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Database: PDB
Entry: 2WQY
LinkDB: 2WQY
Original site: 2WQY 
HEADER    OXIDOREDUCTASE                          27-AUG-09   2WQY              
TITLE     REMODELLING OF CARBOXIN BINDING TO THE Q-SITE OF AVIAN RESPIRATORY    
TITLE    2 COMPLEX II                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT;              
COMPND   3 CHAIN: A, N;                                                         
COMPND   4 EC: 1.3.5.1;                                                         
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: SUCCINATE DEHYDROGENASE IP SUBUNIT;                        
COMPND   7 CHAIN: B, O;                                                         
COMPND   8 EC: 1.3.5.1;                                                         
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: SUCCINATE DEHYDROGENASE CYTOCHROME B, LARGE SUBUNIT;       
COMPND  11 CHAIN: C, P;                                                         
COMPND  12 EC: 1.3.5.1;                                                         
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: SUCCINATE DEHYDROGENASE CYTOCHROME B, SMALL SUBUNIT;       
COMPND  15 CHAIN: D, Q;                                                         
COMPND  16 FRAGMENT: RESIDUES 55-157;                                           
COMPND  17 EC: 1.3.5.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   4 ORGANISM_TAXID: 9031;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   7 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   8 ORGANISM_TAXID: 9031;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  11 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  12 ORGANISM_TAXID: 9031;                                                
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  15 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  16 ORGANISM_TAXID: 9031                                                 
KEYWDS    OXALOACETATE NITROPROPIONATE UBIQUINONE, RESPIRATORY CHAIN, COMPLEX   
KEYWDS   2 II, CYTOCROME B, REDOX ENZYME, HEME PROTEIN, FLAVOPROTEIN,           
KEYWDS   3 OXIDOREDUCTASE, METAL-BINDING, MITOCHONDRION INNER MEMBRANE, IRON    
KEYWDS   4 SULFUR PROTEIN, TRICARBOXYLIC ACID CYCLE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.RUPRECHT,S.IWATA,G.CECCHINI                                         
REVDAT   5   06-FEB-19 2WQY    1       REMARK                                   
REVDAT   4   30-JAN-19 2WQY    1       REMARK                                   
REVDAT   3   20-MAY-15 2WQY    1       HETNAM HETSYN                            
REVDAT   2   25-APR-12 2WQY    1       REMARK VERSN  HETSYN                     
REVDAT   1   25-AUG-10 2WQY    0                                                
JRNL        AUTH   J.RUPRECHT,S.IWATA,G.CECCHINI                                
JRNL        TITL   REMODELLING OF CARBOXIN BINDING TO THE Q-SITE OF AVIAN       
JRNL        TITL 2 RESPIRATORY COMPLEX II                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   0                                                                      
REMARK   0 THIS ENTRY 2WQY REFLECTS AN ALTERNATIVE MODELING OF THE              
REMARK   0 ORIGINAL STRUCTURAL DATA (R2FBWSF) DETERMINED BY                     
REMARK   0 AUTHORS OF THE PDB ENTRY 2FBW:                                       
REMARK   0 L.S.HUANG,G.SUN,D.COBESSI,A.C.WANG,J.T.SHEN,E.Y.TUNG,                
REMARK   0 V.E.ANDERSON,E.A.BERRY                                               
REMARK   0 ORIGINAL DATA REFERENCE 1                                            
REMARK   0  PDB ID: 2FBW                                                        
REMARK   0  AUTH   L.HUANG,G.SUN,D.COBESSI,A.C.WANG,J.T.SHEN,E.Y.TUNG,          
REMARK   0  AUTH 2 V.E.ANDERSON,E.A.BERRY                                       
REMARK   0  TITL   3-NITROPROPIONIC ACID IS A SUICIDE INHIBITOR OF              
REMARK   0  TITL 2 MITOCHONDRIAL RESPIRATION THAT, UPON OXIDATION BY COMPLEX    
REMARK   0  TITL 3 II, FORMS A COVALENT ADDUCT WITH A CATALYTIC BASE ARGININE   
REMARK   0  TITL 4 IN THE ACTIVE SITE OF THE ENZYME.                            
REMARK   0  REF    J.BIOL.CHEM.                  V. 281  5965 2006              
REMARK   0  REFN                   ISSN 0021-9258                               
REMARK   0  PMID   16371358                                                     
REMARK   0  DOI    10.1074/JBC.M511270200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 154202                         
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) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8009                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7054                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 375                          
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16978                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 516                                     
REMARK   3   SOLVENT ATOMS            : 1996                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.73000                                             
REMARK   3    B22 (A**2) : 1.50000                                              
REMARK   3    B33 (A**2) : -0.77000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.40000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.207         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY. STRUCTURE IS A            
REMARK   3  REMODELLING OF CARBOXIN BINDING TO THE Q- SITE OF AVIAN COMPLEX     
REMARK   3  II. POSITIONAL AND B-FACTOR REFINEMENT OF CARBOXIN ONLY WAS         
REMARK   3  PERFORMED. THE REST OF THE STRUCTURE IS AS MODELLED IN 2FBW.        
REMARK   4                                                                      
REMARK   4 2WQY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-AUG-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290040892.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1YQ3                                       
REMARK 200                                                                      
REMARK 200 REMARK: AUTHOR USED THE SF DATA FROM ENTRY 2FBW.                     
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 G/L PEG-3350, 25 ML/L ISOPROPANOL,    
REMARK 280  15 ML/L PEG-400 0.05 M NA-HEPES, 0.01 M TRIS-HCL, 0.0005 M MNCL2,   
REMARK 280  0.0013 M MGCL2, 0.0015 M NA-AZIDE, 0.00025 M NA-EDTA, CARBOXIN,     
REMARK 280  PH 7.50, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K            
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      100.37650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 15910 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 51890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 15650 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 50890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, O, P, Q                            
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     SER A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     ILE A     8                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     GLU B   247                                                      
REMARK 465     LYS B   248                                                      
REMARK 465     ALA B   249                                                      
REMARK 465     ALA B   250                                                      
REMARK 465     ALA B   251                                                      
REMARK 465     ALA B   252                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     SER N     1                                                      
REMARK 465     THR N     2                                                      
REMARK 465     LYS N     3                                                      
REMARK 465     VAL N     4                                                      
REMARK 465     SER N     5                                                      
REMARK 465     ASP N     6                                                      
REMARK 465     SER N     7                                                      
REMARK 465     ILE N     8                                                      
REMARK 465     SER N     9                                                      
REMARK 465     ALA O     1                                                      
REMARK 465     GLN O     2                                                      
REMARK 465     THR O     3                                                      
REMARK 465     ALA O     4                                                      
REMARK 465     ALA O     5                                                      
REMARK 465     ALA O     6                                                      
REMARK 465     ALA O     7                                                      
REMARK 465     GLU O   247                                                      
REMARK 465     LYS O   248                                                      
REMARK 465     ALA O   249                                                      
REMARK 465     ALA O   250                                                      
REMARK 465     ALA O   251                                                      
REMARK 465     ALA O   252                                                      
REMARK 465     MET P     1                                                      
REMARK 465     GLY Q     1                                                      
REMARK 465     SER Q     2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG B  66    CD                                                  
