   SOLVENT ATOMS            : 137                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.81000                                             
REMARK   3    B22 (A**2) : -2.85000                                             
REMARK   3    B33 (A**2) : 5.60000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.22000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.341         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.222         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.190         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.154        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13187 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17995 ; 1.623 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1556 ; 6.233 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   574 ;37.150 ;23.763       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2214 ;16.648 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;18.036 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1878 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10050 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 6                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     174      2                      
REMARK   3           1     D      1       D     174      2                      
REMARK   3           2     A    176       A     176      2                      
REMARK   3           2     D    176       D     176      2                      
REMARK   3           3     A    185       A     218      2                      
REMARK   3           3     D    185       D     218      2                      
REMARK   3           4     A    220       A     222      2                      
REMARK   3           4     D    220       D     222      2                      
REMARK   3           5     A    224       A     386      3                      
REMARK   3           5     D    224       D     386      3                      
REMARK   3           6     A   2570       A    2576      1                      
REMARK   3           6     D   2570       D    2576      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1579 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1579 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1440 ; 0.240 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    A    (A):    124 ; 0.030 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    829 ; 0.030 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    829 ; 0.030 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    707 ; 0.510 ; 0.500           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    661 ; 0.030 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    661 ; 0.030 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    818 ; 1.180 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    142 ; 0.030 ; 5.000           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1579 ; 4.240 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1579 ; 4.240 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1440 ; 8.170 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):    124 ; 9.870 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    829 ; 5.280 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    829 ; 5.280 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    707 ; 5.870 ; 2.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):    661 ; 3.390 ;10.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):    661 ; 3.390 ;10.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):    818 ;11.240 ;10.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):    142 ; 8.900 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      4       B     180      2                      
REMARK   3           1     E      4       E     180      2                      
REMARK   3           2     B    184       B     366      3                      
REMARK   3           2     E    184       E     366      3                      
REMARK   3           3     B   2580       B    2586      3                      
REMARK   3           3     E   2580       E    2586      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):   1440 ; 0.240 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    707 ; 0.510 ; 0.500           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    818 ; 1.180 ; 5.000           
REMARK   3   TIGHT THERMAL      2    A (A**2):   1440 ; 8.170 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    707 ; 5.870 ; 2.000           
REMARK   3   LOOSE THERMAL      2    A (A**2):    818 ;11.240 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : D A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):    124 ; 0.030 ; 0.050           
REMARK   3   LOOSE POSITIONAL   3    A    (A):    142 ; 0.030 ; 5.000           
REMARK   3   TIGHT THERMAL      3    A (A**2):    124 ; 9.870 ; 0.500           
REMARK   3   LOOSE THERMAL      3    A (A**2):    142 ; 8.900 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   417                          
REMARK   3    RESIDUE RANGE :   B     4        B   366                          
REMARK   3    RESIDUE RANGE :   D     1        D   417                          
REMARK   3    RESIDUE RANGE :   E     4        E   366                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.2880  17.1270  38.9410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3150 T22:   0.2994                                     
REMARK   3      T33:   0.1384 T12:  -0.0301                                     
REMARK   3      T13:   0.0927 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0600 L22:   1.2691                                     
REMARK   3      L33:   0.5808 L12:   0.1384                                     
REMARK   3      L13:  -0.0533 L23:  -0.0566                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0694 S12:   0.4821 S13:   0.0237                       
REMARK   3      S21:  -0.5798 S22:   0.0543 S23:  -0.3182                       
REMARK   3      S31:   0.0026 S32:   0.1676 S33:   0.0150                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 3MM8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000058720.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99980                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.280                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 1.930                              
REMARK 200  R MERGE                    (I) : 0.20800                            
REMARK 200  R SYM                      (I) : 0.15300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.1900                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.88                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.44000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.050                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC 5.6.0046                                       
REMARK 200 STARTING MODEL: 3C7B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 100 MM NA-CITRATE, 0.2 M   
REMARK 280  NACL, 5% (V/V) 2-PROPANOL, 50 MM NANO3, PH 6.5, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 291.0K                                    
