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Database: PDB
Entry: 3MM7
LinkDB: 3MM7
Original site: 3MM7 
HEADER    OXIDOREDUCTASE                          19-APR-10   3MM7              
TITLE     DISSIMILATORY SULFITE REDUCTASE CARBON MONOXIDE 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 3MM7    1       REMARK                                   
REVDAT   2   06-JUL-11 3MM7    1       JRNL                                     
REVDAT   1   21-JUL-10 3MM7    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.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 133609                         
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7021                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9898                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 497                          
REMARK   3   BIN FREE R VALUE                    : 0.4000                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12462                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 318                                     
REMARK   3   SOLVENT ATOMS            : 512                                     
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) : 17.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.98000                                             
REMARK   3    B22 (A**2) : -2.28000                                             
REMARK   3    B33 (A**2) : 4.68000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.35000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.170         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.160         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.162         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.015        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13189 ; 0.023 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18000 ; 2.253 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1556 ; 7.411 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   574 ;36.801 ;23.763       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2214 ;17.172 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;20.084 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1878 ; 0.174 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10062 ; 0.013 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
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    ORIGIN FOR THE GROUP (A):  46.2720  11.7840  60.2920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0845 T22:   0.1046                                     
REMARK   3      T33:   0.0474 T12:  -0.0035                                     
REMARK   3      T13:  -0.0208 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2376 L22:   1.3545                                     
REMARK   3      L33:   0.4750 L12:   0.1150                                     
REMARK   3      L13:  -0.0837 L23:  -0.0193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0315 S12:   0.0838 S13:  -0.0472                       
REMARK   3      S21:  -0.1087 S22:   0.0314 S23:  -0.1573                       
REMARK   3      S31:   0.0183 S32:   0.0342 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   417                          
REMARK   3    RESIDUE RANGE :   E     4        E   366                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.1000  22.7850  18.1810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7308 T22:   0.7462                                     
REMARK   3      T33:   0.3514 T12:  -0.0516                                     
REMARK   3      T13:   0.2157 T23:   0.0818                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7020 L22:   1.1489                                     
REMARK   3      L33:   1.3378 L12:   0.1618                                     
REMARK   3      L13:  -0.0616 L23:   0.3593                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0487 S12:   0.6178 S13:   0.0516                       
REMARK   3      S21:  -0.7586 S22:   0.0866 S23:  -0.3849                       
REMARK   3      S31:  -0.0478 S32:   0.2563 S33:  -0.0379                       
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 3MM7 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_1000058719.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-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) : 1.0001                             
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) : 1.900                              
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     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.16400                            
REMARK 200  R SYM                      (I) : 0.13300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.28                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.65800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.760                              
