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Database: PDB
Entry: 2FBW
LinkDB: 2FBW
Original site: 2FBW 
HEADER    OXIDOREDUCTASE                          10-DEC-05   2FBW              
TITLE     AVIAN RESPIRATORY COMPLEX II WITH CARBOXIN BOUND                      
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 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    COMPLEX II, MEMBRANE PROTEIN, HEME PROTEIN, IRON SULFUR PROTEIN,      
KEYWDS   2 CYTOCHROME B, OXIDOREDUCTASE, REDOX ENZYME, RESPIRATORY CHAIN,       
KEYWDS   3 OXALOACETATE NITROPROPIONATE UBIQUINONE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.S.HUANG,G.SUN,D.COBESSI,A.C.WANG,J.T.SHEN,E.Y.TUNG,V.E.ANDERSON,    
AUTHOR   2 E.A.BERRY                                                            
REVDAT   6   29-OCT-14 2FBW    1       HETNAM                                   
REVDAT   5   13-JUL-11 2FBW    1       VERSN                                    
REVDAT   4   31-MAR-09 2FBW    1       ATOM   CONECT                            
REVDAT   3   24-FEB-09 2FBW    1       VERSN                                    
REVDAT   2   04-APR-06 2FBW    1       JRNL                                     
REVDAT   1   20-DEC-05 2FBW    0                                                
JRNL        AUTH   L.S.HUANG,G.SUN,D.COBESSI,A.C.WANG,J.T.SHEN,E.Y.TUNG,        
JRNL        AUTH 2 V.E.ANDERSON,E.A.BERRY                                       
JRNL        TITL   3-NITROPROPIONIC ACID IS A SUICIDE INHIBITOR OF              
JRNL        TITL 2 MITOCHONDRIAL RESPIRATION THAT, UPON OXIDATION BY COMPLEX    
JRNL        TITL 3 II, FORMS A COVALENT ADDUCT WITH A CATALYTIC BASE ARGININE   
JRNL        TITL 4 IN THE ACTIVE SITE OF THE ENZYME.                            
JRNL        REF    J.BIOL.CHEM.                  V. 281  5965 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16371358                                                     
JRNL        DOI    10.1074/JBC.M511270200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.S.HUANG,T.M.BORDERS,J.T.SHEN,C.J.WANG,E.A.BERRY            
REMARK   1  TITL   CRYSTALLIZATION OF MITOCHONDRIAL RESPIRATORY COMPLEX II FROM 
REMARK   1  TITL 2 CHICKEN HEART: A MEMBRANE-PROTEIN COMPLEX DIFFRACTING TO 2.0 
REMARK   1  TITL 3 A                                                            
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  61   380 2005              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   F.SUN,X.HUO,Y.ZHAI,A.WANG,J.XU,D.SU,M.BARTLAM,Z.RAO          
REMARK   1  TITL   CRYSTAL STRUCTURE OF MITOCHONDRIAL RESPIRATORY MEMBRANE      
REMARK   1  TITL 2 PROTEIN COMPLEX II.                                          
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V. 121  1043 2005              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3447934.670                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 162208                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8009                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6353                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2770                       
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 332                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
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            : 2000                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.06000                                             
REMARK   3    B22 (A**2) : 6.84000                                              
REMARK   3    B33 (A**2) : -3.78000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.30                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.022                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.900                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.700                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.150                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.390 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.150 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.920 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.080 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 100.01                                               
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : SQRPROSTH5.PAR                                 
REMARK   3  PARAMETER FILE  3  : FAD5.PAR                                       
REMARK   3  PARAMETER FILE  4  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  5  : MORE.PAR                                       
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: STRONG NCS RESTRAINTS WERE USED IN        
REMARK   3  POSITIONAL REFINEMENT. THE NCS IS IMPROPER, CORRESPONDING TO A 2-   
REMARK   3  FOLD AXIS PARALLEL TO C WITH A SCREW COMPONENT OF ~3.1 ANGSTROMS.   
REMARK   3  THE COMPLEX WAS DIVIDED INTO 12 TWO-FOLD NCS GROUPS. SPECIFIC       
REMARK   3  RESIDUES NOT OBEYING NCS WERE IDENTIFIED AND RELEASED FROM THE      
REMARK   3  RESTRAINT. NO NCS RESTRAINT ON B-FACTOR WAS USED.                   