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       34.45000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 35000 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 50270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -207.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E                            
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 A     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     MET D     0                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     VAL E     3                                                      
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 B 308   C     ALA B 309   N       0.144                       
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    PHE A  94       73.67   -153.12                                   
REMARK 500    TYR A 210     -169.51   -169.36                                   
REMARK 500    CYS A 223        3.51    -68.45                                   
REMARK 500    ASP A 240     -157.72   -103.15                                   
REMARK 500    VAL A 262      -63.62   -130.48                                   
REMARK 500    MET A 289      -16.76     91.43                                   
REMARK 500    VAL A 318      -95.18     55.94                                   
REMARK 500    MET A 416     -125.21    -87.35                                   
REMARK 500    TYR B  27      118.64    -28.80                                   
REMARK 500    ARG B  60      -53.44     72.01                                   
REMARK 500    THR B 134     -145.78   -108.90                                   
REMARK 500    HIS B 139      -11.51   -154.64                                   
REMARK 500    ARG B 276      -42.98     78.31                                   
REMARK 500    TRP B 296       53.39     39.99                                   
REMARK 500    HIS B 317       -9.80     85.86                                   
REMARK 500    PHE D  94       71.06   -153.15                                   
REMARK 500    PRO D 178        1.11    -64.20                                   
REMARK 500    ASP D 240     -156.41   -102.07                                   
REMARK 500    VAL D 262      -62.61   -131.45                                   
REMARK 500    MET D 289      -20.38     88.02                                   
REMARK 500    VAL D 318      -93.64     55.18                                   
REMARK 500    MET D 416     -124.11    -87.01                                   
REMARK 500    VAL E  36      -72.52    -59.81                                   
REMARK 500    LYS E  37     -155.38   -132.51                                   
REMARK 500    ARG E  60      -63.98     69.89                                   
REMARK 500    TYR E  77      -37.57   -143.86                                   
REMARK 500    THR E  95      -86.65    -93.17                                   
REMARK 500    THR E 134     -143.98   -124.51                                   
REMARK 500    HIS E 139      -15.00   -148.04                                   
REMARK 500    ALA E 147      -76.94    -54.59                                   
REMARK 500    LYS E 166       25.50    -68.42                                   
REMARK 500    PRO E 168      -41.02    -19.36                                   
REMARK 500    ALA E 184       43.97    -84.48                                   
REMARK 500    THR E 210     -155.02   -110.48                                   
REMARK 500    CYS E 211      119.06     59.77                                   
REMARK 500    LYS E 230      -73.91    -76.66                                   
REMARK 500    ASN E 231      -48.28     85.02                                   
REMARK 500    ARG E 276      -48.31     66.92                                   
REMARK 500    HIS E 317       -9.55     79.58                                   
REMARK 500    GLU E 318       85.07    -64.13                                   
REMARK 500    ARG E 319      175.16    -59.77                                   
REMARK 500    ASP E 347       12.68   -145.80                                   
REMARK 500    SER E 361      149.49    173.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE A  317     VAL A  318                 -142.10                    
REMARK 500 PHE D  317     VAL D  318                 -146.43                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    HIS E 165         10.40                                           
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                             SF4 E 586  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 244   SG                                                     
REMARK 620 2 SF4 E 586   S1  118.4                                              
REMARK 620 3 SF4 E 586   S2  107.0 105.7                                        
REMARK 620 4 SF4 E 586   S4  114.2 105.1 105.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 575  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 223   SG                                                     
REMARK 620 2 SF4 D 575   S1  109.3                                              
REMARK 620 3 SF4 D 575   S3  109.9 109.7                                        
REMARK 620 4 SF4 D 575   S4  117.8 106.0 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 585  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 182   SG                                                     
REMARK 620 2 SF4 B 585   S1  103.6                                              
REMARK 620 3 SF4 B 585   S2   99.6 102.4                                        
REMARK 620 4 SF4 B 585   S4  135.3 104.4 107.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 576  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 285   SG                                                     
REMARK 620 2 SF4 D 576   S1  128.3                                              
REMARK 620 3 SF4 D 576   S2   98.2 107.4                                        
REMARK 620 4 SF4 D 576   S3  109.8 105.7 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 575  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 219   SG                                                     
REMARK 620 2 SF4 D 575   S2  128.2                                              
REMARK 620 3 SF4 D 575   S3  120.6 103.3                                        
REMARK 620 4 SF4 D 575   S4   87.9 107.0 105.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 E 586  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 220   SG                                                     
REMARK 620 2 SF4 E 586   S2  111.9                                              
REMARK 620 3 SF4 E 586   S3  120.3 104.0                                        
REMARK 620 4 SF4 E 586   S4  108.9 105.6 105.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 586  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 247   SG                                                     
REMARK 620 2 SF4 B 586   S1  105.7                                              
REMARK 620 3 SF4 B 586   S2  120.0 102.5                                        