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   (%): 51.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 100 MM NA-CITRATE, 0.2 M   
REMARK 280  NACL, 5% (V/V) 2-PROPANOL, 10 MM KCN, 1 BAR CO, PH 6.5, VAPOR       
REMARK 280  DIFFUSION, 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       34.64000            
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: 34970 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 51150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -208.0 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG A   229     O    HOH A   594              1.92            
REMARK 500   SG   CYS D   288     O    HOH D   540              1.93            
REMARK 500   O    HOH A   530     O    HOH B   554              2.04            
REMARK 500   O    HOH A   507     O    HOH A   535              2.05            
REMARK 500   O    HOH E   381     O    HOH E   439              2.06            
REMARK 500   O    HOH A   533     O    HOH A   585              2.12            
REMARK 500   O    HOH A   447     O    HOH A   466              2.13            
REMARK 500   OH   TYR A   252     O    HOH A   543              2.15            
REMARK 500   SG   CYS A   219     O    HOH A   522              2.17            
REMARK 500   O    HOH B   370     O    HOH B   499              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ALA A 111   CA    ALA A 111   CB      0.138                       
REMARK 500    ARG A 113   C     ARG A 113   O       0.151                       
REMARK 500    SER A 124   CB    SER A 124   OG      0.087                       
REMARK 500    TYR A 145   CE2   TYR A 145   CD2     0.111                       
REMARK 500    CYS A 149   CB    CYS A 149   SG      0.130                       
REMARK 500    GLY A 177   N     GLY A 177   CA     -0.093                       
REMARK 500    CYS A 219   CB    CYS A 219   SG     -0.183                       
REMARK 500    CYS A 223   CB    CYS A 223   SG      0.107                       
REMARK 500    CYS A 223   C     CYS A 223   O       0.120                       
REMARK 500    ALA A 225   CA    ALA A 225   CB      0.134                       
REMARK 500    VAL A 263   CB    VAL A 263   CG1    -0.162                       
REMARK 500    CYS A 266   CB    CYS A 266   SG      0.143                       
REMARK 500    ALA A 270   CA    ALA A 270   CB      0.214                       
REMARK 500    GLU A 284   CB    GLU A 284   CG      0.149                       
REMARK 500    ARG A 287   CZ    ARG A 287   NH1     0.084                       
REMARK 500    ARG B  55   CB    ARG B  55   CG      0.182                       
REMARK 500    ARG B  55   CG    ARG B  55   CD      0.205                       
REMARK 500    THR B  85   N     THR B  85   CA      0.149                       
REMARK 500    ARG B  87   CB    ARG B  87   CG      0.174                       
REMARK 500    TRP B 119   CB    TRP B 119   CG      0.122                       
REMARK 500    CYS B 140   CB    CYS B 140   SG     -0.110                       
REMARK 500    GLU B 274   C     GLU B 274   O       0.157                       
REMARK 500    ASP E  72   CB    ASP E  72   CG      0.325                       
REMARK 500    ASP E  79   CG    ASP E  79   OD2     0.138                       
REMARK 500    ASP E  79   C     GLY E  80   N       0.153                       
REMARK 500    SER E  98   CA    SER E  98   CB      0.102                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 156   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    PRO A 220   C   -  N   -  CA  ANGL. DEV. = -14.2 DEGREES          
REMARK 500    CYS A 266   CA  -  CB  -  SG  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG A 287   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B  55   CG  -  CD  -  NE  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ARG B  55   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    PRO B  59   C   -  N   -  CA  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ARG B 172   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG B 276   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP E  72   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    PRO E 168   C   -  N   -  CA  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    PRO E 168   C   -  N   -  CD  ANGL. DEV. = -13.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A  40       61.21   -111.18                                   
REMARK 500    PHE A  94       70.11   -150.09                                   
REMARK 500    TYR A 210     -159.83   -172.22                                   
REMARK 500    ASP A 241      139.09    -37.45                                   