REMARK 470     ARG O  66    CD                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ASN N   277     O    HOH N  2286              2.15            
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    ARG A 469   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG B  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG N 469   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG O  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 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    THR A  10      -22.06   -159.48                                   
REMARK 500    ALA A 150     -127.17     49.63                                   
REMARK 500    LYS A 292     -126.07     58.33                                   
REMARK 500    HIS A 364      -34.27   -139.37                                   
REMARK 500    ASN A 407      114.81   -169.24                                   
REMARK 500    ALA A 480       51.81   -145.82                                   
REMARK 500    ALA A 481     -157.02    -92.57                                   
REMARK 500    ASN A 607       91.98   -172.57                                   
REMARK 500    SER B  64      -61.50   -153.49                                   
REMARK 500    ARG B  66       -2.46     53.84                                   
REMARK 500    PRO B  91        4.28    -69.88                                   
REMARK 500    LYS B 109      140.91   -172.25                                   
REMARK 500    ASP B 110     -113.45     39.71                                   
REMARK 500    HIS C  26      -75.99   -136.46                                   
REMARK 500    ILE C 140      106.25     78.92                                   
REMARK 500    ASP D  90     -167.09   -129.65                                   
REMARK 500    ALA N 150     -126.31     50.07                                   
REMARK 500    ASN N 277     -166.07   -100.66                                   
REMARK 500    LYS N 292     -125.84     57.83                                   
REMARK 500    HIS N 364      -34.68   -138.82                                   
REMARK 500    ASN N 407      115.45   -168.44                                   
REMARK 500    ALA N 480       51.52   -145.04                                   
REMARK 500    ALA N 481     -157.32    -92.75                                   
REMARK 500    ASN N 607       90.76   -172.54                                   
REMARK 500    ASP O  56       97.81   -160.26                                   
REMARK 500    SER O  64      -60.39   -153.82                                   
REMARK 500    ARG O  66       -2.00     53.93                                   
REMARK 500    LYS O 109      139.42   -172.35                                   
REMARK 500    ASP O 110     -113.73     40.73                                   
REMARK 500    HIS P  26      -75.69   -136.05                                   
REMARK 500    ILE P 140      106.11     81.00                                   
REMARK 500    ASP Q  90     -167.69   -129.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR C  30         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2200        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A2545        DISTANCE =  9.09 ANGSTROMS                       
REMARK 525    HOH A2546        DISTANCE =  7.94 ANGSTROMS                       
REMARK 525    HOH B2159        DISTANCE = 10.91 ANGSTROMS                       
REMARK 525    HOH B2291        DISTANCE = 10.01 ANGSTROMS                       
REMARK 525    HOH B2292        DISTANCE = 10.32 ANGSTROMS                       
REMARK 525    HOH C2028        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH D2014        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH N2037        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH N2046        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH N2099        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH N2221        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH N2358        DISTANCE = 10.64 ANGSTROMS                       
REMARK 525    HOH N2555        DISTANCE =  8.60 ANGSTROMS                       
REMARK 525    HOH O2057        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH O2283        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH P2025        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH P2081        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH Q2025        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH Q2033        DISTANCE =  6.18 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     HEM C  143                                                       
REMARK 610     PEE D  109                                                       
REMARK 610     HEM P  201                                                       
REMARK 610     PEE Q  210                                                       
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                               K A 622   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 397   O                                                      
REMARK 620 2 ALA A 399   O    86.0                                              
REMARK 620 3 TYR A 365   OH  102.3 117.9                                        
REMARK 620 4 ASN A 366   O    95.5 163.9  77.6                                  
REMARK 620 5 MET A 367   O   149.3  91.5 105.9  79.0                            
REMARK 620 6 GLY A 368   O    82.3  90.2 151.6  74.1  67.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 253   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 199   OG1                                                    
REMARK 620 2 HOH B2245   O    52.5                                              
REMARK 620 3 HOH B2250   O    68.2 120.7                                        
REMARK 620 4 HOH B2251   O    48.0  82.1  54.3                                  
REMARK 620 5 HOH B2244   O   110.6 143.3  55.0  66.7                            
REMARK 620 6 ASP B 196   O    89.6  76.8 103.4  57.1  70.3                      
REMARK 620 7 MET B 191   O    70.5  63.1 101.1 118.1 149.1 139.6                
REMARK 620 8 HOH B2241   O   122.7 156.2  61.8 112.1  59.6 126.8  93.1          
REMARK 620 9 ASP B 193   O   157.5 105.0 134.2 137.3  87.0  83.1 101.9  77.9    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B1002  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B1002   S1  111.6                                              
REMARK 620 3 FES B1002   S2  118.6 101.3                                        
REMARK 620 4 CYS B  85   SG  103.1 121.0 101.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B1002  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  70   SG                                                     
REMARK 620 2 FES B1002   S1  114.8                                              
REMARK 620 3 FES B1002   S2  116.4 101.1                                        
REMARK 620 4 CYS B  65   SG  104.4 114.4 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1003  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 164   SG                                                     
REMARK 620 2 SF4 B1003   S2  109.6                                              
REMARK 620 3 SF4 B1003   S3  116.6 102.1                                        
REMARK 620 4 SF4 B1003   S4  118.6 102.1 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1003  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 161   SG                                                     
REMARK 620 2 SF4 B1003   S1  127.1                                              
REMARK 620 3 SF4 B1003   S2  102.7 100.6                                        
REMARK 620 4 SF4 B1003   S3  115.8 105.0 101.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1003  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 225   SG                                                     
REMARK 620 2 SF4 B1003   S1  112.3                                              
REMARK 620 3 SF4 B1003   S2  112.1 102.4                                        
REMARK 620 4 SF4 B1003   S4  123.3 101.1 103.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1003  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 SF4 B1003   S1  124.5                                              
REMARK 620 3 SF4 B1003   S3   98.3 104.2                                        
REMARK 620 4 SF4 B1003   S4  121.2  99.9 106.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B1004  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 215   SG                                                     
REMARK 620 2 F3S B1004   S1  110.3                                              
REMARK 620 3 F3S B1004   S2  113.5 112.7                                        
REMARK 620 4 F3S B1004   S3  119.1  99.3 101.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B1004  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 221   SG                                                     
REMARK 620 2 F3S B1004   S1  108.2                                              
REMARK 620 3 F3S B1004   S3  114.1  99.0                                        
REMARK 620 4 F3S B1004   S4  115.0 115.7 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B1004  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 168   SG                                                     
REMARK 620 2 F3S B1004   S2  109.7                                              
REMARK 620 3 F3S B1004   S3  113.8 102.9                                        