REMARK 620 4 SF4 B 586   S3  116.8 102.4 107.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 585  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 140   SG                                                     
REMARK 620 2 SF4 B 585   S1  123.4                                              
REMARK 620 3 SF4 B 585   S3  102.9 104.5                                        
REMARK 620 4 SF4 B 585   S4  116.5 103.1 104.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 576  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 285   SG                                                     
REMARK 620 2 SF4 A 576   S1  124.7                                              
REMARK 620 3 SF4 A 576   S2   94.6 106.3                                        
REMARK 620 4 SF4 A 576   S3  116.5 109.2 100.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 575  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 181   SG                                                     
REMARK 620 2 SF4 D 575   S1  129.0                                              
REMARK 620 3 SF4 D 575   S2   97.5 105.3                                        
REMARK 620 4 SF4 D 575   S4  109.6 106.5 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 586  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 244   SG                                                     
REMARK 620 2 SF4 B 586   S1  121.4                                              
REMARK 620 3 SF4 B 586   S2   92.8 102.0                                        
REMARK 620 4 SF4 B 586   S4  122.2 107.7 105.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 576  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 291   SG                                                     
REMARK 620 2 SF4 A 576   S2  116.9                                              
REMARK 620 3 SF4 A 576   S3  108.8 101.0                                        
REMARK 620 4 SF4 A 576   S4  118.2 106.6 103.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 586  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 241   SG                                                     
REMARK 620 2 SF4 B 586   S1  108.4                                              
REMARK 620 3 SF4 B 586   S3  117.5 102.3                                        
REMARK 620 4 SF4 B 586   S4  114.2 108.7 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 585  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 178   SG                                                     
REMARK 620 2 SF4 B 585   S1  100.8                                              
REMARK 620 3 SF4 B 585   S2  126.4 103.0                                        
REMARK 620 4 SF4 B 585   S3  111.4 105.2 107.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 575  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 175   SG                                                     
REMARK 620 2 SF4 D 575   S1  110.5                                              
REMARK 620 3 SF4 D 575   S2  117.6 105.5                                        
REMARK 620 4 SF4 D 575   S3  111.1 109.1 102.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 576  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 266   SG                                                     
REMARK 620 2 SF4 D 576   S1  101.6                                              
REMARK 620 3 SF4 D 576   S3  118.7 105.5                                        
REMARK 620 4 SF4 D 576   S4  118.1 108.2 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 586  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 220   SG                                                     
REMARK 620 2 SF4 B 586   S2  110.6                                              
REMARK 620 3 SF4 B 586   S3  120.9 105.9                                        
REMARK 620 4 SF4 B 586   S4  107.9 105.8 104.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 575  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 223   SG                                                     
REMARK 620 2 SF4 A 575   S1  120.6                                              
REMARK 620 3 SF4 A 575   S3  100.7 109.8                                        
REMARK 620 4 SF4 A 575   S4  112.4 108.1 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 576  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 288   SG                                                     
REMARK 620 2 SF4 D 576   S1  113.0                                              
REMARK 620 3 SF4 D 576   S2  124.1 106.6                                        
REMARK 620 4 SF4 D 576   S4  100.9 108.5 102.1                                  
REMARK 620 5 HOH D 423   O    80.2 166.4  65.8  64.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 576  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 291   SG                                                     
REMARK 620 2 SF4 D 576   S2  104.5                                              
REMARK 620 3 SF4 D 576   S3  125.2 106.0                                        
REMARK 620 4 SF4 D 576   S4  111.5 104.1 103.7                                  
REMARK 620 5 HOH D 423   O    84.8  60.9 150.1  59.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 E 585  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 178   SG                                                     
REMARK 620 2 SF4 E 585   S1  109.8                                              
REMARK 620 3 SF4 E 585   S2  141.7 104.9                                        
REMARK 620 4 SF4 E 585   S3   81.8 105.3 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 E 585  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 140   SG                                                     
REMARK 620 2 SF4 E 585   S1  147.9                                              
REMARK 620 3 SF4 E 585   S3   93.9 105.2                                        
REMARK 620 4 SF4 E 585   S4   93.8 105.3 105.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 575  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 219   SG                                                     
REMARK 620 2 SF4 A 575   S2  121.5                                              
REMARK 620 3 SF4 A 575   S3  123.8 102.2                                        
REMARK 620 4 SF4 A 575   S4   96.0 105.0 105.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 576  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 288   SG                                                     
REMARK 620 2 SF4 A 576   S1  119.8                                              
REMARK 620 3 SF4 A 576   S2  119.9 104.4                                        
REMARK 620 4 SF4 A 576   S4   97.4 108.7 105.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 575  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 181   SG                                                     
REMARK 620 2 SF4 A 575   S1  122.6                                              
REMARK 620 3 SF4 A 575   S2  105.0 109.9                                        
REMARK 620 4 SF4 A 575   S4  107.3 107.9 102.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 585  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 134   OG1                                                    