REMARK 500    TRP A 255      -36.36   -142.04                                   
REMARK 500    VAL A 262      -72.06   -132.77                                   
REMARK 500    MET A 289      -37.97     53.08                                   
REMARK 500    HIS A 290      -39.88    -32.18                                   
REMARK 500    VAL A 383      -36.25    -39.13                                   
REMARK 500    TYR B  27      119.56    -36.15                                   
REMARK 500    GLU B  46      -38.18    -38.88                                   
REMARK 500    ARG B  60      -48.50     57.72                                   
REMARK 500    THR B 134     -152.72   -118.07                                   
REMARK 500    HIS B 139      -21.00   -144.43                                   
REMARK 500    HIS B 165       73.36   -105.83                                   
REMARK 500    MET B 181      -43.14     85.25                                   
REMARK 500    CYS B 182       39.11     34.09                                   
REMARK 500    ALA B 187       56.81   -144.35                                   
REMARK 500    MET B 254       54.90   -118.82                                   
REMARK 500    ARG B 276      -40.40     85.64                                   
REMARK 500    HIS B 317       -5.08     81.65                                   
REMARK 500    ARG B 319      172.97    -59.99                                   
REMARK 500    SER B 361      147.65   -177.42                                   
REMARK 500    ASP D  37       70.46    -69.21                                   
REMARK 500    PHE D  94       55.29   -158.06                                   
REMARK 500    ASN D 100      127.00    -37.40                                   
REMARK 500    PRO D 178        2.81    -67.29                                   
REMARK 500    TYR D 199       40.24   -109.91                                   
REMARK 500    TYR D 210     -170.52   -172.96                                   
REMARK 500    CYS D 223        1.05    -65.92                                   
REMARK 500    ASP D 240     -162.48   -109.19                                   
REMARK 500    VAL D 262      -69.21   -130.46                                   
REMARK 500    MET D 289      -15.46     88.29                                   
REMARK 500    PRO D 336       36.23    -93.28                                   
REMARK 500    TYR E  27      116.67    -36.75                                   
REMARK 500    LYS E  31      -70.85    -72.28                                   
REMARK 500    GLU E  34       97.53    176.65                                   
REMARK 500    VAL E  36      -79.02    -81.95                                   
REMARK 500    ARG E  60      -65.36     70.01                                   
REMARK 500    ASP E  79        8.09     47.97                                   
REMARK 500    LEU E  82     -175.31   -175.78                                   
REMARK 500    PHE E  93       67.01   -119.26                                   
REMARK 500    LEU E 103      -84.43    -46.83                                   
REMARK 500    ILE E 104      -57.09    -13.93                                   
REMARK 500    SER E 129     -151.55    -80.67                                   
REMARK 500    THR E 134     -138.75   -107.02                                   
REMARK 500    HIS E 139      -32.91   -142.93                                   
REMARK 500    ALA E 147      -70.81    -50.08                                   
REMARK 500    LYS E 152      -74.63    -61.48                                   
REMARK 500    ALA E 153      -77.92    -25.43                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      64 RAMACHANDRAN OUTLIERS.                        
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 ILE A  280     ASP A  281                  145.56                    
REMARK 500 ASN B   88     ASN B   89                  147.53                    
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    CYS A 288         17.09                                           
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 D 576  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 285   SG                                                     
REMARK 620 2 SF4 D 576   S1  117.7                                              
REMARK 620 3 SF4 D 576   S2  109.7 105.5                                        
REMARK 620 4 SF4 D 576   S3  108.4 105.9 109.4                                  
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  117.9                                              
REMARK 620 3 SF4 A 575   S3  124.6 105.9                                        
REMARK 620 4 SF4 A 575   S4   93.2 103.1 108.7                                  