REMARK 620 4 F3S B1004   S4  111.6 113.4 105.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 143  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  98   NE2                                                    
REMARK 620 2 HEM C 143   NA   87.3                                              
REMARK 620 3 HEM C 143   NB   88.1  87.8                                        
REMARK 620 4 HEM C 143   NC   89.7 177.0  92.0                                  
REMARK 620 5 HEM C 143   ND   89.6  91.5 177.6  88.6                            
REMARK 620 6 HIS D  46   NE2 177.9  94.1  90.5  88.9  91.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K N 622   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA N 399   O                                                      
REMARK 620 2 MET N 367   O    91.8                                              
REMARK 620 3 ASN N 366   O   166.1  80.1                                        
REMARK 620 4 TYR N 365   OH  116.3 104.9  76.9                                  
REMARK 620 5 GLU N 397   O    86.1 152.0  95.7 101.0                            
REMARK 620 6 GLY N 368   O    90.9  68.1  75.7 152.5  84.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K O 253   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH O2244   O                                                      
REMARK 620 2 ASP O 196   O    78.0                                              
REMARK 620 3 ASP O 193   O    99.1  83.9                                        
REMARK 620 4 HOH O2243   O   128.0  71.7 118.0                                  
REMARK 620 5 THR O 199   OG1  54.6  92.1 153.6  84.9                            
REMARK 620 6 MET O 191   O    59.9 137.4  96.1 139.4  69.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES O1002  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O  70   SG                                                     
REMARK 620 2 FES O1002   S1  113.9                                              
REMARK 620 3 FES O1002   S2  115.0  99.9                                        
REMARK 620 4 CYS O  65   SG  104.6 117.6 105.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES O1002  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O  85   SG                                                     
REMARK 620 2 FES O1002   S1  119.9                                              
REMARK 620 3 FES O1002   S2  102.8 100.3                                        
REMARK 620 4 CYS O  73   SG  105.3 109.7 119.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 O1003  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 161   SG                                                     
REMARK 620 2 SF4 O1003   S1  127.8                                              
REMARK 620 3 SF4 O1003   S2  102.8 100.2                                        
REMARK 620 4 SF4 O1003   S3  116.0 103.5 102.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 O1003  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 225   SG                                                     
REMARK 620 2 SF4 O1003   S1  115.3                                              
REMARK 620 3 SF4 O1003   S2  108.0 102.1                                        
REMARK 620 4 SF4 O1003   S4  125.3 100.6 102.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 O1003  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 158   SG                                                     
REMARK 620 2 SF4 O1003   S1  122.1                                              
REMARK 620 3 SF4 O1003   S3   99.8 104.3                                        
REMARK 620 4 SF4 O1003   S4  121.8 100.7 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 O1003  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 164   SG                                                     
REMARK 620 2 SF4 O1003   S2  111.5                                              
REMARK 620 3 SF4 O1003   S3  117.6 101.8                                        
REMARK 620 4 SF4 O1003   S4  118.6  99.6 105.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S O1004  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 168   SG                                                     
REMARK 620 2 F3S O1004   S2  111.0                                              
REMARK 620 3 F3S O1004   S3  114.4 101.5                                        
REMARK 620 4 F3S O1004   S4  114.9 112.1 101.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S O1004  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 221   SG                                                     
REMARK 620 2 F3S O1004   S1  109.8                                              
REMARK 620 3 F3S O1004   S3  116.3 100.6                                        
REMARK 620 4 F3S O1004   S4  112.4 114.6 102.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S O1004  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 215   SG                                                     
REMARK 620 2 F3S O1004   S1  108.6                                              
REMARK 620 3 F3S O1004   S2  114.8 113.7                                        
REMARK 620 4 F3S O1004   S3  118.5  99.4 100.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM P 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Q  46   NE2                                                    
REMARK 620 2 HEM P 201   NA   90.4                                              
REMARK 620 3 HEM P 201   NB   90.6  88.1                                        
REMARK 620 4 HEM P 201   NC   89.1 179.4  91.5                                  
REMARK 620 5 HEM P 201   ND   87.8  92.4 178.3  87.9                            
REMARK 620 6 HIS P  98   NE2 178.9  90.1  90.4  90.4  91.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BHG C 142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BHG P 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 622                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 253                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K N 622                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K O 253                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD N 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES O 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 O 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S O 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 143                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE C 144                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OAA A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE D 109                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM P 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE P 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OAA N 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE Q 210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL O 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL P 208                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FBW   RELATED DB: PDB                                   
REMARK 900 AVIAN RESPIRATORY COMPLEX II WITH CARBOXIN BOUND                     
REMARK 900 RELATED ID: 1YQ4   RELATED DB: PDB                                   
REMARK 900 AVIAN RESPIRATORY COMPLEX II WITH 3- NITROPROPIONATE ANDUBIQUINONE   
REMARK 900 RELATED ID: 1YQ3   RELATED DB: PDB                                   
REMARK 900 AVIAN RESPIRATORY COMPLEX II WITH OXALOACETATE ANDUBIQUINONE         
REMARK 900 RELATED ID: 2H89   RELATED DB: PDB                                   
REMARK 900 AVIAN RESPIRATORY COMPLEX II WITH MALONATE BOUND                     
REMARK 900 RELATED ID: 2H88   RELATED DB: PDB                                   
REMARK 900 AVIAN MITOCHONDRIAL RESPIRATORY COMPLEX II AT 1.8 ANGSTROMRESOLUTION 
DBREF  2WQY A    1   621  UNP    Q9YHT1   DHSA_CHICK      45    665             
DBREF  2WQY B    1   252  UNP    Q9YHT2   DHSB_CHICK      39    290             
DBREF  2WQY C    1   141  PDB    2WQY     2WQY             1    141             
DBREF  2WQY D    1   103  UNP    Q5ZIS0   DHSD_CHICK      55    157             
DBREF  2WQY N    1   621  UNP    Q9YHT1   DHSA_CHICK      45    665             
DBREF  2WQY O    1   252  UNP    Q9YHT2   DHSB_CHICK      39    290             
DBREF  2WQY P    1   141  PDB    2WQY     2WQY             1    141             
DBREF  2WQY Q    1   103  UNP    Q5ZIS0   DHSD_CHICK      55    157             
SEQADV 2WQY ARG A  501  UNP  Q9YHT1    CYS   545 CONFLICT                       
SEQADV 2WQY LEU A  556  UNP  Q9YHT1    PHE   600 CONFLICT                       
SEQADV 2WQY GLU A  560  UNP  Q9YHT1    ASP   604 CONFLICT                       
SEQADV 2WQY ARG N  501  UNP  Q9YHT1    CYS   545 CONFLICT                       
SEQADV 2WQY LEU N  556  UNP  Q9YHT1    PHE   600 CONFLICT                       
SEQADV 2WQY GLU N  560  UNP  Q9YHT1    ASP   604 CONFLICT                       
SEQRES   1 A  621  SER THR LYS VAL SER ASP SER ILE SER THR GLN TYR PRO          
SEQRES   2 A  621  VAL VAL ASP HIS GLU PHE ASP ALA VAL VAL VAL GLY ALA          
SEQRES   3 A  621  GLY GLY ALA GLY LEU ARG ALA ALA PHE GLY LEU SER GLU          
SEQRES   4 A  621  ALA GLY PHE ASN THR ALA CYS VAL THR LYS LEU PHE PRO          
SEQRES   5 A  621  THR ARG SER HIS THR VAL ALA ALA GLN GLY GLY ILE ASN          
SEQRES   6 A  621  ALA ALA LEU GLY ASN MET GLU ASP ASP ASN TRP ARG TRP          
SEQRES   7 A  621  HIS PHE TYR ASP THR VAL LYS GLY SER ASP TRP LEU GLY          
SEQRES   8 A  621  ASP GLN ASP ALA ILE HIS TYR MET THR GLU GLN ALA PRO          
SEQRES   9 A  621  ALA ALA VAL ILE GLU LEU GLU ASN TYR GLY MET PRO PHE          