REMARK 620 2 SF4 B 585   S2   93.8                                              
REMARK 620 3 SF4 B 585   S3  154.5 106.4                                        
REMARK 620 4 SF4 B 585   S4   85.4 107.2 102.5                                  
REMARK 620 5 CYS B 177   SG   57.5 113.4  99.5 125.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 E 586  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 241   SG                                                     
REMARK 620 2 SF4 E 586   S1  104.1                                              
REMARK 620 3 SF4 E 586   S3  118.6 105.6                                        
REMARK 620 4 SF4 E 586   S4  117.2 105.4 104.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 E 586  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 247   SG                                                     
REMARK 620 2 SF4 E 586   S1  103.2                                              
REMARK 620 3 SF4 E 586   S2  113.2 105.9                                        
REMARK 620 4 SF4 E 586   S3  123.2 106.0 104.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 575  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 175   SG                                                     
REMARK 620 2 SF4 A 575   S1  105.6                                              
REMARK 620 3 SF4 A 575   S2  122.1 108.2                                        
REMARK 620 4 SF4 A 575   S3  108.6 109.8 102.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 576  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 266   SG                                                     
REMARK 620 2 SF4 A 576   S1   95.7                                              
REMARK 620 3 SF4 A 576   S3  123.5 108.2                                        
REMARK 620 4 SF4 A 576   S4  118.4 108.3 101.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 E 585  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 182   SG                                                     
REMARK 620 2 SF4 E 585   S1   86.4                                              
REMARK 620 3 SF4 E 585   S2  108.2 104.7                                        
REMARK 620 4 SF4 E 585   S4  140.2 105.4 105.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SRM B 570  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 223   SG                                                     
REMARK 620 2 SRM B 570   NA  104.1                                              
REMARK 620 3 SRM B 570   NB   99.0  88.9                                        
REMARK 620 4 SRM B 570   NC   85.8 170.1  90.3                                  
REMARK 620 5 SRM B 570   ND   91.5  88.9 169.6  90.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SRM A 580  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NO3 A 590   O2                                                     
REMARK 620 2 SRM A 580   NA  108.3                                              
REMARK 620 3 SRM A 580   NB   86.9  85.7                                        
REMARK 620 4 SRM A 580   NC   74.2 170.3  85.1                                  
REMARK 620 5 SRM A 580   ND   93.6  94.2 179.5  94.9                            
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 SRM A 580                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 575                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 576                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 590                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 585                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 586                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRM B 570                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRM D 580                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D 575                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D 576                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 E 585                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 E 586                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRM E 570                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3MM5   RELATED DB: PDB                                   
REMARK 900 DISSIMILATORY SULFITE REDUCTASE IN COMPLEX WITH THE SUBSTRATE        
REMARK 900 SULFITE                                                              
REMARK 900 RELATED ID: 3MM6   RELATED DB: PDB                                   
REMARK 900 DISSIMILATORY SULFITE REDUCTASE CYANIDE COMPLEX                      
REMARK 900 RELATED ID: 3MM7   RELATED DB: PDB                                   
REMARK 900 DISSIMILATORY SULFITE REDUCTASE CARBON MONOXIDE COMPLEX              
REMARK 900 RELATED ID: 3MM9   RELATED DB: PDB                                   
REMARK 900 DISSIMILATORY SULFITE REDUCTASE NITRITE COMPLEX                      
REMARK 900 RELATED ID: 3MMA   RELATED DB: PDB                                   
REMARK 900 DISSIMILATORY SULFITE REDUCTASE PHOSPHATE COMPLEX                    
REMARK 900 RELATED ID: 3MMB   RELATED DB: PDB                                   
REMARK 900 DISSIMILATORY SULFITE REDUCTASE IN COMPLEX WITH THE ENDPRODUCT       
REMARK 900 SULFIDE                                                              
DBREF  3MM8 A    0   417  UNP    Q59109   DSRA_ARCFU       1    418             
DBREF  3MM8 B    1   366  UNP    Q59110   DSRB_ARCFU       1    366             
DBREF  3MM8 D    0   417  UNP    Q59109   DSRA_ARCFU       1    418             
DBREF  3MM8 E    1   366  UNP    Q59110   DSRB_ARCFU       1    366             
SEQRES   1 A  418  MET SER GLU THR PRO LEU LEU ASP GLU LEU GLU LYS GLY          
SEQRES   2 A  418  PRO TRP PRO SER PHE VAL LYS GLU ILE LYS LYS THR ALA          
SEQRES   3 A  418  GLU LEU MET GLU LYS ALA ALA ALA GLU GLY LYS ASP VAL          
SEQRES   4 A  418  LYS MET PRO LYS GLY ALA ARG GLY LEU LEU LYS GLN LEU          
SEQRES   5 A  418  GLU ILE SER TYR LYS ASP LYS LYS THR HIS TRP LYS HIS          
SEQRES   6 A  418  GLY GLY ILE VAL SER VAL VAL GLY TYR GLY GLY GLY VAL          
SEQRES   7 A  418  ILE GLY ARG TYR SER ASP LEU GLY GLU GLN ILE PRO GLU          
SEQRES   8 A  418  VAL GLU HIS PHE HIS THR MET ARG ILE ASN GLN PRO SER          
SEQRES   9 A  418  GLY TRP PHE TYR SER THR LYS ALA LEU ARG GLY LEU CYS          
SEQRES  10 A  418  ASP VAL TRP GLU LYS TRP GLY SER GLY LEU THR ASN PHE          
SEQRES  11 A  418  HIS GLY SER THR GLY ASP ILE ILE PHE LEU GLY THR ARG          
SEQRES  12 A  418  SER GLU TYR LEU GLN PRO CYS PHE GLU ASP LEU GLY ASN          
SEQRES  13 A  418  LEU GLU ILE PRO PHE ASP ILE GLY GLY SER GLY SER ASP          
SEQRES  14 A  418  LEU ARG THR PRO SER ALA CYS MET GLY PRO ALA LEU CYS          
SEQRES  15 A  418  GLU PHE ALA CYS TYR ASP THR LEU GLU LEU CYS TYR ASP          
SEQRES  16 A  418  LEU THR MET THR TYR GLN ASP GLU LEU HIS ARG PRO MET          
SEQRES  17 A  418  TRP PRO TYR LYS PHE LYS ILE LYS CYS ALA GLY CYS PRO          
SEQRES  18 A  418  ASN ASP CYS VAL ALA SER LYS ALA ARG SER ASP PHE ALA          
SEQRES  19 A  418  ILE ILE GLY THR TRP LYS ASP ASP ILE LYS VAL ASP GLN          
SEQRES  20 A  418  GLU ALA VAL LYS GLU TYR ALA SER TRP MET ASP ILE GLU          