REMARK 620 N                    1     2     3                                   
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  120.6                                              
REMARK 620 3 SF4 E 586   S2  101.5 103.8                                        
REMARK 620 4 SF4 E 586   S4  116.1 107.4 105.4                                  
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  113.4                                              
REMARK 620 3 SF4 B 586   S3  121.7 104.3                                        
REMARK 620 4 SF4 B 586   S4  105.5 104.8 105.8                                  
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   95.6                                              
REMARK 620 3 SF4 A 576   S3  100.0 102.6                                        
REMARK 620 4 SF4 A 576   S4  135.2 116.9 101.9                                  
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  101.9                                              
REMARK 620 3 SF4 B 585   S2  105.8 100.5                                        
REMARK 620 4 SF4 B 585   S4  136.7 100.4 105.9                                  
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  111.8                                              
REMARK 620 3 SF4 D 576   S3  121.5 106.1                                        
REMARK 620 4 SF4 D 576   S4  102.9 111.8 102.2                                  
REMARK 620 N                    1     2     3                                   
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  102.3                                              
REMARK 620 3 SF4 D 576   S3  122.7 109.5                                        
REMARK 620 4 SF4 D 576   S4  112.5 103.8 104.6                                  
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  116.1                                              
REMARK 620 3 SF4 A 575   S3  101.9 111.8                                        
REMARK 620 4 SF4 A 575   S4  111.0 108.1 107.6                                  
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  123.6                                              
REMARK 620 3 SF4 B 585   S3  102.4 103.9                                        
REMARK 620 4 SF4 B 585   S4  120.5 100.4 103.2                                  
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  118.0                                              
REMARK 620 3 SF4 D 575   S3  111.2 108.5                                        
REMARK 620 4 SF4 D 575   S4  113.6 100.4 103.8                                  
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  124.8                                              
REMARK 620 3 SF4 D 575   S2  105.9 104.6                                        
REMARK 620 4 SF4 D 575   S4  110.5 100.0 110.7                                  
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  118.3                                              
REMARK 620 3 SF4 A 576   S2  107.2 109.4                                        
REMARK 620 4 SF4 A 576   S3  112.7  96.5 112.5                                  
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  102.5                                              
REMARK 620 3 SF4 B 585   S2  124.5 100.1                                        
REMARK 620 4 SF4 B 585   S3  114.6 103.8 108.0                                  
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  113.9                                              
REMARK 620 3 SF4 D 576   S2  119.2 105.9                                        
REMARK 620 4 SF4 D 576   S4  104.6 110.9 101.5                                  
REMARK 620 5 HOH D 540   O    52.6 165.3  79.9  80.5                            
REMARK 620 N                    1     2     3     4                             
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  112.3                                              
REMARK 620 3 SF4 B 586   S2  110.1 102.0                                        
REMARK 620 4 SF4 B 586   S3  120.0 105.5 105.2                                  
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  130.2                                              
REMARK 620 3 SF4 A 576   S2  102.7 106.1                                        
REMARK 620 4 SF4 A 576   S4  103.0 115.3  92.4                                  
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  122.3                                              
REMARK 620 3 SF4 A 575   S2  107.1 108.2                                        
REMARK 620 4 SF4 A 575   S4  108.7 109.1  99.0                                  
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  106.4                                              
REMARK 620 3 SF4 A 576   S3  121.6 112.4                                        