SEQRES  10 A  621  SER ARG THR GLU GLU GLY LYS ILE TYR GLN ARG ALA PHE          
SEQRES  11 A  621  GLY GLY GLN SER LEU GLN PHE GLY LYS GLY GLY GLN ALA          
SEQRES  12 A  621  HIS ARG CYS CYS CYS VAL ALA ASP ARG THR GLY HIS SER          
SEQRES  13 A  621  LEU LEU HIS THR LEU TYR GLY ARG SER LEU ARG TYR ASP          
SEQRES  14 A  621  THR SER TYR PHE VAL GLU TYR PHE ALA LEU ASP LEU LEU          
SEQRES  15 A  621  MET GLU ASN GLY GLU CYS ARG GLY VAL ILE ALA LEU CYS          
SEQRES  16 A  621  ILE GLU ASP GLY THR ILE HIS ARG PHE ARG ALA LYS ASN          
SEQRES  17 A  621  THR VAL ILE ALA THR GLY GLY TYR GLY ARG THR TYR PHE          
SEQRES  18 A  621  SER CYS THR SER ALA HIS THR SER THR GLY ASP GLY THR          
SEQRES  19 A  621  ALA MET VAL THR ARG ALA GLY LEU PRO CYS GLN ASP LEU          
SEQRES  20 A  621  GLU PHE VAL GLN PHE HIS PRO THR GLY ILE TYR GLY ALA          
SEQRES  21 A  621  GLY CYS LEU ILE THR GLU GLY CYS ARG GLY GLU GLY GLY          
SEQRES  22 A  621  ILE LEU ILE ASN SER GLN GLY GLU ARG PHE MET GLU ARG          
SEQRES  23 A  621  TYR ALA PRO VAL ALA LYS ASP LEU ALA SER ARG ASP VAL          
SEQRES  24 A  621  VAL SER ARG SER MET THR ILE GLU ILE ARG GLU GLY ARG          
SEQRES  25 A  621  GLY CYS GLY PRO GLU LYS ASP HIS VAL TYR LEU GLN LEU          
SEQRES  26 A  621  HIS HIS LEU PRO PRO GLN GLN LEU ALA THR ARG LEU PRO          
SEQRES  27 A  621  GLY ILE SER GLU THR ALA MET ILE PHE ALA GLY VAL ASP          
SEQRES  28 A  621  VAL THR LYS GLU PRO ILE PRO VAL LEU PRO THR VAL HIS          
SEQRES  29 A  621  TYR ASN MET GLY GLY ILE PRO THR ASN TYR LYS GLY GLN          
SEQRES  30 A  621  VAL ILE THR HIS VAL ASN GLY GLU ASP LYS VAL VAL PRO          
SEQRES  31 A  621  GLY LEU TYR ALA CYS GLY GLU ALA ALA SER ALA SER VAL          
SEQRES  32 A  621  HIS GLY ALA ASN ARG LEU GLY ALA ASN SER LEU LEU ASP          
SEQRES  33 A  621  LEU VAL VAL PHE GLY ARG ALA CYS ALA LEU THR ILE ALA          
SEQRES  34 A  621  GLU THR CYS LYS PRO GLY GLU PRO VAL PRO SER ILE LYS          
SEQRES  35 A  621  PRO ASN ALA GLY GLU GLU SER VAL ALA ASN LEU ASP LYS          
SEQRES  36 A  621  LEU ARG PHE ALA ASP GLY THR ILE ARG THR SER GLU ALA          
SEQRES  37 A  621  ARG LEU ASN MET GLN LYS THR MET GLN SER HIS ALA ALA          
SEQRES  38 A  621  VAL PHE ARG THR GLY SER ILE LEU GLN GLU GLY CYS GLU          
SEQRES  39 A  621  LYS LEU SER GLN ILE TYR ARG ASP LEU ALA HIS LEU LYS          
SEQRES  40 A  621  THR PHE ASP ARG GLY ILE VAL TRP ASN THR ASP LEU VAL          
SEQRES  41 A  621  GLU THR LEU GLU LEU GLN ASN LEU MET LEU CYS ALA LEU          
SEQRES  42 A  621  GLN THR ILE TYR GLY ALA GLU ALA ARG LYS GLU SER ARG          
SEQRES  43 A  621  GLY ALA HIS ALA ARG GLU ASP TYR LYS LEU ARG ILE ASP          
SEQRES  44 A  621  GLU PHE ASP TYR SER LYS PRO LEU GLN GLY GLN GLN LYS          
SEQRES  45 A  621  ARG PRO PHE GLU GLU HIS TRP ARG LYS HIS THR LEU SER          
SEQRES  46 A  621  TYR VAL ASP VAL LYS SER GLY LYS VAL THR LEU LYS TYR          
SEQRES  47 A  621  ARG PRO VAL ILE ASP ARG THR LEU ASN GLU GLU ASP CYS          
SEQRES  48 A  621  SER SER VAL PRO PRO ALA ILE ARG SER TYR                      
SEQRES   1 B  252  ALA GLN THR ALA ALA ALA ALA THR SER ARG ILE LYS LYS          
SEQRES   2 B  252  PHE SER ILE TYR ARG TRP ASP PRO ASP LYS PRO GLY ASP          
SEQRES   3 B  252  LYS PRO ARG MET GLN THR TYR GLU VAL ASP LEU ASN LYS          
SEQRES   4 B  252  CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS ILE LYS          
SEQRES   5 B  252  ASN GLU LEU ASP SER THR LEU THR PHE ARG ARG SER CYS          
SEQRES   6 B  252  ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN ILE ALA          
SEQRES   7 B  252  GLY GLY ASN THR LEU ALA CYS THR LYS LYS ILE ASP PRO          
SEQRES   8 B  252  ASP LEU SER LYS THR THR LYS ILE TYR PRO LEU PRO HIS          
SEQRES   9 B  252  MET TYR VAL VAL LYS ASP LEU VAL PRO ASP LEU SER ASN          
SEQRES  10 B  252  PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR LEU LYS          
SEQRES  11 B  252  LYS LYS ASP GLU SER LYS GLN GLY LYS GLU GLN TYR LEU          
SEQRES  12 B  252  GLN SER ILE GLU ASP ARG GLN LYS LEU ASP GLY LEU TYR          
SEQRES  13 B  252  GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER CYS PRO          
SEQRES  14 B  252  SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY PRO ALA          
SEQRES  15 B  252  VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP SER ARG          
SEQRES  16 B  252  ASP ASP TYR THR GLU GLU ARG LEU ALA GLN LEU GLN ASP          
SEQRES  17 B  252  PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET ASN CYS          
SEQRES  18 B  252  THR ARG THR CYS PRO LYS GLY LEU ASN PRO GLY LYS ALA          
SEQRES  19 B  252  ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR LYS GLU          
SEQRES  20 B  252  LYS ALA ALA ALA ALA                                          
SEQRES   1 C  141  MET ALA THR THR ALA LYS GLU GLU MET ALA ARG PHE TRP          
SEQRES   2 C  141  GLU LYS ASN THR LYS SER SER ARG PRO LEU SER PRO HIS          
SEQRES   3 C  141  ILE SER ILE TYR LYS TRP SER LEU PRO MET ALA MET SER          
SEQRES   4 C  141  ILE THR HIS ARG GLY THR GLY VAL ALA LEU SER LEU GLY          
SEQRES   5 C  141  VAL SER LEU PHE SER VAL ALA ALA LEU LEU LEU PRO GLU          
SEQRES   6 C  141  GLN PHE PRO HIS TYR VAL ALA VAL VAL LYS SER LEU SER          
SEQRES   7 C  141  LEU SER PRO ALA LEU ILE TYR SER ALA LYS PHE ALA LEU          
SEQRES   8 C  141  VAL PHE PRO LEU SER TYR HIS THR TRP ASN GLY ILE ARG          
SEQRES   9 C  141  HIS LEU VAL TRP ASP MET GLY LYS GLY PHE LYS LEU SER          
SEQRES  10 C  141  GLN VAL GLU GLN SER GLY VAL VAL VAL LEU ILE LEU THR          
SEQRES  11 C  141  LEU LEU SER SER ALA GLY ILE ALA ALA ILE SER                  
SEQRES   1 D  103  GLY SER SER LYS ALA ALA SER LEU HIS TRP THR SER GLU          
SEQRES   2 D  103  ARG ALA VAL SER ALA LEU LEU LEU GLY LEU LEU PRO ALA          
SEQRES   3 D  103  ALA TYR LEU TYR PRO GLY PRO ALA VAL ASP TYR SER LEU          
SEQRES   4 D  103  ALA ALA ALA LEU THR LEU HIS GLY HIS TRP GLY LEU GLY          
SEQRES   5 D  103  GLN VAL ILE THR ASP TYR VAL HIS GLY ASP THR PRO ILE          
SEQRES   6 D  103  LYS VAL ALA ASN THR GLY LEU TYR VAL LEU SER ALA ILE          
SEQRES   7 D  103  THR PHE THR GLY LEU CYS TYR PHE ASN TYR TYR ASP VAL          
SEQRES   8 D  103  GLY ILE CYS LYS ALA VAL ALA MET LEU TRP SER ILE              
SEQRES   1 N  621  SER THR LYS VAL SER ASP SER ILE SER THR GLN TYR PRO          
SEQRES   2 N  621  VAL VAL ASP HIS GLU PHE ASP ALA VAL VAL VAL GLY ALA          
SEQRES   3 N  621  GLY GLY ALA GLY LEU ARG ALA ALA PHE GLY LEU SER GLU          
SEQRES   4 N  621  ALA GLY PHE ASN THR ALA CYS VAL THR LYS LEU PHE PRO          
SEQRES   5 N  621  THR ARG SER HIS THR VAL ALA ALA GLN GLY GLY ILE ASN          
SEQRES   6 N  621  ALA ALA LEU GLY ASN MET GLU ASP ASP ASN TRP ARG TRP          
SEQRES   7 N  621  HIS PHE TYR ASP THR VAL LYS GLY SER ASP TRP LEU GLY          
SEQRES   8 N  621  ASP GLN ASP ALA ILE HIS TYR MET THR GLU GLN ALA PRO          
SEQRES   9 N  621  ALA ALA VAL ILE GLU LEU GLU ASN TYR GLY MET PRO PHE          
SEQRES  10 N  621  SER ARG THR GLU GLU GLY LYS ILE TYR GLN ARG ALA PHE          
SEQRES  11 N  621  GLY GLY GLN SER LEU GLN PHE GLY LYS GLY GLY GLN ALA          
SEQRES  12 N  621  HIS ARG CYS CYS CYS VAL ALA ASP ARG THR GLY HIS SER          
SEQRES  13 N  621  LEU LEU HIS THR LEU TYR GLY ARG SER LEU ARG TYR ASP          
SEQRES  14 N  621  THR SER TYR PHE VAL GLU TYR PHE ALA LEU ASP LEU LEU          
SEQRES  15 N  621  MET GLU ASN GLY GLU CYS ARG GLY VAL ILE ALA LEU CYS          
SEQRES  16 N  621  ILE GLU ASP GLY THR ILE HIS ARG PHE ARG ALA LYS ASN          
SEQRES  17 N  621  THR VAL ILE ALA THR GLY GLY TYR GLY ARG THR TYR PHE          
SEQRES  18 N  621  SER CYS THR SER ALA HIS THR SER THR GLY ASP GLY THR          
SEQRES  19 N  621  ALA MET VAL THR ARG ALA GLY LEU PRO CYS GLN ASP LEU          
SEQRES  20 N  621  GLU PHE VAL GLN PHE HIS PRO THR GLY ILE TYR GLY ALA          
SEQRES  21 N  621  GLY CYS LEU ILE THR GLU GLY CYS ARG GLY GLU GLY GLY          
SEQRES  22 N  621  ILE LEU ILE ASN SER GLN GLY GLU ARG PHE MET GLU ARG          
SEQRES  23 N  621  TYR ALA PRO VAL ALA LYS ASP LEU ALA SER ARG ASP VAL          
SEQRES  24 N  621  VAL SER ARG SER MET THR ILE GLU ILE ARG GLU GLY ARG          
SEQRES  25 N  621  GLY CYS GLY PRO GLU LYS ASP HIS VAL TYR LEU GLN LEU          
SEQRES  26 N  621  HIS HIS LEU PRO PRO GLN GLN LEU ALA THR ARG LEU PRO          
SEQRES  27 N  621  GLY ILE SER GLU THR ALA MET ILE PHE ALA GLY VAL ASP          
SEQRES  28 N  621  VAL THR LYS GLU PRO ILE PRO VAL LEU PRO THR VAL HIS          
SEQRES  29 N  621  TYR ASN MET GLY GLY ILE PRO THR ASN TYR LYS GLY GLN          
SEQRES  30 N  621  VAL ILE THR HIS VAL ASN GLY GLU ASP LYS VAL VAL PRO          
SEQRES  31 N  621  GLY LEU TYR ALA CYS GLY GLU ALA ALA SER ALA SER VAL          
SEQRES  32 N  621  HIS GLY ALA ASN ARG LEU GLY ALA ASN SER LEU LEU ASP          
SEQRES  33 N  621  LEU VAL VAL PHE GLY ARG ALA CYS ALA LEU THR ILE ALA          
SEQRES  34 N  621  GLU THR CYS LYS PRO GLY GLU PRO VAL PRO SER ILE LYS          
SEQRES  35 N  621  PRO ASN ALA GLY GLU GLU SER VAL ALA ASN LEU ASP LYS          
SEQRES  36 N  621  LEU ARG PHE ALA ASP GLY THR ILE ARG THR SER GLU ALA          
SEQRES  37 N  621  ARG LEU ASN MET GLN LYS THR MET GLN SER HIS ALA ALA          
SEQRES  38 N  621  VAL PHE ARG THR GLY SER ILE LEU GLN GLU GLY CYS GLU          
SEQRES  39 N  621  LYS LEU SER GLN ILE TYR ARG ASP LEU ALA HIS LEU LYS          
SEQRES  40 N  621  THR PHE ASP ARG GLY ILE VAL TRP ASN THR ASP LEU VAL          
SEQRES  41 N  621  GLU THR LEU GLU LEU GLN ASN LEU MET LEU CYS ALA LEU          