SEQRES  21 A  418  ASN GLU VAL VAL LYS LEU CYS PRO THR GLY ALA ILE LYS          
SEQRES  22 A  418  TRP ASP GLY LYS GLU LEU THR ILE ASP ASN ARG GLU CYS          
SEQRES  23 A  418  VAL ARG CYS MET HIS CYS ILE ASN LYS MET PRO LYS ALA          
SEQRES  24 A  418  LEU LYS PRO GLY ASP GLU ARG GLY ALA THR ILE LEU ILE          
SEQRES  25 A  418  GLY GLY LYS ALA PRO PHE VAL GLU GLY ALA VAL ILE GLY          
SEQRES  26 A  418  TRP VAL ALA VAL PRO PHE VAL GLU VAL GLU LYS PRO TYR          
SEQRES  27 A  418  ASP GLU ILE LYS GLU ILE LEU GLU ALA ILE TRP ASP TRP          
SEQRES  28 A  418  TRP ASP GLU GLU GLY LYS PHE ARG GLU ARG ILE GLY GLU          
SEQRES  29 A  418  LEU ILE TRP ARG LYS GLY MET ARG GLU PHE LEU LYS VAL          
SEQRES  30 A  418  ILE GLY ARG GLU ALA ASP VAL ARG MET VAL LYS ALA PRO          
SEQRES  31 A  418  ARG ASN ASN PRO PHE MET PHE PHE GLU LYS ASP GLU LEU          
SEQRES  32 A  418  LYS PRO SER ALA TYR THR GLU GLU LEU LYS LYS ARG GLY          
SEQRES  33 A  418  MET TRP                                                      
SEQRES   1 B  366  MET VAL VAL GLU GLY VAL LYS THR ASP PHE GLY PRO PRO          
SEQRES   2 B  366  TYR PHE ARG ASP LEU LEU HIS PRO VAL ILE ALA LYS ASN          
SEQRES   3 B  366  TYR GLY LYS TRP LYS TYR HIS GLU VAL VAL LYS PRO GLY          
SEQRES   4 B  366  VAL ILE LYS ARG VAL ALA GLU SER GLY ASP VAL ILE TYR          
SEQRES   5 B  366  VAL VAL ARG PHE GLY THR PRO ARG LEU LEU SER ILE TYR          
SEQRES   6 B  366  THR VAL ARG GLU LEU CYS ASP ILE ALA ASP LYS TYR SER          
SEQRES   7 B  366  ASP GLY TYR LEU ARG TRP THR SER ARG ASN ASN VAL GLU          
SEQRES   8 B  366  PHE PHE VAL THR ASP GLU SER LYS ILE ASP ASP LEU ILE          
SEQRES   9 B  366  ASN GLU VAL GLN GLU ARG VAL GLY PHE PRO CYS GLY GLY          
SEQRES  10 B  366  THR TRP ASP ALA VAL LYS GLY GLU TYR GLY LEU SER ASN          
SEQRES  11 B  366  ILE VAL HIS THR GLN GLY TRP ILE HIS CYS HIS THR PRO          
SEQRES  12 B  366  ALA ILE ASP ALA SER GLY ILE VAL LYS ALA VAL MET ASP          
SEQRES  13 B  366  GLU LEU TYR GLU TYR PHE THR ASP HIS LYS LEU PRO ALA          
SEQRES  14 B  366  MET CYS ARG ILE SER LEU ALA CYS CYS ALA ASN MET CYS          
SEQRES  15 B  366  GLY ALA VAL HIS ALA SER ASP ILE ALA ILE VAL GLY ILE          
SEQRES  16 B  366  HIS ARG THR PRO PRO ILE PRO ASN ASP GLU ALA ILE ARG          
SEQRES  17 B  366  LYS THR CYS GLU ILE PRO SER THR VAL ALA ALA CYS PRO          
SEQRES  18 B  366  THR GLY ALA LEU LYS PRO ASP MET LYS ASN LYS THR ILE          
SEQRES  19 B  366  LYS VAL ASP VAL GLU LYS CYS MET TYR CYS GLY ASN CYS          
SEQRES  20 B  366  TYR THR MET CYS PRO GLY MET PRO LEU PHE ASP PRO GLU          
SEQRES  21 B  366  ASN ASP GLY ALA ALA ILE MET VAL GLY GLY LYS LEU SER          
SEQRES  22 B  366  GLU ALA ARG ARG MET PRO GLU LEU SER LYS VAL VAL VAL          
SEQRES  23 B  366  PRO TRP VAL PRO ASN GLU PRO PRO ARG TRP PRO THR LEU          
SEQRES  24 B  366  VAL LYS TYR VAL LYS GLN ILE LEU GLU ALA TRP ALA ALA          
SEQRES  25 B  366  ASN ALA ASN LYS HIS GLU ARG LEU ILE GLU TRP VAL ASP          
SEQRES  26 B  366  ARG ILE GLY TRP GLU ARG PHE PHE GLU LEU THR GLY LEU          
SEQRES  27 B  366  GLU PHE THR GLN HIS LEU ILE ASP ASP TYR ARG ILE THR          
SEQRES  28 B  366  PRO TYR PHE TYR SER GLU PHE ARG ALA SER THR GLN PHE          
SEQRES  29 B  366  LYS TRP                                                      
SEQRES   1 D  418  MET SER GLU THR PRO LEU LEU ASP GLU LEU GLU LYS GLY          
SEQRES   2 D  418  PRO TRP PRO SER PHE VAL LYS GLU ILE LYS LYS THR ALA          
SEQRES   3 D  418  GLU LEU MET GLU LYS ALA ALA ALA GLU GLY LYS ASP VAL          
SEQRES   4 D  418  LYS MET PRO LYS GLY ALA ARG GLY LEU LEU LYS GLN LEU          
SEQRES   5 D  418  GLU ILE SER TYR LYS ASP LYS LYS THR HIS TRP LYS HIS          
SEQRES   6 D  418  GLY GLY ILE VAL SER VAL VAL GLY TYR GLY GLY GLY VAL          
SEQRES   7 D  418  ILE GLY ARG TYR SER ASP LEU GLY GLU GLN ILE PRO GLU          
SEQRES   8 D  418  VAL GLU HIS PHE HIS THR MET ARG ILE ASN GLN PRO SER          
SEQRES   9 D  418  GLY TRP PHE TYR SER THR LYS ALA LEU ARG GLY LEU CYS          
SEQRES  10 D  418  ASP VAL TRP GLU LYS TRP GLY SER GLY LEU THR ASN PHE          
SEQRES  11 D  418  HIS GLY SER THR GLY ASP ILE ILE PHE LEU GLY THR ARG          
SEQRES  12 D  418  SER GLU TYR LEU GLN PRO CYS PHE GLU ASP LEU GLY ASN          
SEQRES  13 D  418  LEU GLU ILE PRO PHE ASP ILE GLY GLY SER GLY SER ASP          
SEQRES  14 D  418  LEU ARG THR PRO SER ALA CYS MET GLY PRO ALA LEU CYS          
SEQRES  15 D  418  GLU PHE ALA CYS TYR ASP THR LEU GLU LEU CYS TYR ASP          
SEQRES  16 D  418  LEU THR MET THR TYR GLN ASP GLU LEU HIS ARG PRO MET          
SEQRES  17 D  418  TRP PRO TYR LYS PHE LYS ILE LYS CYS ALA GLY CYS PRO          
SEQRES  18 D  418  ASN ASP CYS VAL ALA SER LYS ALA ARG SER ASP PHE ALA          
SEQRES  19 D  418  ILE ILE GLY THR TRP LYS ASP ASP ILE LYS VAL ASP GLN          
SEQRES  20 D  418  GLU ALA VAL LYS GLU TYR ALA SER TRP MET ASP ILE GLU          
SEQRES  21 D  418  ASN GLU VAL VAL LYS LEU CYS PRO THR GLY ALA ILE LYS          
SEQRES  22 D  418  TRP ASP GLY LYS GLU LEU THR ILE ASP ASN ARG GLU CYS          
SEQRES  23 D  418  VAL ARG CYS MET HIS CYS ILE ASN LYS MET PRO LYS ALA          
SEQRES  24 D  418  LEU LYS PRO GLY ASP GLU ARG GLY ALA THR ILE LEU ILE          
SEQRES  25 D  418  GLY GLY LYS ALA PRO PHE VAL GLU GLY ALA VAL ILE GLY          
SEQRES  26 D  418  TRP VAL ALA VAL PRO PHE VAL GLU VAL GLU LYS PRO TYR          
SEQRES  27 D  418  ASP GLU ILE LYS GLU ILE LEU GLU ALA ILE TRP ASP TRP          
SEQRES  28 D  418  TRP ASP GLU GLU GLY LYS PHE ARG GLU ARG ILE GLY GLU          
SEQRES  29 D  418  LEU ILE TRP ARG LYS GLY MET ARG GLU PHE LEU LYS VAL          
SEQRES  30 D  418  ILE GLY ARG GLU ALA ASP VAL ARG MET VAL LYS ALA PRO          
SEQRES  31 D  418  ARG ASN ASN PRO PHE MET PHE PHE GLU LYS ASP GLU LEU          
SEQRES  32 D  418  LYS PRO SER ALA TYR THR GLU GLU LEU LYS LYS ARG GLY          
SEQRES  33 D  418  MET TRP                                                      
SEQRES   1 E  366  MET VAL VAL GLU GLY VAL LYS THR ASP PHE GLY PRO PRO          
SEQRES   2 E  366  TYR PHE ARG ASP LEU LEU HIS PRO VAL ILE ALA LYS ASN          
SEQRES   3 E  366  TYR GLY LYS TRP LYS TYR HIS GLU VAL VAL LYS PRO GLY          
SEQRES   4 E  366  VAL ILE LYS ARG VAL ALA GLU SER GLY ASP VAL ILE TYR          
SEQRES   5 E  366  VAL VAL ARG PHE GLY THR PRO ARG LEU LEU SER ILE TYR          
SEQRES   6 E  366  THR VAL ARG GLU LEU CYS ASP ILE ALA ASP LYS TYR SER          
SEQRES   7 E  366  ASP GLY TYR LEU ARG TRP THR SER ARG ASN ASN VAL GLU          
SEQRES   8 E  366  PHE PHE VAL THR ASP GLU SER LYS ILE ASP ASP LEU ILE          
SEQRES   9 E  366  ASN GLU VAL GLN GLU ARG VAL GLY PHE PRO CYS GLY GLY          
SEQRES  10 E  366  THR TRP ASP ALA VAL LYS GLY GLU TYR GLY LEU SER ASN          
SEQRES  11 E  366  ILE VAL HIS THR GLN GLY TRP ILE HIS CYS HIS THR PRO          
SEQRES  12 E  366  ALA ILE ASP ALA SER GLY ILE VAL LYS ALA VAL MET ASP          
SEQRES  13 E  366  GLU LEU TYR GLU TYR PHE THR ASP HIS LYS LEU PRO ALA          
SEQRES  14 E  366  MET CYS ARG ILE SER LEU ALA CYS CYS ALA ASN MET CYS          