REMARK 620 4 SF4 A 576   S4  110.2  95.7 107.5                                  
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  127.1                                              
REMARK 620 3 SF4 B 586   S2   98.2 102.2                                        
REMARK 620 4 SF4 B 586   S4  117.8 103.2 104.7                                  
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   95.5                                              
REMARK 620 3 SF4 A 575   S2  123.6 108.1                                        
REMARK 620 4 SF4 A 575   S3  106.5 114.7 108.3                                  
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  108.6                                              
REMARK 620 3 SF4 E 586   S3  118.7 104.5                                        
REMARK 620 4 SF4 E 586   S4  113.3 105.4 105.2                                  
REMARK 620 N                    1     2     3                                   
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  120.6                                              
REMARK 620 3 SF4 E 585   S2  116.9 104.7                                        
REMARK 620 4 SF4 E 585   S3  101.2 107.3 104.8                                  
REMARK 620 N                    1     2     3                                   
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  107.2                                              
REMARK 620 3 SF4 E 586   S3  115.5 105.5                                        
REMARK 620 4 SF4 E 586   S4  116.4 107.3 104.2                                  
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  103.7                                              
REMARK 620 3 SF4 B 586   S3  119.7 105.5                                        
REMARK 620 4 SF4 B 586   S4  115.5 103.4 107.2                                  
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  123.3                                              
REMARK 620 3 SF4 D 575   S3  114.2 101.2                                        
REMARK 620 4 SF4 D 575   S4  102.8 110.2 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SRM E 570  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 223   SG                                                     
REMARK 620 2 SRM E 570   NA  102.7                                              
REMARK 620 3 SRM E 570   NB   92.2  85.6                                        
REMARK 620 4 SRM E 570   NC   86.7 170.0  90.9                                  
REMARK 620 5 SRM E 570   ND   97.8  90.1 169.8  91.8                            
REMARK 620 N                    1     2     3     4                             
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  113.2                                              
REMARK 620 3 SF4 D 575   S2  119.4 105.2                                        
REMARK 620 4 SF4 D 575   S3  108.1 108.7 101.2                                  
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   96.7                                              
REMARK 620 3 SF4 E 586   S2  113.0 105.0                                        
REMARK 620 4 SF4 E 586   S3  128.8 105.9 104.6                                  
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  101.5                                              
REMARK 620 3 SRM B 570   NB   95.7  81.4                                        
REMARK 620 4 SRM B 570   NC   88.5 170.0  98.7                                  
REMARK 620 5 SRM B 570   ND   94.5  96.0 169.8  82.1                            
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 CYS B 182   SG                                                     
REMARK 620 2 SRM A 580   NA   90.9                                              
REMARK 620 3 SRM A 580   NB   92.4  83.0                                        
REMARK 620 4 SRM A 580   NC   86.4 170.8  88.3                                  
REMARK 620 5 SRM A 580   ND   87.9  96.9 179.7  91.8                            
REMARK 620 N                    1     2     3     4                             
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  130.1                                              
REMARK 620 3 SF4 E 585   S3   87.2 107.2                                        
REMARK 620 4 SF4 E 585   S4  116.1 106.2 104.7                                  
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  107.7                                              
REMARK 620 3 SF4 E 585   S2   91.0 104.6                                        
REMARK 620 4 SF4 E 585   S4  136.3 105.9 106.6                                  
REMARK 620 N                    1     2     3                                   
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 CMO 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: 3MM8   RELATED DB: PDB                                   