REMARK   4                                                                      
REMARK   4 2FBW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035694.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9800                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 166966                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.19200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 49.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.51800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.160                              
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: LOW COMPLETENESS IN OUTER SHELLS IS DUE TO DETECTOR          
REMARK 200  GEOMETRY WHICH WAS A COMPROMISE BETWEEN RESOLVING SPOTS AND         
REMARK 200  COLLECTING HIGH RESOLUTION DATA. OPTICAL RESOLUTION FOR THE         
REMARK 200  DATASET: 1.63 A                                                     
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 300 REMARK: THE BIOLOGICAL UNIT IS BELIEVED TO BE A SINGLE               
REMARK 300 HETROTETRAMER. THE DEPOSITED COORDINATES CONSTITUTE THE ASYMMETRIC   
REMARK 300 UNIT WHICH CONSISTS OF TWO BIOLOGICAL UNITS, ONE COMPRISING CHAINS   
REMARK 300 A,B,C AND D AND THE OTHER COMPRISING CHAINS N,O,P AND Q. LIGANDS     
REMARK 300 WITH RESIDUE NUMBER 100-199 ARE ASSOCIATED WITH [ABCD] WHILE THOSE   
REMARK 300 WITH RESIDUE NUMBERS 200-299 ARE ASSOCIATED WITH [NOPQ] OR OCCUPY    
REMARK 300 ASYMMETRIC POSITIONS. THE OPERATOR TAKING [ABCD] ONTO [NOPQ] IS      
REMARK 300 GIVEN IN THE MTRIX1 ENTRIES. MTRIX1 1 -0.999997 0.001496 -0.0019022  
REMARK 300 59.287878 1 MTRIX1 1 -0.001500 -0.999996 0.0025438 0.332060 1        
REMARK 300 MTRIX1 1 -0.001898 0.002547 0.9999950 -3.116521 1                    
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 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 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  1552              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  -  NH1 ANGL. DEV. =   3.0 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       91.96   -172.53                                   
REMARK 500    SER B  64      -61.47   -153.51                                   
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     -166.05   -100.68                                   
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   -145.07                                   
REMARK 500    ALA N 481     -157.32    -92.75                                   
REMARK 500    ASN N 607       90.81   -172.53                                   
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR B 213        24.7      L          L   OUTSIDE RANGE           
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 B2346        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH B2447        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH C2175        DISTANCE =  8.11 ANGSTROMS                       
REMARK 525    HOH C2263        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH C2284        DISTANCE =  8.28 ANGSTROMS                       
REMARK 525    HOH D2002        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH D2527        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH N1149        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH P1436        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH P1456        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH Q1644        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH Q1664        DISTANCE =  6.78 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                             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  65   SG                                                     
REMARK 620 2 FES B1002   S1  114.4                                              
REMARK 620 3 FES B1002   S2  105.7 101.1                                        
REMARK 620 4 CYS B  70   SG  104.4 114.8 116.4                                  
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  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                             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  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                             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                             FES O1002  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O  73   SG                                                     
REMARK 620 2 FES O1002   S1  109.7                                              
REMARK 620 3 FES O1002   S2  119.5 100.3                                        
REMARK 620 4 CYS O  85   SG  105.3 119.9 102.8                                  
REMARK 620 N                    1     2     3                                   
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  65   SG                                                     
REMARK 620 2 FES O1002   S1  117.6                                              
REMARK 620 3 FES O1002   S2  105.9  99.9                                        
REMARK 620 4 CYS O  70   SG  104.6 113.9 115.0                                  
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  118.5  99.6 105.2                                  
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  122.0                                              
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  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  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                             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                             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  116.2 100.6                                        
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  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                             HEM P 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P  98   NE2                                                    
REMARK 620 2 HEM P 201   NA   90.1                                              
REMARK 620 3 HEM P 201   NB   90.4  88.1                                        
REMARK 620 4 HEM P 201   NC   90.4 179.4  91.5                                  
REMARK 620 5 HEM P 201   ND   91.2  92.4 178.3  87.9                            
REMARK 620 6 HIS Q  46   NE2 178.9  90.4  90.6  89.1  87.8                      
REMARK 620 N                    1     2     3     4     5                       