SEQRES  15 E  366  GLY ALA VAL HIS ALA SER ASP ILE ALA ILE VAL GLY ILE          
SEQRES  16 E  366  HIS ARG THR PRO PRO ILE PRO ASN ASP GLU ALA ILE ARG          
SEQRES  17 E  366  LYS THR CYS GLU ILE PRO SER THR VAL ALA ALA CYS PRO          
SEQRES  18 E  366  THR GLY ALA LEU LYS PRO ASP MET LYS ASN LYS THR ILE          
SEQRES  19 E  366  LYS VAL ASP VAL GLU LYS CYS MET TYR CYS GLY ASN CYS          
SEQRES  20 E  366  TYR THR MET CYS PRO GLY MET PRO LEU PHE ASP PRO GLU          
SEQRES  21 E  366  ASN ASP GLY ALA ALA ILE MET VAL GLY GLY LYS LEU SER          
SEQRES  22 E  366  GLU ALA ARG ARG MET PRO GLU LEU SER LYS VAL VAL VAL          
SEQRES  23 E  366  PRO TRP VAL PRO ASN GLU PRO PRO ARG TRP PRO THR LEU          
SEQRES  24 E  366  VAL LYS TYR VAL LYS GLN ILE LEU GLU ALA TRP ALA ALA          
SEQRES  25 E  366  ASN ALA ASN LYS HIS GLU ARG LEU ILE GLU TRP VAL ASP          
SEQRES  26 E  366  ARG ILE GLY TRP GLU ARG PHE PHE GLU LEU THR GLY LEU          
SEQRES  27 E  366  GLU PHE THR GLN HIS LEU ILE ASP ASP TYR ARG ILE THR          
SEQRES  28 E  366  PRO TYR PHE TYR SER GLU PHE ARG ALA SER THR GLN PHE          
SEQRES  29 E  366  LYS TRP                                                      
HET    SRM  A 580      63                                                       
HET    SF4  A 575       8                                                       
HET    SF4  A 576       8                                                       
HET    NO3  A 590       4                                                       
HET    SF4  B 585       8                                                       
HET    SF4  B 586       8                                                       
HET    SRM  B 570      63                                                       
HET    SRM  D 580      63                                                       
HET    SF4  D 575       8                                                       
HET    SF4  D 576       8                                                       
HET    SF4  E 585       8                                                       
HET    SF4  E 586       8                                                       
HET    SRM  E 570      63                                                       
HETNAM     SRM SIROHEME                                                         
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     NO3 NITRATE ION                                                      
FORMUL   5  SRM    4(C42 H42 FE N4 O16)                                         
FORMUL   6  SF4    8(FE4 S4)                                                    
FORMUL   8  NO3    N O3 1-                                                      
FORMUL  18  HOH   *137(H2 O)                                                    
HELIX    1   1 THR A    3  GLU A    8  1                                   6    
HELIX    2   2 LEU A    9  LYS A   11  5                                   3    
HELIX    3   3 SER A   16  GLU A   34  1                                  19    
HELIX    4   4 LYS A   42  LYS A   58  1                                  17    
HELIX    5   5 ILE A   88  GLU A   92  5                                   5    
HELIX    6   6 PRO A  102  GLY A  104  5                                   3    
HELIX    7   7 THR A  109  GLY A  123  1                                  15    
HELIX    8   8 ARG A  142  GLU A  144  5                                   3    
HELIX    9   9 TYR A  145  LEU A  156  1                                  12    
HELIX   10  10 MET A  176  LEU A  180  5                                   5    
HELIX   11  11 ASP A  187  TYR A  199  1                                  13    
HELIX   12  12 TYR A  199  ARG A  205  1                                   7    
HELIX   13  13 ALA A  225  SER A  230  1                                   6    
HELIX   14  14 ASP A  245  SER A  254  1                                  10    
HELIX   15  15 ASP A  257  VAL A  262  1                                   6    
HELIX   16  16 VAL A  263  CYS A  266  5                                   4    
HELIX   17  17 MET A  289  MET A  295  1                                   7    
HELIX   18  18 TYR A  337  GLY A  355  1                                  19    
HELIX   19  19 ARG A  360  GLY A  369  1                                  10    
HELIX   20  20 GLY A  369  ILE A  377  1                                   9    
HELIX   21  21 ASP A  382  VAL A  386  5                                   5    
HELIX   22  22 GLU A  398  LEU A  402  5                                   5    
HELIX   23  23 SER A  405  GLY A  415  1                                  11    
HELIX   24  24 TYR B   14  LEU B   19  5                                   6    
HELIX   25  25 HIS B   20  TYR B   27  1                                   8    
HELIX   26  26 ILE B   64  SER B   78  1                                  15    
HELIX   27  27 ASP B   96  SER B   98  5                                   3    
HELIX   28  28 LYS B   99  VAL B  111  1                                  13    
HELIX   29  29 GLN B  135  HIS B  139  5                                   5    
HELIX   30  30 ASP B  146  ASP B  164  1                                  19    
HELIX   31  31 ASN B  203  CYS B  211  1                                   9    
HELIX   32  32 GLU B  212  CYS B  220  1                                   9    
HELIX   33  33 GLY B  245  CYS B  251  1                                   7    
HELIX   34  34 TRP B  296  ALA B  314  1                                  19    
HELIX   35  35 ARG B  319  GLY B  337  1                                  19    
HELIX   36  36 THR B  341  ILE B  345  5                                   5    
HELIX   37  37 PRO B  352  PHE B  358  5                                   7    
HELIX   38  38 THR D    3  GLU D    8  1                                   6    
HELIX   39  39 LEU D    9  LYS D   11  5                                   3    
HELIX   40  40 SER D   16  GLU D   34  1                                  19    
HELIX   41  41 LYS D   42  LYS D   58  1                                  17    
HELIX   42  42 ILE D   88  GLU D   92  5                                   5    
HELIX   43  43 PRO D  102  GLY D  104  5                                   3    
HELIX   44  44 THR D  109  GLY D  123  1                                  15    
HELIX   45  45 ARG D  142  GLU D  144  5                                   3    
HELIX   46  46 TYR D  145  LEU D  156  1                                  12    
HELIX   47  47 MET D  176  LEU D  180  5                                   5    
HELIX   48  48 ASP D  187  TYR D  199  1                                  13    
HELIX   49  49 TYR D  199  ARG D  205  1                                   7    
HELIX   50  50 ALA D  225  SER D  230  1                                   6    
HELIX   51  51 ASP D  245  SER D  254  1                                  10    
HELIX   52  52 ASP D  257  VAL D  262  1                                   6    
HELIX   53  53 VAL D  263  CYS D  266  5                                   4    
HELIX   54  54 MET D  289  MET D  295  1                                   7    
HELIX   55  55 TYR D  337  GLY D  355  1                                  19    