REMARK 900 DISSIMILATORY SULFITE REDUCTASE NITRATE 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  3MM7 A    0   417  UNP    Q59109   DSRA_ARCFU       1    418             
DBREF  3MM7 B    1   366  UNP    Q59110   DSRB_ARCFU       1    366             
DBREF  3MM7 D    0   417  UNP    Q59109   DSRA_ARCFU       1    418             
DBREF  3MM7 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    CMO  A 590       2                                                       
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     CMO CARBON MONOXIDE                                                  
FORMUL   5  SRM    4(C42 H42 FE N4 O16)                                         
FORMUL   6  SF4    8(FE4 S4)                                                    
FORMUL   8  CMO    C O                                                          
FORMUL  18  HOH   *512(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  ASN A  155  1                                  11    
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  GLY A  378  1                                  10    
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  ARG A  414  1                                  10    
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  GLY B  112  1                                  14    
HELIX   29  29 GLN B  135  HIS B  139  5                                   5    
HELIX   30  30 ALA B  147  THR B  163  1                                  17    
HELIX   31  31 GLY B  183  SER B  188  5                                   6    
HELIX   32  32 ASN B  203  CYS B  211  1                                   9    
HELIX   33  33 GLU B  212  ALA B  219  1                                   8    
HELIX   34  34 MET B  229  LYS B  232  5                                   4    
HELIX   35  35 GLY B  245  CYS B  251  1                                   7    
HELIX   36  36 TRP B  296  ALA B  314  1                                  19    
HELIX   37  37 ARG B  319  GLY B  328  1                                  10    
HELIX   38  38 GLY B  328  THR B  336  1                                   9    
HELIX   39  39 THR B  341  ILE B  345  5                                   5    
HELIX   40  40 PRO B  352  PHE B  358  5                                   7    
HELIX   41  41 THR D    3  GLU D    8  1                                   6    
HELIX   42  42 LEU D    9  LYS D   11  5                                   3    
HELIX   43  43 SER D   16  GLU D   34  1                                  19    
HELIX   44  44 LYS D   42  LYS D   58  1                                  17    
HELIX   45  45 ILE D   88  GLU D   92  5                                   5    
HELIX   46  46 PRO D  102  GLY D  104  5                                   3    
HELIX   47  47 THR D  109  GLY D  123  1                                  15    
HELIX   48  48 TYR D  145  ASN D  155  1                                  11    
HELIX   49  49 MET D  176  LEU D  180  5                                   5    
HELIX   50  50 ASP D  187  TYR D  199  1                                  13    
HELIX   51  51 TYR D  199  ARG D  205  1                                   7    
HELIX   52  52 ALA D  225  SER D  230  1                                   6    
HELIX   53  53 ASP D  245  SER D  254  1                                  10    
HELIX   54  54 ASP D  257  VAL D  262  1                                   6    
HELIX   55  55 MET D  289  MET D  295  1                                   7    
HELIX   56  56 TYR D  337  GLY D  355  1                                  19    
HELIX   57  57 ARG D  360  GLY D  369  1                                  10    
HELIX   58  58 GLY D  369  ILE D  377  1                                   9    
HELIX   59  59 ASP D  382  VAL D  386  5                                   5    
HELIX   60  60 GLU D  398  LEU D  402  5                                   5    
HELIX   61  61 SER D  405  ARG D  414  1                                  10    
HELIX   62  62 TYR E   14  LEU E   18  5                                   5    
HELIX   63  63 HIS E   20  TYR E   27  1                                   8    
HELIX   64  64 ILE E   64  SER E   78  1                                  15    
HELIX   65  65 LYS E   99  GLU E  109  1                                  11    
HELIX   66  66 GLN E  135  HIS E  139  5                                   5    
HELIX   67  67 ASP E  146  GLU E  157  1                                  12    
HELIX   68  68 LEU E  158  THR E  163  1                                   6    
HELIX   69  69 ASN E  203  THR E  210  1                                   8    
HELIX   70  70 GLU E  212  ALA E  218  1                                   7    
HELIX   71  71 VAL E  238  CYS E  241  5                                   4    