SEQRES  42 N  621  GLN THR ILE TYR GLY ALA GLU ALA ARG LYS GLU SER ARG          
SEQRES  43 N  621  GLY ALA HIS ALA ARG GLU ASP TYR LYS LEU ARG ILE ASP          
SEQRES  44 N  621  GLU PHE ASP TYR SER LYS PRO LEU GLN GLY GLN GLN LYS          
SEQRES  45 N  621  ARG PRO PHE GLU GLU HIS TRP ARG LYS HIS THR LEU SER          
SEQRES  46 N  621  TYR VAL ASP VAL LYS SER GLY LYS VAL THR LEU LYS TYR          
SEQRES  47 N  621  ARG PRO VAL ILE ASP ARG THR LEU ASN GLU GLU ASP CYS          
SEQRES  48 N  621  SER SER VAL PRO PRO ALA ILE ARG SER TYR                      
SEQRES   1 O  252  ALA GLN THR ALA ALA ALA ALA THR SER ARG ILE LYS LYS          
SEQRES   2 O  252  PHE SER ILE TYR ARG TRP ASP PRO ASP LYS PRO GLY ASP          
SEQRES   3 O  252  LYS PRO ARG MET GLN THR TYR GLU VAL ASP LEU ASN LYS          
SEQRES   4 O  252  CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS ILE LYS          
SEQRES   5 O  252  ASN GLU LEU ASP SER THR LEU THR PHE ARG ARG SER CYS          
SEQRES   6 O  252  ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN ILE ALA          
SEQRES   7 O  252  GLY GLY ASN THR LEU ALA CYS THR LYS LYS ILE ASP PRO          
SEQRES   8 O  252  ASP LEU SER LYS THR THR LYS ILE TYR PRO LEU PRO HIS          
SEQRES   9 O  252  MET TYR VAL VAL LYS ASP LEU VAL PRO ASP LEU SER ASN          
SEQRES  10 O  252  PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR LEU LYS          
SEQRES  11 O  252  LYS LYS ASP GLU SER LYS GLN GLY LYS GLU GLN TYR LEU          
SEQRES  12 O  252  GLN SER ILE GLU ASP ARG GLN LYS LEU ASP GLY LEU TYR          
SEQRES  13 O  252  GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER CYS PRO          
SEQRES  14 O  252  SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY PRO ALA          
SEQRES  15 O  252  VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP SER ARG          
SEQRES  16 O  252  ASP ASP TYR THR GLU GLU ARG LEU ALA GLN LEU GLN ASP          
SEQRES  17 O  252  PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET ASN CYS          
SEQRES  18 O  252  THR ARG THR CYS PRO LYS GLY LEU ASN PRO GLY LYS ALA          
SEQRES  19 O  252  ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR LYS GLU          
SEQRES  20 O  252  LYS ALA ALA ALA ALA                                          
SEQRES   1 P  141  MET ALA THR THR ALA LYS GLU GLU MET ALA ARG PHE TRP          
SEQRES   2 P  141  GLU LYS ASN THR LYS SER SER ARG PRO LEU SER PRO HIS          
SEQRES   3 P  141  ILE SER ILE TYR LYS TRP SER LEU PRO MET ALA MET SER          
SEQRES   4 P  141  ILE THR HIS ARG GLY THR GLY VAL ALA LEU SER LEU GLY          
SEQRES   5 P  141  VAL SER LEU PHE SER VAL ALA ALA LEU LEU LEU PRO GLU          
SEQRES   6 P  141  GLN PHE PRO HIS TYR VAL ALA VAL VAL LYS SER LEU SER          
SEQRES   7 P  141  LEU SER PRO ALA LEU ILE TYR SER ALA LYS PHE ALA LEU          
SEQRES   8 P  141  VAL PHE PRO LEU SER TYR HIS THR TRP ASN GLY ILE ARG          
SEQRES   9 P  141  HIS LEU VAL TRP ASP MET GLY LYS GLY PHE LYS LEU SER          
SEQRES  10 P  141  GLN VAL GLU GLN SER GLY VAL VAL VAL LEU ILE LEU THR          
SEQRES  11 P  141  LEU LEU SER SER ALA GLY ILE ALA ALA ILE SER                  
SEQRES   1 Q  103  GLY SER SER LYS ALA ALA SER LEU HIS TRP THR SER GLU          
SEQRES   2 Q  103  ARG ALA VAL SER ALA LEU LEU LEU GLY LEU LEU PRO ALA          
SEQRES   3 Q  103  ALA TYR LEU TYR PRO GLY PRO ALA VAL ASP TYR SER LEU          
SEQRES   4 Q  103  ALA ALA ALA LEU THR LEU HIS GLY HIS TRP GLY LEU GLY          
SEQRES   5 Q  103  GLN VAL ILE THR ASP TYR VAL HIS GLY ASP THR PRO ILE          
SEQRES   6 Q  103  LYS VAL ALA ASN THR GLY LEU TYR VAL LEU SER ALA ILE          
SEQRES   7 Q  103  THR PHE THR GLY LEU CYS TYR PHE ASN TYR TYR ASP VAL          
SEQRES   8 Q  103  GLY ILE CYS LYS ALA VAL ALA MET LEU TRP SER ILE              
HET    UNL  A1003       6                                                       
HET    UNL  A1004       4                                                       
HET      K  A 622       1                                                       
HET    AZI  A 623       3                                                       
HET    FAD  A1001      53                                                       
HET    OAA  A1002       9                                                       
HET    UNL  A1005       1                                                       
HET    UNL  A1006       1                                                       
HET    UNL  A1007       1                                                       
HET    UNL  A1008       1                                                       
HET    UNL  A1009       1                                                       
HET    UNL  A1010       1                                                       
HET    UNL  A1011       1                                                       
HET    UNL  A1012       1                                                       
HET    UNL  A1013       1                                                       
HET    UNL  A1014       1                                                       
HET    UNL  A1015       1                                                       
HET    UNL  A1016       1                                                       
HET    UNL  A1017       1                                                       
HET    UNL  A1018       1                                                       
HET    UNL  A1019       1                                                       
HET    UNL  A1020       1                                                       
HET    UNL  A1021       1                                                       
HET    UNL  A1022       1                                                       
HET    UNL  A1023       1                                                       
HET      K  B 253       1                                                       
HET    UNL  B 258       1                                                       
HET    UNL  B 268       1                                                       
HET    UNL  B 277       1                                                       
HET    UNL  B 280       1                                                       
HET    UNL  B 297       1                                                       
HET    FES  B1002       4                                                       
HET    SF4  B1003       8                                                       
HET    F3S  B1004       7                                                       
HET    UNL  B1005       5                                                       
HET    UNL  B1006       1                                                       
HET    UNL  B1007       1                                                       
HET    UNL  B1008       1                                                       
HET    UNL  B1009       1                                                       
HET    GOL  B1010       6                                                       
HET    BHG  C 142      18                                                       
HET    HEM  C 143      41                                                       
HET    CBE  C 144      16                                                       
HET    UNL  C 145       4                                                       
HET    UNL  C 214       5                                                       
HET    UNL  C 235       1                                                       
HET    UNL  C 240       1                                                       
HET    UNL  C 241       1                                                       
HET    UNL  C 248       1                                                       
HET    UNL  C 251       1                                                       
HET    UNL  C 254       1                                                       
HET    UNL  C 256       1                                                       
HET    UNL  C 259       1                                                       
HET    UNL  C 267       1                                                       
HET    UNL  C 272       1                                                       
HET    UNL  C 289       1                                                       
HET    UNL  C 292       1                                                       
HET    UNL  C 293       1                                                       
HET    GOL  C 294       6                                                       
HET    PEE  D 109      24                                                       
HET    UNL  D 245       1                                                       
HET    UNL  D 247       1                                                       
HET    UNL  D 250       1                                                       
HET    UNL  D 255       1                                                       
HET    UNL  D 262       1                                                       
HET    UNL  D 263       1                                                       
HET    UNL  D 265       1                                                       
HET    UNL  D 266       1                                                       
HET    UNL  D 291       1                                                       
HET      K  N 622       1                                                       
HET    FAD  N1001      53                                                       
HET    OAA  N1002       9                                                       
HET    UNL  N1003       4                                                       