HELIX   56  56 ARG D  360  GLY D  369  1                                  10    
HELIX   57  57 GLY D  369  ILE D  377  1                                   9    
HELIX   58  58 ASP D  382  VAL D  386  5                                   5    
HELIX   59  59 GLU D  398  LEU D  402  5                                   5    
HELIX   60  60 SER D  405  GLY D  415  1                                  11    
HELIX   61  61 TYR E   14  LEU E   19  5                                   6    
HELIX   62  62 HIS E   20  ASN E   26  1                                   7    
HELIX   63  63 ILE E   64  ASP E   79  1                                  16    
HELIX   64  64 LYS E   99  VAL E  111  1                                  13    
HELIX   65  65 ASP E  146  LEU E  158  1                                  13    
HELIX   66  66 LEU E  158  THR E  163  1                                   6    
HELIX   67  67 ASN E  203  ARG E  208  1                                   6    
HELIX   68  68 GLU E  212  ALA E  219  1                                   8    
HELIX   69  69 VAL E  238  CYS E  241  5                                   4    
HELIX   70  70 GLY E  245  CYS E  251  1                                   7    
HELIX   71  71 TRP E  296  ALA E  314  1                                  19    
HELIX   72  72 ARG E  319  GLY E  337  1                                  19    
HELIX   73  73 THR E  341  ILE E  345  5                                   5    
HELIX   74  74 PRO E  352  PHE E  358  5                                   7    
SHEET    1   A 2 TRP A  62  LYS A  63  0                                        
SHEET    2   A 2 TYR A  81  SER A  82 -1  O  TYR A  81   N  LYS A  63           
SHEET    1   B 5 VAL A  77  ILE A  78  0                                        
SHEET    2   B 5 HIS A  95  ILE A  99 -1  O  THR A  96   N  ILE A  78           
SHEET    3   B 5 ILE A 136  THR A 141 -1  O  ILE A 136   N  ILE A  99           
SHEET    4   B 5 LEU A 126  ASN A 128 -1  N  ASN A 128   O  ILE A 137           
SHEET    5   B 5 LEU B  61  SER B  63 -1  O  LEU B  62   N  THR A 127           
SHEET    1   C 6 PHE A 106  SER A 108  0                                        
SHEET    2   C 6 TYR B  81  TRP B  84 -1  O  LEU B  82   N  TYR A 107           
SHEET    3   C 6 VAL B  90  VAL B  94 -1  O  GLU B  91   N  ARG B  83           
SHEET    4   C 6 VAL B  50  PHE B  56 -1  N  VAL B  54   O  PHE B  92           
SHEET    5   C 6 VAL B  40  ALA B  45 -1  N  ILE B  41   O  VAL B  53           
SHEET    6   C 6 TRP B  30  LYS B  37 -1  N  GLU B  34   O  LYS B  42           
SHEET    1   D 5 SER A 173  ALA A 174  0                                        
SHEET    2   D 5 ILE A 214  ALA A 217  1  O  CYS A 216   N  SER A 173           
SHEET    3   D 5 PHE A 232  TRP A 238  1  O  ILE A 234   N  ALA A 217           
SHEET    4   D 5 ARG A 305  ILE A 311 -1  O  LEU A 310   N  ALA A 233           
SHEET    5   D 5 TRP A 325  VAL A 331 -1  O  TRP A 325   N  ILE A 311           
SHEET    1   E 2 LYS A 243  VAL A 244  0                                        
SHEET    2   E 2 LEU A 299  LYS A 300 -1  O  LYS A 300   N  LYS A 243           
SHEET    1   F 2 ILE A 271  TRP A 273  0                                        
SHEET    2   F 2 LEU A 278  ILE A 280 -1  O  THR A 279   N  LYS A 272           
SHEET    1   G 2 TRP B 119  ASP B 120  0                                        
SHEET    2   G 2 GLU B 125  TYR B 126 -1  O  GLU B 125   N  ASP B 120           
SHEET    1   H 4 ILE B 173  ALA B 176  0                                        
SHEET    2   H 4 ILE B 190  ILE B 195  1  O  ILE B 192   N  ALA B 176           
SHEET    3   H 4 GLY B 263  VAL B 268 -1  O  ALA B 265   N  VAL B 193           
SHEET    4   H 4 LYS B 283  PRO B 290 -1  O  VAL B 285   N  ILE B 266           
SHEET    1   I 2 LEU B 225  ASP B 228  0                                        
SHEET    2   I 2 THR B 233  VAL B 236 -1  O  THR B 233   N  ASP B 228           
SHEET    1   J 2 TRP D  62  LYS D  63  0                                        
SHEET    2   J 2 TYR D  81  SER D  82 -1  O  TYR D  81   N  LYS D  63           
SHEET    1   K 5 VAL D  77  ILE D  78  0                                        
SHEET    2   K 5 HIS D  95  ILE D  99 -1  O  THR D  96   N  ILE D  78           
SHEET    3   K 5 ILE D 136  THR D 141 -1  O  THR D 141   N  HIS D  95           
SHEET    4   K 5 LEU D 126  ASN D 128 -1  N  ASN D 128   O  ILE D 137           
SHEET    5   K 5 LEU E  61  SER E  63 -1  O  LEU E  62   N  THR D 127           
SHEET    1   L 6 PHE D 106  SER D 108  0                                        
SHEET    2   L 6 TYR E  81  TRP E  84 -1  O  LEU E  82   N  TYR D 107           
SHEET    3   L 6 VAL E  90  VAL E  94 -1  O  GLU E  91   N  ARG E  83           
SHEET    4   L 6 VAL E  50  PHE E  56 -1  N  TYR E  52   O  VAL E  94           
SHEET    5   L 6 VAL E  40  ALA E  45 -1  N  ILE E  41   O  VAL E  53           
SHEET    6   L 6 TRP E  30  LYS E  37 -1  N  GLU E  34   O  LYS E  42           
SHEET    1   M 5 SER D 173  ALA D 174  0                                        
SHEET    2   M 5 ILE D 214  ALA D 217  1  O  CYS D 216   N  SER D 173           
SHEET    3   M 5 PHE D 232  TRP D 238  1  O  ILE D 234   N  ALA D 217           
SHEET    4   M 5 ARG D 305  ILE D 311 -1  O  THR D 308   N  ILE D 235           
SHEET    5   M 5 TRP D 325  VAL D 331 -1  O  TRP D 325   N  ILE D 311           
SHEET    1   N 2 LYS D 243  VAL D 244  0                                        
SHEET    2   N 2 LEU D 299  LYS D 300 -1  O  LYS D 300   N  LYS D 243           
SHEET    1   O 2 ILE D 271  TRP D 273  0                                        
SHEET    2   O 2 LEU D 278  ILE D 280 -1  O  THR D 279   N  LYS D 272           
SHEET    1   P 2 TRP E 119  ASP E 120  0                                        
SHEET    2   P 2 GLU E 125  TYR E 126 -1  O  GLU E 125   N  ASP E 120           
SHEET    1   Q 4 ILE E 173  ALA E 176  0                                        
SHEET    2   Q 4 ILE E 190  ILE E 195  1  O  ILE E 192   N  ALA E 176           
SHEET    3   Q 4 GLY E 263  VAL E 268 -1  O  GLY E 263   N  ILE E 195           
SHEET    4   Q 4 LYS E 283  PRO E 290 -1  O  VAL E 285   N  ILE E 266           
SHEET    1   R 2 LEU E 225  ASP E 228  0                                        
SHEET    2   R 2 THR E 233  VAL E 236 -1  O  LYS E 235   N  LYS E 226           
SSBOND   1 CYS B  211    CYS B  251                          1555   1555  2.03  
SSBOND   2 CYS E  211    CYS E  251                          1555   1555  2.03  
LINK         SG  CYS E 244                FE3  SF4 E 586     1555   1555  2.15  
LINK         SG  CYS D 223                FE2  SF4 D 575     1555   1555  2.17  
LINK         SG  CYS B 182                FE3  SF4 B 585     1555   1555  2.17  
LINK         SG  CYS D 285                FE4  SF4 D 576     1555   1555  2.19  
LINK         SG  CYS D 219                FE1  SF4 D 575     1555   1555  2.19  
LINK         SG  CYS E 220                FE1  SF4 E 586     1555   1555  2.19  
LINK         SG  CYS B 247                FE4  SF4 B 586     1555   1555  2.21  
LINK         SG  CYS B 140                FE2  SF4 B 585     1555   1555  2.23  