HELIX   72  72 GLY E  245  CYS E  251  1                                   7    
HELIX   73  73 TRP E  296  ALA E  314  1                                  19    
HELIX   74  74 ARG E  319  GLY E  328  1                                  10    
HELIX   75  75 GLY E  328  THR E  336  1                                   9    
HELIX   76  76 THR E  341  ILE E  345  5                                   5    
HELIX   77  77 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  PHE A 138   N  MET A  97           
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  LYS B  31   O  VAL B  44           
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  GLY A 236   N  ALA A 217           
SHEET    4   D 5 ARG A 305  ILE A 311 -1  O  THR A 308   N  ILE A 235           
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 5 ILE B 131  VAL B 132  0                                        
SHEET    2   H 5 ILE B 173  ALA B 176  1  O  LEU B 175   N  VAL B 132           
SHEET    3   H 5 ILE B 190  ILE B 195  1  O  ILE B 192   N  ALA B 176           
SHEET    4   H 5 GLY B 263  VAL B 268 -1  O  ALA B 265   N  VAL B 193           
SHEET    5   H 5 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  ILE D 136   N  ILE D  99           
SHEET    4   K 5 LEU D 126  ASN D 128 -1  N  LEU D 126   O  LEU D 139           
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  VAL E  54   O  PHE E  92           
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  VAL E  35 -1  N  TYR E  32   O  VAL E  44           
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  GLY D 236   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  ALA D 327   N  ILE D 309           
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  GLY E 194   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  LYS E 283   N  VAL E 268           
SHEET    1   R 2 LEU E 225  ASP E 228  0                                        
SHEET    2   R 2 THR E 233  VAL E 236 -1  O  THR E 233   N  ASP E 228           
SSBOND   1 CYS B  211    CYS B  251                          1555   1555  2.01  
SSBOND   2 CYS E  211    CYS E  251                          1555   1555  2.03  
LINK         SG  CYS D 285                FE4  SF4 D 576     1555   1555  1.94  
LINK         SG  CYS A 219                FE1  SF4 A 575     1555   1555  2.11  
LINK         SG  CYS E 244                FE3  SF4 E 586     1555   1555  2.20  
LINK         SG  CYS B 220                FE1  SF4 B 586     1555   1555  2.20  
LINK         SG  CYS A 266                FE2  SF4 A 576     1555   1555  2.20  
LINK         SG  CYS B 182                FE3  SF4 B 585     1555   1555  2.20  
LINK         SG  CYS D 266                FE2  SF4 D 576     1555   1555  2.22  
LINK         SG  CYS D 291                FE1  SF4 D 576     1555   1555  2.23  
LINK         SG  CYS A 223                FE2  SF4 A 575     1555   1555  2.23  
LINK         SG  CYS B 140                FE2  SF4 B 585     1555   1555  2.24  
LINK         SG  CYS D 223                FE2  SF4 D 575     1555   1555  2.24  
LINK         SG  CYS D 181                FE3  SF4 D 575     1555   1555  2.27  
LINK         SG  CYS A 285                FE4  SF4 A 576     1555   1555  2.29  
LINK         SG  CYS B 178                FE4  SF4 B 585     1555   1555  2.29  
LINK         SG  CYS D 288                FE3  SF4 D 576     1555   1555  2.32  
LINK         SG  CYS B 247                FE4  SF4 B 586     1555   1555  2.33  
LINK         SG  CYS A 288                FE3  SF4 A 576     1555   1555  2.34  
LINK         SG  CYS A 181                FE3  SF4 A 575     1555   1555  2.38  
LINK         SG  CYS A 291                FE1  SF4 A 576     1555   1555  2.39  
LINK         SG  CYS B 244                FE3  SF4 B 586     1555   1555  2.40  
LINK         SG  CYS A 175                FE4  SF4 A 575     1555   1555  2.40  
LINK         SG  CYS E 220                FE1  SF4 E 586     1555   1555  2.41  
LINK         SG  CYS E 178                FE4  SF4 E 585     1555   1555  2.42  
LINK         SG  CYS E 241                FE2  SF4 E 586     1555   1555  2.43  
LINK         SG  CYS B 241                FE2  SF4 B 586     1555   1555  2.43  
LINK         SG  CYS D 219                FE1  SF4 D 575     1555   1555  2.48  
LINK         SG  CYS D 223                FE   SRM E 570     1555   1555  2.48  
LINK         SG  CYS D 175                FE4  SF4 D 575     1555   1555  2.57  
LINK         SG  CYS E 247                FE4  SF4 E 586     1555   1555  2.57  
LINK         SG  CYS A 223                FE   SRM B 570     1555   1555  2.60  
LINK         SG  CYS B 182                FE   SRM A 580     1555   1555  2.67  
LINK        FE3  SF4 D 576                 O   HOH D 540     1555   1555  1.98  
LINK         SG  CYS E 140                FE2  SF4 E 585     1555   1555  1.75  