HET    UNL  N1004       1                                                       
HET    UNL  N1005       1                                                       
HET    UNL  N1006       1                                                       
HET    UNL  N1007       1                                                       
HET    UNL  N1008       1                                                       
HET    UNL  N1009       1                                                       
HET    UNL  N1010       1                                                       
HET    UNL  N1011       1                                                       
HET    UNL  N1012       1                                                       
HET    UNL  N1013       1                                                       
HET    UNL  N1014       1                                                       
HET    UNL  N1015       1                                                       
HET    UNL  N1016       1                                                       
HET    UNL  N1017       1                                                       
HET    UNL  N1018       1                                                       
HET    UNL  N1019       1                                                       
HET    UNL  N1020       1                                                       
HET    UNL  N1021       1                                                       
HET    UNL  N1022       1                                                       
HET    UNL  N1023       1                                                       
HET      K  O 253       1                                                       
HET    UNL  O 276       1                                                       
HET    UNL  O 282       1                                                       
HET    FES  O1002       4                                                       
HET    SF4  O1003       8                                                       
HET    F3S  O1004       7                                                       
HET    UNL  O1005       5                                                       
HET    UNL  O1006       1                                                       
HET    UNL  O1007       1                                                       
HET    UNL  O1008       1                                                       
HET    GOL  O1009       6                                                       
HET    HEM  P 201      41                                                       
HET    CBE  P 202      16                                                       
HET    BHG  P 204      18                                                       
HET    GOL  P 208       6                                                       
HET    UNL  P 211       5                                                       
HET    UNL  P 218       1                                                       
HET    UNL  P 224       1                                                       
HET    UNL  P 233       1                                                       
HET    UNL  P 236       1                                                       
HET    UNL  P 274       1                                                       
HET    UNL  P 285       1                                                       
HET    PEE  Q 210      24                                                       
HET    UNL  Q 219       1                                                       
HET    UNL  Q 221       1                                                       
HET    UNL  Q 234       1                                                       
HET    UNL  Q 237       1                                                       
HET    UNL  Q 287       1                                                       
HET    UNL  Q 288       1                                                       
HETNAM     UNL UNKNOWN LIGAND                                                   
HETNAM       K POTASSIUM ION                                                    
HETNAM     AZI AZIDE ION                                                        
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     OAA OXALOACETATE ION                                                 
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     BHG 2-HEXYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL          
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CBE 2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-                   
HETNAM   2 CBE  CARBOXAMIDE                                                     
HETNAM     PEE 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     HEM HEME                                                             
HETSYN     CBE 5,6-DIHYDRO-2-METHYL-1,4-OXATHIIN-3-CARBOXANILID;                
HETSYN   2 CBE  CARBOXIN; CBX                                                   
HETSYN     PEE DOPE                                                             
FORMUL  11    K    4(K 1+)                                                      
FORMUL  12  AZI    N3 1-                                                        
FORMUL  13  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  14  OAA    2(C4 H3 O5 1-)                                               
FORMUL  40  FES    2(FE2 S2)                                                    
FORMUL  41  SF4    2(FE4 S4)                                                    
FORMUL  42  F3S    2(FE3 S4)                                                    
FORMUL  48  GOL    4(C3 H8 O3)                                                  
FORMUL  49  BHG    2(C12 H24 O6)                                                
FORMUL  50  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL  51  CBE    2(C12 H13 N O2 S)                                            
FORMUL  68  PEE    2(C41 H83 N O8 P 1+)                                         
FORMUL  31  HOH   *1996(H2 O)                                                   
HELIX    1   1 GLY A   27  ALA A   40  1                                  14    
HELIX    2   2 PHE A   51  SER A   55  5                                   5    
HELIX    3   3 SER A   55  ALA A   60  5                                   6    
HELIX    4   4 ASN A   75  SER A   87  1                                  13    
HELIX    5   5 ASP A   92  TYR A  113  1                                  22    
HELIX    6   6 ARG A  152  LEU A  166  1                                  15    
HELIX    7   7 TYR A  216  TYR A  220  5                                   5    
HELIX    8   8 GLY A  231  ALA A  240  1                                  10    
HELIX    9   9 GLU A  266  GLU A  271  1                                   6    
HELIX   10  10 PHE A  283  ALA A  288  1                                   6    
HELIX   11  11 ALA A  291  ALA A  295  5                                   5    
HELIX   12  12 SER A  296  GLU A  310  1                                  15    
HELIX   13  13 PRO A  329  LEU A  337  1                                   9    
HELIX   14  14 LEU A  337  GLY A  349  1                                  13    
HELIX   15  15 ASN A  412  GLU A  430  1                                  19    
HELIX   16  16 GLY A  446  PHE A  458  1                                  13    
HELIX   17  17 THR A  465  ALA A  480  1                                  16    
HELIX   18  18 THR A  485  LEU A  503  1                                  19    
HELIX   19  19 ASN A  516  ARG A  542  1                                  27    
HELIX   20  20 PRO A  574  HIS A  578  5                                   5    
HELIX   21  21 ASN B   38  CYS B   40  5                                   3    
HELIX   22  22 MET B   43  LEU B   55  1                                  13    
HELIX   23  23 CYS B   85  LYS B   87  5                                   3    
HELIX   24  24 LEU B  115  ILE B  125  1                                  11    
HELIX   25  25 SER B  145  LYS B  151  1                                   7    
HELIX   26  26 CYS B  164  SER B  167  5                                   4    
HELIX   27  27 CYS B  168  GLY B  175  1                                   8    
HELIX   28  28 GLY B  180  ILE B  192  1                                  13    
HELIX   29  29 TYR B  198  GLN B  205  1                                   8    
HELIX   30  30 MET B  219  CYS B  225  1                                   7    
HELIX   31  31 ASN B  230  TYR B  245  1                                  16    
HELIX   32  32 THR C    4  LYS C   18  1                                  15    
HELIX   33  33 SER C   33  LEU C   63  1                                  31    
HELIX   34  34 GLN C   66  LEU C   77  1                                  12    
HELIX   35  35 SER C   80  MET C  110  1                                  31    
HELIX   36  36 LYS C  115  ALA C  139  1                                  25    
HELIX   37  37 LYS D    4  TYR D   30  1                                  27    
HELIX   38  38 GLY D   32  VAL D   59  1                                  28    
HELIX   39  39 GLY D   61  ASP D   90  1                                  30    
HELIX   40  40 GLY D   92  TRP D  101  1                                  10    
HELIX   41  41 GLY N   27  ALA N   40  1                                  14    
HELIX   42  42 PHE N   51  SER N   55  5                                   5    
HELIX   43  43 SER N   55  ALA N   60  5                                   6    
HELIX   44  44 ASN N   75  SER N   87  1                                  13    