LINK         SG  CYS A 285                FE4  SF4 A 576     1555   1555  2.25  
LINK         SG  CYS D 181                FE3  SF4 D 575     1555   1555  2.26  
LINK         SG  CYS B 244                FE3  SF4 B 586     1555   1555  2.26  
LINK         SG  CYS A 291                FE1  SF4 A 576     1555   1555  2.27  
LINK         SG  CYS B 241                FE2  SF4 B 586     1555   1555  2.27  
LINK         SG  CYS B 178                FE4  SF4 B 585     1555   1555  2.28  
LINK         SG  CYS D 175                FE4  SF4 D 575     1555   1555  2.29  
LINK         SG  CYS D 266                FE2  SF4 D 576     1555   1555  2.29  
LINK         SG  CYS B 220                FE1  SF4 B 586     1555   1555  2.29  
LINK         SG  CYS A 223                FE2  SF4 A 575     1555   1555  2.29  
LINK         SG  CYS D 288                FE3  SF4 D 576     1555   1555  2.31  
LINK         SG  CYS D 291                FE1  SF4 D 576     1555   1555  2.33  
LINK         SG  CYS E 178                FE4  SF4 E 585     1555   1555  2.35  
LINK         SG  CYS E 140                FE2  SF4 E 585     1555   1555  2.35  
LINK        FE3  SF4 D 576                 O   HOH D 423     1555   1555  2.36  
LINK         SG  CYS A 219                FE1  SF4 A 575     1555   1555  2.36  
LINK         SG  CYS A 288                FE3  SF4 A 576     1555   1555  2.37  
LINK         SG  CYS A 181                FE3  SF4 A 575     1555   1555  2.37  
LINK         OG1 THR B 134                FE1  SF4 B 585     1555   1555  2.39  
LINK         SG  CYS E 241                FE2  SF4 E 586     1555   1555  2.39  
LINK         SG  CYS E 247                FE4  SF4 E 586     1555   1555  2.41  
LINK         SG  CYS A 175                FE4  SF4 A 575     1555   1555  2.48  
LINK         SG  CYS A 266                FE2  SF4 A 576     1555   1555  2.51  
LINK         SG  CYS E 182                FE3  SF4 E 585     1555   1555  2.52  
LINK         SG  CYS B 177                FE1  SF4 B 585     1555   1555  2.53  
LINK         SG  CYS A 223                FE   SRM B 570     1555   1555  2.53  
LINK        FE1  SF4 D 576                 O   HOH D 423     1555   1555  2.69  
LINK        FE   SRM A 580                 O2  NO3 A 590     1555   1555  2.72  
CISPEP   1 PHE A  129    HIS A  130          0        -0.83                     
CISPEP   2 LYS A  335    PRO A  336          0         4.89                     
CISPEP   3 PRO B  293    PRO B  294          0         1.87                     
CISPEP   4 PHE D  129    HIS D  130          0        -0.55                     
CISPEP   5 LYS D  335    PRO D  336          0         4.99                     
CISPEP   6 LYS E  230    ASN E  231          0        14.28                     
CISPEP   7 PRO E  293    PRO E  294          0         1.83                     
SITE     1 AC1 28 ARG A  80  ARG A  98  GLY A 131  SER A 132                    
SITE     2 AC1 28 THR A 133  GLY A 134  ASP A 135  TYR A 210                    
SITE     3 AC1 28 LYS A 211  LYS A 213  LYS A 215  ARG A 229                    
SITE     4 AC1 28 LYS A 314  ALA A 315  PHE A 317  ARG A 358                    
SITE     5 AC1 28 ARG A 360  NO3 A 590  ARG B  60  GLN B 135                    
SITE     6 AC1 28 HIS B 139  HIS B 141  THR B 142  ASN B 180                    
SITE     7 AC1 28 CYS B 182  GLY B 183  THR B 249  SF4 B 585                    
SITE     1 AC2 10 CYS A 175  MET A 176  CYS A 181  ALA A 184                    
SITE     2 AC2 10 GLY A 218  CYS A 219  ASN A 221  ASP A 222                    
SITE     3 AC2 10 CYS A 223  SRM B 570                                          
SITE     1 AC3  8 CYS A 266  THR A 268  CYS A 285  VAL A 286                    
SITE     2 AC3  8 ARG A 287  CYS A 288  MET A 289  CYS A 291                    
SITE     1 AC4  5 ARG A  98  ARG A 170  LYS A 211  LYS A 213                    
SITE     2 AC4  5 SRM A 580                                                     
SITE     1 AC5  9 SRM A 580  THR B 134  GLN B 135  CYS B 140                    
SITE     2 AC5  9 PRO B 143  CYS B 177  CYS B 178  ASN B 180                    
SITE     3 AC5  9 CYS B 182                                                     
SITE     1 AC6  9 CYS B 220  THR B 222  LEU B 225  CYS B 241                    
SITE     2 AC6  9 MET B 242  CYS B 244  GLY B 245  CYS B 247                    
SITE     3 AC6  9 LEU B 256                                                     
SITE     1 AC7 34 CYS A 175  MET A 176  CYS A 181  GLU A 182                    
SITE     2 AC7 34 PHE A 183  ASN A 221  CYS A 223  ASN A 293                    
SITE     3 AC7 34 HOH A 457  SF4 A 575  HIS B  33  ILE B  41                    
SITE     4 AC7 34 ARG B  43  ARG B  55  ARG B  83  THR B  85                    
SITE     5 AC7 34 SER B  86  ARG B  87  ASN B  89  GLY B 117                    
SITE     6 AC7 34 TRP B 119  ALA B 121  SER B 129  MET B 170                    
SITE     7 AC7 34 ARG B 172  LEU B 272  SER B 273  ARG B 276                    
SITE     8 AC7 34 ARG B 319  HOH B 369  HOH B 370  HOH B 385                    
SITE     9 AC7 34 HOH B 405  HOH B 419                                          
SITE     1 AC8 26 ILE D  78  ARG D  80  THR D  96  GLY D 131                    
SITE     2 AC8 26 SER D 132  THR D 133  ILE D 137  TYR D 210                    
SITE     3 AC8 26 LYS D 211  LYS D 213  LYS D 215  ARG D 229                    
SITE     4 AC8 26 ALA D 315  PHE D 317  ARG D 358  ARG D 360                    
SITE     5 AC8 26 GLN E 135  HIS E 139  HIS E 141  THR E 142                    
SITE     6 AC8 26 ASN E 180  MET E 181  CYS E 182  GLY E 183                    
SITE     7 AC8 26 THR E 249  SF4 E 585                                          
SITE     1 AC9  8 CYS D 175  CYS D 181  PHE D 183  GLY D 218                    
SITE     2 AC9  8 CYS D 219  ASN D 221  CYS D 223  SRM E 570                    
SITE     1 BC1  7 CYS D 266  THR D 268  CYS D 285  VAL D 286                    
SITE     2 BC1  7 CYS D 288  CYS D 291  HOH D 423                               
SITE     1 BC2  8 SRM D 580  THR E 134  CYS E 140  PRO E 143                    
SITE     2 BC2  8 CYS E 177  CYS E 178  ASN E 180  CYS E 182                    
SITE     1 BC3  7 CYS E 220  THR E 222  LEU E 225  CYS E 241                    
SITE     2 BC3  7 CYS E 244  GLY E 245  CYS E 247                               
SITE     1 BC4 24 MET D 176  CYS D 181  GLU D 182  PHE D 183                    
SITE     2 BC4 24 ASN D 221  CYS D 223  ASN D 293  SF4 D 575                    
SITE     3 BC4 24 HIS E  33  ARG E  43  ARG E  55  ARG E  83                    
SITE     4 BC4 24 THR E  85  SER E  86  ARG E  87  ASN E  89                    
SITE     5 BC4 24 TRP E 119  ALA E 121  SER E 129  ARG E 172                    
SITE     6 BC4 24 LEU E 272  SER E 273  ARG E 276  ARG E 319                    
CRYST1   94.600   68.900  145.100  90.00 107.50  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010571  0.000000  0.003333        0.00000                         
SCALE2      0.000000  0.014514  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007226        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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