LINK         SG  CYS E 182                FE3  SF4 E 585     1555   1555  1.84  
CISPEP   1 PHE A  129    HIS A  130          0         3.16                     
CISPEP   2 PHE A  317    VAL A  318          0         6.16                     
CISPEP   3 LYS A  335    PRO A  336          0         5.39                     
CISPEP   4 PRO B  293    PRO B  294          0         3.14                     
CISPEP   5 PHE D  129    HIS D  130          0        -3.71                     
CISPEP   6 PHE D  317    VAL D  318          0        -0.88                     
CISPEP   7 LYS D  335    PRO D  336          0         1.54                     
CISPEP   8 LYS E  230    ASN E  231          0        14.91                     
CISPEP   9 PRO E  293    PRO E  294          0        -2.22                     
SITE     1 AC1 29 ILE A  78  ARG A  80  ARG A  98  GLY A 131                    
SITE     2 AC1 29 SER A 132  THR A 133  GLY A 134  ASP A 135                    
SITE     3 AC1 29 TYR A 210  LYS A 211  LYS A 213  LYS A 215                    
SITE     4 AC1 29 ARG A 229  LYS A 314  ALA A 315  PHE A 317                    
SITE     5 AC1 29 ARG A 358  ARG A 360  CMO A 590  HOH A 638                    
SITE     6 AC1 29 ARG B  60  THR B 134  HIS B 139  HIS B 141                    
SITE     7 AC1 29 THR B 142  ASN B 180  CYS B 182  GLY B 183                    
SITE     8 AC1 29 SF4 B 585                                                     
SITE     1 AC2  8 CYS A 175  MET A 176  CYS A 181  ALA A 184                    
SITE     2 AC2  8 GLY A 218  CYS A 219  ASN A 221  CYS A 223                    
SITE     1 AC3  8 CYS A 266  ALA A 270  ILE A 271  CYS A 285                    
SITE     2 AC3  8 VAL A 286  CYS A 288  MET A 289  CYS A 291                    
SITE     1 AC4  3 ARG A  98  ARG A 170  SRM A 580                               
SITE     1 AC5  9 SRM A 580  THR B 134  CYS B 140  THR B 142                    
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  8 CYS B 220  THR B 222  LEU B 225  CYS B 241                    
SITE     2 AC6  8 MET B 242  CYS B 244  GLY B 245  CYS B 247                    
SITE     1 AC7 32 MET A 176  CYS A 181  GLU A 182  PHE A 183                    
SITE     2 AC7 32 ASN A 221  CYS A 223  ASN A 293  HIS B  33                    
SITE     3 AC7 32 ILE B  41  ARG B  43  ARG B  55  ARG B  83                    
SITE     4 AC7 32 THR B  85  SER B  86  ARG B  87  ASN B  89                    
SITE     5 AC7 32 GLY B 117  THR B 118  TRP B 119  ALA B 121                    
SITE     6 AC7 32 SER B 129  MET B 170  ARG B 172  LEU B 272                    
SITE     7 AC7 32 SER B 273  ARG B 276  ARG B 319  HOH B 373                    
SITE     8 AC7 32 HOH B 392  HOH B 414  HOH B 472  HOH B 476                    
SITE     1 AC8 28 ILE D  78  ARG D  80  ARG D  98  GLY D 131                    
SITE     2 AC8 28 SER D 132  THR D 133  GLY D 134  ASP D 135                    
SITE     3 AC8 28 TYR D 210  LYS D 211  LYS D 213  LYS D 215                    
SITE     4 AC8 28 ARG D 229  LYS D 314  ALA D 315  PRO D 316                    
SITE     5 AC8 28 PHE D 317  ARG D 358  ARG D 360  ARG E  60                    
SITE     6 AC8 28 HIS E 133  THR E 134  HIS E 139  HIS E 141                    
SITE     7 AC8 28 ASN E 180  CYS E 182  GLY E 183  THR E 249                    
SITE     1 AC9  8 CYS D 175  CYS D 181  ALA D 184  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  CYS D 285  VAL D 286  CYS D 288                    
SITE     2 BC1  7 MET D 289  CYS D 291  HOH D 540                               
SITE     1 BC2  8 THR E 134  GLN E 135  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  6 CYS E 220  LEU E 225  CYS E 241  CYS E 244                    
SITE     2 BC3  6 GLY E 245  CYS E 247                                          
SITE     1 BC4 25 CYS D 175  MET D 176  CYS D 181  GLU D 182                    
SITE     2 BC4 25 PHE D 183  ASN D 221  CYS D 223  ASN D 293                    
SITE     3 BC4 25 SF4 D 575  HIS E  33  ARG E  43  ARG E  55                    
SITE     4 BC4 25 ARG E  83  THR E  85  SER E  86  ARG E  87                    
SITE     5 BC4 25 ASN E  89  TRP E 119  ALA E 121  SER E 129                    
SITE     6 BC4 25 ARG E 172  LEU E 272  SER E 273  ARG E 276                    
SITE     7 BC4 25 ARG E 319                                                     
CRYST1   94.840   69.280  146.330  90.00 107.68  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      0.010544  0.000000  0.003361        0.00000                         
SCALE2      0.000000  0.014434  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007173        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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