HELIX   45  45 ASP N   92  TYR N  113  1                                  22    
HELIX   46  46 ARG N  152  LEU N  166  1                                  15    
HELIX   47  47 TYR N  216  TYR N  220  5                                   5    
HELIX   48  48 GLY N  231  ALA N  240  1                                  10    
HELIX   49  49 GLU N  266  GLU N  271  1                                   6    
HELIX   50  50 PHE N  283  ALA N  288  1                                   6    
HELIX   51  51 ALA N  291  ALA N  295  5                                   5    
HELIX   52  52 SER N  296  GLU N  310  1                                  15    
HELIX   53  53 PRO N  329  LEU N  337  1                                   9    
HELIX   54  54 LEU N  337  GLY N  349  1                                  13    
HELIX   55  55 ASN N  412  GLU N  430  1                                  19    
HELIX   56  56 GLY N  446  PHE N  458  1                                  13    
HELIX   57  57 THR N  465  ALA N  480  1                                  16    
HELIX   58  58 THR N  485  LEU N  503  1                                  19    
HELIX   59  59 ASN N  516  ARG N  542  1                                  27    
HELIX   60  60 PRO N  574  HIS N  578  5                                   5    
HELIX   61  61 ASN O   38  CYS O   40  5                                   3    
HELIX   62  62 MET O   43  LEU O   55  1                                  13    
HELIX   63  63 CYS O   85  LYS O   87  5                                   3    
HELIX   64  64 LEU O  115  ILE O  125  1                                  11    
HELIX   65  65 SER O  145  LYS O  151  1                                   7    
HELIX   66  66 CYS O  164  SER O  167  5                                   4    
HELIX   67  67 CYS O  168  GLY O  175  1                                   8    
HELIX   68  68 GLY O  180  ILE O  192  1                                  13    
HELIX   69  69 TYR O  198  GLN O  205  1                                   8    
HELIX   70  70 MET O  219  CYS O  225  1                                   7    
HELIX   71  71 ASN O  230  TYR O  245  1                                  16    
HELIX   72  72 THR P    4  LYS P   18  1                                  15    
HELIX   73  73 SER P   33  LEU P   63  1                                  31    
HELIX   74  74 GLN P   66  LEU P   77  1                                  12    
HELIX   75  75 SER P   80  MET P  110  1                                  31    
HELIX   76  76 LYS P  115  ALA P  139  1                                  25    
HELIX   77  77 LYS Q    4  TYR Q   30  1                                  27    
HELIX   78  78 GLY Q   32  VAL Q   59  1                                  28    
HELIX   79  79 GLY Q   61  ASP Q   90  1                                  30    
HELIX   80  80 GLY Q   92  TRP Q  101  1                                  10    
SHEET    1  AA 6 SER A 171  VAL A 174  0                                        
SHEET    2  AA 6 THR A  44  THR A  48  1  O  THR A  44   N  SER A 171           
SHEET    3  AA 6 VAL A  14  VAL A  24  1  O  ALA A  21   N  ALA A  45           
SHEET    4  AA 6 ILE A 201  ILE A 211  1  O  ILE A 201   N  VAL A  15           
SHEET    5  AA 6 GLU A 385  ALA A 394 -1  O  GLY A 391   N  THR A 209           
SHEET    6  AA 6 GLN A 377  VAL A 382  1  O  VAL A 378   N  VAL A 389           
SHEET    1  AB 6 SER A 171  VAL A 174  0                                        
SHEET    2  AB 6 THR A  44  THR A  48  1  O  THR A  44   N  SER A 171           
SHEET    3  AB 6 VAL A  14  VAL A  24  1  O  ALA A  21   N  ALA A  45           
SHEET    4  AB 6 ILE A 201  ILE A 211  1  O  ILE A 201   N  VAL A  15           
SHEET    5  AB 6 GLU A 187  CYS A 195 -1  O  ARG A 189   N  ALA A 206           
SHEET    6  AB 6 TYR A 176  GLU A 184 -1  O  PHE A 177   N  LEU A 194           
SHEET    1  AC 3 ILE A  64  ASN A  65  0                                        
SHEET    2  AC 3 GLN A 142  CYS A 147 -1  O  CYS A 147   N  ILE A  64           
SHEET    3  AC 3 GLN A 127  SER A 134 -1  O  ARG A 128   N  CYS A 146           
SHEET    1  AD 3 CYS A 244  GLN A 245  0                                        
SHEET    2  AD 3 LYS A 581  ASP A 588 -1  O  SER A 585   N  CYS A 244           
SHEET    3  AD 3 LYS A 593  PRO A 600 -1  O  LYS A 593   N  ASP A 588           
SHEET    1  AE 4 VAL A 250  ILE A 257  0                                        
SHEET    2  AE 4 ILE A 357  ASN A 366 -1  O  LEU A 360   N  GLY A 256           
SHEET    3  AE 4 VAL A 321  GLN A 324 -1  O  VAL A 321   N  VAL A 359           
SHEET    4  AE 4 ILE A 274  ILE A 276 -1  O  ILE A 274   N  GLN A 324           
SHEET    1  AF 2 ILE A 370  PRO A 371  0                                        
SHEET    2  AF 2 ALA A 399  SER A 400  1  N  SER A 400   O  ILE A 370           
SHEET    1  AG 2 ILE A 463  ARG A 464  0                                        
SHEET    2  AG 2 LEU A 506  LYS A 507  1  N  LYS A 507   O  ILE A 463           
SHEET    1  BA 5 ARG B  29  ASP B  36  0                                        
SHEET    2  BA 5 ILE B  11  ARG B  18 -1  O  LYS B  12   N  VAL B  35           
SHEET    3  BA 5 THR B  97  TYR B 100  1  O  THR B  97   N  SER B  15           
SHEET    4  BA 5 ALA B  74  ILE B  77 -1  O  ASN B  76   N  TYR B 100           
SHEET    5  BA 5 GLY B  80  LEU B  83 -1  O  GLY B  80   N  ILE B  77           
SHEET    1  BB 2 VAL B 107  LYS B 109  0                                        
SHEET    2  BB 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  VAL B 108           
SHEET    1  NA 4 VAL N  14  GLU N  18  0                                        
SHEET    2  NA 4 ILE N 201  ARG N 205  1  O  ILE N 201   N  VAL N  15           
SHEET    3  NA 4 GLU N 187  CYS N 195 -1  O  VAL N 191   N  PHE N 204           
SHEET    4  NA 4 TYR N 176  GLU N 184 -1  O  PHE N 177   N  LEU N 194           
SHEET    1  NB 6 SER N 171  VAL N 174  0                                        
SHEET    2  NB 6 THR N  44  THR N  48  1  O  THR N  44   N  SER N 171           
SHEET    3  NB 6 ALA N  21  VAL N  24  1  O  ALA N  21   N  ALA N  45           
SHEET    4  NB 6 ASN N 208  ILE N 211  1  O  ASN N 208   N  VAL N  22           
SHEET    5  NB 6 GLU N 385  ALA N 394  1  O  GLY N 391   N  THR N 209           
SHEET    6  NB 6 GLN N 377  VAL N 382 -1  O  VAL N 378   N  VAL N 389           
SHEET    1  NC 3 ILE N  64  ASN N  65  0                                        
SHEET    2  NC 3 GLN N 142  CYS N 147 -1  O  CYS N 147   N  ILE N  64           
SHEET    3  NC 3 GLN N 127  SER N 134 -1  O  ARG N 128   N  CYS N 146           
SHEET    1  ND 3 CYS N 244  GLN N 245  0                                        
SHEET    2  ND 3 LYS N 581  VAL N 587 -1  O  SER N 585   N  CYS N 244           
SHEET    3  ND 3 VAL N 594  PRO N 600 -1  O  THR N 595   N  TYR N 586           
SHEET    1  NE 4 VAL N 250  ILE N 257  0                                        
SHEET    2  NE 4 ILE N 357  ASN N 366 -1  O  LEU N 360   N  GLY N 256           
SHEET    3  NE 4 VAL N 321  GLN N 324 -1  O  VAL N 321   N  VAL N 359           
SHEET    4  NE 4 ILE N 274  ILE N 276 -1  O  ILE N 274   N  GLN N 324           
SHEET    1  NF 2 ILE N 370  PRO N 371  0                                        
SHEET    2  NF 2 ALA N 399  SER N 400  1  N  SER N 400   O  ILE N 370           
SHEET    1  NG 2 ILE N 463  ARG N 464  0                                        
SHEET    2  NG 2 LEU N 506  LYS N 507  1  N  LYS N 507   O  ILE N 463           
SHEET    1  OA 5 ARG O  29  ASP O  36  0                                        
SHEET    2  OA 5 ILE O  11  ARG O  18 -1  O  LYS O  12   N  VAL O  35           
SHEET    3  OA 5 THR O  97  TYR O 100  1  O  THR O  97   N  SER O  15           
SHEET    4  OA 5 ALA O  74  ILE O  77 -1  O  ASN O  76   N  TYR O 100           
SHEET    5  OA 5 GLY O  80  LEU O  83 -1  O  GLY O  80   N  ILE O  77           
SHEET    1  OB 2 VAL O 107  LYS O 109  0                                        
SHEET    2  OB 2 VAL O 112  PRO O 113 -1  O  VAL O 112   N  VAL O 108           
LINK         NE2 HIS A  56                 C8M FAD A1001     1555   1555  1.43  
LINK         K     K A 622                 O   GLU A 397     1555   1555  2.70  
LINK         K     K A 622                 O   ALA A 399     1555   1555  2.81  
LINK         K     K A 622                 OH  TYR A 365     1555   1555  3.35  
LINK         K     K A 622                 O   ASN A 366     1555   1555  2.59  
LINK         K     K A 622                 O   MET A 367     1555   1555  3.08  
LINK         K     K A 622                 O   GLY A 368     1555   1555  2.91  
LINK         K     K B 253                 OG1 THR B 199     1555   1555  2.99  
LINK         K     K B 253                 O   HOH B2245     1555   1555  3.17  
LINK         K     K B 253                 O   HOH B2250     1555   1555  3.31  
LINK         K     K B 253                 O   HOH B2251     1555   1555  3.34  
LINK         K     K B 253                 O   HOH B2244     1555   1555  3.27  
LINK         K     K B 253                 O   ASP B 196     1555   1555  2.94  
LINK         K     K B 253                 O   MET B 191     1555   1555  2.86  
LINK         K     K B 253                 O   HOH B2241     1555   1555  2.96  
LINK         K     K B 253                 O   ASP B 193     1555   1555  2.75  
LINK        FE1  FES B1002                 SG  CYS B  73     1555   1555  2.21  
LINK        FE1  FES B1002                 SG  CYS B  85     1555   1555  2.24  
LINK        FE2  FES B1002                 SG  CYS B  70     1555   1555  2.25  
LINK        FE2  FES B1002                 SG  CYS B  65     1555   1555  2.27  
LINK        FE1  SF4 B1003                 SG  CYS B 164     1555   1555  2.24  
LINK        FE4  SF4 B1003                 SG  CYS B 161     1555   1555  2.27  
LINK        FE3  SF4 B1003                 SG  CYS B 225     1555   1555  2.23  
LINK        FE2  SF4 B1003                 SG  CYS B 158     1555   1555  2.28  
LINK        FE1  F3S B1004                 SG  CYS B 215     1555   1555  2.22  
LINK        FE3  F3S B1004                 SG  CYS B 221     1555   1555  2.29  
LINK        FE4  F3S B1004                 SG  CYS B 168     1555   1555  2.24  
LINK        FE   HEM C 143                 NE2 HIS C  98     1555   1555  1.99  
LINK        FE   HEM C 143                 NE2 HIS D  46     1555   1555  2.01  
LINK         NE2 HIS N  56                 C8M FAD N1001     1555   1555  1.41  
LINK         K     K N 622                 O   ALA N 399     1555   1555  2.80  
LINK         K     K N 622                 O   MET N 367     1555   1555  3.05  
LINK         K     K N 622                 O   ASN N 366     1555   1555  2.55  
LINK         K     K N 622                 OH  TYR N 365     1555   1555  3.43  
LINK         K     K N 622                 O   GLU N 397     1555   1555  2.72  
LINK         K     K N 622                 O   GLY N 368     1555   1555  2.83  
LINK         K     K O 253                 O   HOH O2244     1555   1555  3.29  
LINK         K     K O 253                 O   ASP O 196     1555   1555  2.83  
LINK         K     K O 253                 O   ASP O 193     1555   1555  2.82  
LINK         K     K O 253                 O   HOH O2243     1555   1555  3.01  
LINK         K     K O 253                 OG1 THR O 199     1555   1555  2.95  
LINK         K     K O 253                 O   MET O 191     1555   1555  2.99  
LINK        FE2  FES O1002                 SG  CYS O  70     1555   1555  2.27  
LINK        FE2  FES O1002                 SG  CYS O  65     1555   1555  2.26  
LINK        FE1  FES O1002                 SG  CYS O  85     1555   1555  2.22  
LINK        FE1  FES O1002                 SG  CYS O  73     1555   1555  2.22  
LINK        FE4  SF4 O1003                 SG  CYS O 161     1555   1555  2.27  
LINK        FE3  SF4 O1003                 SG  CYS O 225     1555   1555  2.24  
LINK        FE2  SF4 O1003                 SG  CYS O 158     1555   1555  2.23  
LINK        FE1  SF4 O1003                 SG  CYS O 164     1555   1555  2.22  
LINK        FE4  F3S O1004                 SG  CYS O 168     1555   1555  2.19  
LINK        FE3  F3S O1004                 SG  CYS O 221     1555   1555  2.25  
LINK        FE1  F3S O1004                 SG  CYS O 215     1555   1555  2.26  
LINK        FE   HEM P 201                 NE2 HIS Q  46     1555   1555  2.00  
LINK        FE   HEM P 201                 NE2 HIS P  98     1555   1555  2.00  
CISPEP   1 ALA A  401    SER A  402          0        -2.44                     
CISPEP   2 ALA N  401    SER N  402          0        -2.36                     
SITE     1 AC1  8 LYS C  31  TRP C  32  LEU C  34  PRO C  35                    
SITE     2 AC1  8 GLU C 120  HOH C2046  HOH C2095  TYR P  85                    
SITE     1 AC2  8 ALA C 139  TRP P  32  LEU P  34  PRO P  35                    
SITE     2 AC2  8 GLU P 120  HOH P2039  HOH P2079  HOH P2080                    
SITE     1 AC3  6 TYR A 365  ASN A 366  MET A 367  GLY A 368                    
SITE     2 AC3  6 GLU A 397  ALA A 399                                          
SITE     1 AC4  5 MET B 191  ASP B 193  ASP B 196  THR B 199                    
SITE     2 AC4  5 HOH B2241                                                     
SITE     1 AC5  6 TYR N 365  ASN N 366  MET N 367  GLY N 368                    
SITE     2 AC5  6 GLU N 397  ALA N 399                                          
SITE     1 AC6  5 MET O 191  ASP O 193  ASP O 196  THR O 199                    
SITE     2 AC6  5 HOH O2243                                                     
SITE     1 AC7  3 TYR A 172  VAL A 174  HOH A2540                               
SITE     1 AC8 40 VAL A  24  GLY A  25  ALA A  26  GLY A  27                    
SITE     2 AC8 40 GLY A  28  ALA A  29  THR A  48  LYS A  49                    
SITE     3 AC8 40 LEU A  50  SER A  55  HIS A  56  THR A  57                    
SITE     4 AC8 40 ALA A  59  ALA A  60  GLN A  61  GLY A  62                    
SITE     5 AC8 40 GLY A  63  TYR A 176  PHE A 177  ALA A 178                    
SITE     6 AC8 40 ALA A 212  THR A 213  THR A 224  ASP A 232                    
SITE     7 AC8 40 LEU A 263  HIS A 364  TYR A 365  GLY A 396                    
SITE     8 AC8 40 GLU A 397  ARG A 408  ALA A 411  ASN A 412                    
SITE     9 AC8 40 SER A 413  LEU A 414  LEU A 417  OAA A1002                    
SITE    10 AC8 40 HOH A2256  HOH A2368  HOH A2370  HOH A2542                    
SITE     1 AC9  8 SER B  64  CYS B  65  ARG B  66  GLY B  68                    
SITE     2 AC9  8 CYS B  70  GLY B  71  CYS B  73  CYS B  85                    
SITE     1 BC1  8 CYS B 158  ILE B 159  CYS B 161  ALA B 162                    
SITE     2 BC1  8 CYS B 164  CYS B 225  PRO B 226  LYS B 227                    
SITE     1 BC2 10 CYS B 168  TYR B 178  CYS B 215  HIS B 216                    
SITE     2 BC2 10 THR B 217  ILE B 218  MET B 219  ASN B 220                    
SITE     3 BC2 10 CYS B 221  ILE B 235                                          
SITE     1 BC3 40 GLY N  25  ALA N  26  GLY N  27  GLY N  28                    
SITE     2 BC3 40 ALA N  29  THR N  48  LYS N  49  LEU N  50                    
SITE     3 BC3 40 SER N  55  HIS N  56  THR N  57  ALA N  59                    
SITE     4 BC3 40 ALA N  60  GLN N  61  GLY N  62  GLY N  63                    
SITE     5 BC3 40 TYR N 176  PHE N 177  ALA N 178  ALA N 212                    
SITE     6 BC3 40 THR N 213  THR N 224  ASP N 232  LEU N 263                    
SITE     7 BC3 40 HIS N 364  TYR N 365  GLY N 396  GLU N 397                    
SITE     8 BC3 40 ARG N 408  ALA N 411  ASN N 412  SER N 413                    
SITE     9 BC3 40 LEU N 414  LEU N 417  OAA N1002  HOH N2015                    
SITE    10 BC3 40 HOH N2551  HOH N2552  HOH N2553  HOH N2554                    
SITE     1 BC4  8 SER O  64  CYS O  65  ARG O  66  GLY O  68                    
SITE     2 BC4  8 CYS O  70  GLY O  71  CYS O  73  CYS O  85                    
SITE     1 BC5  7 CYS O 158  ILE O 159  CYS O 161  ALA O 162                    
SITE     2 BC5  7 CYS O 164  CYS O 225  PRO O 226                               
SITE     1 BC6 10 CYS O 168  TYR O 178  CYS O 215  HIS O 216                    
SITE     2 BC6 10 THR O 217  ILE O 218  MET O 219  ASN O 220                    
SITE     3 BC6 10 CYS O 221  ILE O 235                                          
SITE     1 BC7 16 HIS C  42  ARG C  43  GLY C  46  LEU C  49                    
SITE     2 BC7 16 SER C  50  HIS C  98  GLY C 102  HIS C 105                    
SITE     3 BC7 16 HOH C2096  HOH C2097  HOH C2098  ARG D  14                    
SITE     4 BC7 16 LEU D  20  LEU D  43  HIS D  46  GLY D  50                    
SITE     1 BC8 10 SER B 170  TRP B 173  HIS B 216  MET C  36                    
SITE     2 BC8 10 SER C  39  ILE C  40  ARG C  43  HOH C2102                    
SITE     3 BC8 10 ASP D  57  TYR D  58                                          
SITE     1 BC9 11 GLY A  62  HIS A 253  LEU A 263  THR A 265                    
SITE     2 BC9 11 GLU A 266  ARG A 297  HIS A 364  ARG A 408                    
SITE     3 BC9 11 GLY A 410  ALA A 411  FAD A1001                               
SITE     1 CC1  4 GOL C 294  ALA D  27  TYR D  28  TRP D 101                    
SITE     1 CC2 16 HOH O2262  HIS P  42  ARG P  43  GLY P  46                    
SITE     2 CC2 16 LEU P  49  SER P  50  HIS P  98  GLY P 102                    
SITE     3 CC2 16 HIS P 105  HOH P2064  HOH P2078  ARG Q  14                    
SITE     4 CC2 16 LEU Q  20  LEU Q  43  HIS Q  46  GLY Q  50                    
SITE     1 CC3 10 SER O 170  TRP O 173  HIS O 216  MET P  36                    
SITE     2 CC3 10 SER P  39  ILE P  40  ARG P  43  HOH P2082                    
SITE     3 CC3 10 ASP Q  57  TYR Q  58                                          
SITE     1 CC4 11 GLY N  62  HIS N 253  LEU N 263  THR N 265                    
SITE     2 CC4 11 GLU N 266  ARG N 297  HIS N 364  ARG N 408                    
SITE     3 CC4 11 GLY N 410  ALA N 411  FAD N1001                               
SITE     1 CC5  5 SER P 141  GOL P 208  ALA Q  27  VAL Q  97                    
SITE     2 CC5  5 TRP Q 101                                                     
SITE     1 CC6  3 PHE C  56  ILE D  93  PEE D 109                               
SITE     1 CC7  9 HIS B 104  MET B 105  TYR B 171  HOH B2155                    
SITE     2 CC7  9 HOH B2225  HOH B2226  HOH B2296  HOH B2297                    
SITE     3 CC7  9 TRP C  13                                                     
SITE     1 CC8 10 HIS O 104  MET O 105  GLY O 175  HOH O2226                    
SITE     2 CC8 10 HOH O2227  HOH O2228  HOH O2286  HOH O2287                    
SITE     3 CC8 10 PHE P  12  TRP P  13                                          
SITE     1 CC9  2 LEU P  91  PEE Q 210                                          
CRYST1  118.700  200.753   67.631  90.00  90.06  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      0.008425  0.000000  0.000009        0.00000                         
SCALE2      0.000000  0.004981  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014786        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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