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 ASN A 366   O                                                      
REMARK 620 2 GLY A 368   O    74.1                                              
REMARK 620 3 GLU A 397   O    95.4  82.3                                        
REMARK 620 4 ALA A 399   O   163.9  90.2  86.0                                  
REMARK 620 5 MET A 367   O    79.0  67.0 149.3  91.5                            
REMARK 620 6 TYR A 365   OH   77.6 151.6 102.3 117.9 105.9                      
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 MET B 191   O                                                      
REMARK 620 2 ASP B 193   O   101.9                                              
REMARK 620 3 ASP B 196   O   139.6  83.1                                        
REMARK 620 4 THR B 199   OG1  70.5 157.5  89.6                                  
REMARK 620 5 HOH B1900   O    93.1  78.0 126.8 122.7                            
REMARK 620 6 HOH B1795   O    63.1 105.0  76.8  52.5 156.2                      
REMARK 620 7 HOH B1777   O   149.1  87.0  70.3 110.6  59.6 143.3                
REMARK 620 8 HOH B2905   O   101.1 134.2 103.4  68.2  61.8 120.7  55.0          
REMARK 620 9 HOH B1861   O   118.1 137.3  57.1  48.0 112.1  82.1  66.7  54.3    
REMARK 620 N                    1     2     3     4     5     6     7     8     
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 ASN N 366   O                                                      
REMARK 620 2 GLY N 368   O    75.7                                              
REMARK 620 3 GLU N 397   O    95.7  84.1                                        
REMARK 620 4 ALA N 399   O   166.1  90.8  86.2                                  
REMARK 620 5 MET N 367   O    80.1  68.1 152.0  91.8                            
REMARK 620 6 TYR N 365   OH   76.9 152.5 101.0 116.4 104.9                      
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 MET O 191   O                                                      
REMARK 620 2 ASP O 193   O    96.1                                              
REMARK 620 3 ASP O 196   O   137.4  83.8                                        
REMARK 620 4 THR O 199   OG1  69.5 153.5  92.1                                  
REMARK 620 5 HOH O1041   O   139.4 118.0  71.8  85.0                            
REMARK 620 6 HOH O1049   O    59.9  99.1  78.0  54.6 128.0                      
REMARK 620 N                    1     2     3     4     5                       
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 TEO 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 UNL C 145                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM P 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE P 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO N 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE Q 210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL P 211                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL N 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL O 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 214                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL B 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL N 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL P 224                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL N 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL N 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL O 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 240                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL D 245                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL B 258                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL B 268                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL B 277                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL B 280                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL Q 288                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 289                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL N 1017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL N 1019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL N 1020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL N 1021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL N 1022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 1023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL O 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
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: 1YQ3   RELATED DB: PDB                                   
REMARK 900 ANOTHER CRYSTAL FORM                                                 
REMARK 900 RELATED ID: 1YQ4   RELATED DB: PDB                                   
REMARK 900 OTHER CRYSTAL FORM, WITH 3-NITROPROPIONIC ACID BOUND                 
REMARK 900 RELATED ID: 1ZOY   RELATED DB: PDB                                   
REMARK 900 PORCINE HOMOLOG                                                      
REMARK 900 RELATED ID: 1ZPO   RELATED DB: PDB                                   
REMARK 900 PORCINE HOMOLOG WITH 3-NPA AND THENOYL TRIFLUOROACETONE              
REMARK 900 BOUND                                                                
REMARK 900 RELATED ID: 1NEK   RELATED DB: PDB                                   
REMARK 900 E.COLI HOMOLOG                                                       
REMARK 900 RELATED ID: 1QJD   RELATED DB: PDB                                   
REMARK 900 FLAVOCYTOCHROME C3 HAS SIMILAR FAD DOMAIN, DICARBOXYLATE             
REMARK 900 BINDING SITE                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE 1-71 OF SUCCINATE DEHYDROGENASE FP SUBUNIT DO NOT           
REMARK 999 MATCH TO ANY OF THE DATABASE SEQUENCE.                               
REMARK 999 THE SEQUENCE OF SUCCINATE DEHYDROGENASE CYTOCHROME B, LARGE          
REMARK 999 SUBUNIT IS NOT AVAILABLE IN ANY OF THE DATABASE SEQUENCE AT          
REMARK 999 THE TIME OF PROCESSING.                                              
REMARK 999 THE DENSITY FOR RESIDUE 58 CHAINS C,P IS NOT QUITE CLEAR.            
REMARK 999 OUR BEST INFORMATION ON THE SEQUENCE INDICATES IT SHOULD             
REMARK 999 BE LEU BUT THE DENSITY FITS VAL SOMEWHAT BETTER.                     
DBREF  2FBW A   71   621  GB     50736125 XP_419054        1    551             
DBREF  2FBW N   71   621  GB     50736125 XP_419054        1    551             
DBREF  2FBW B    1   252  GB     3851612  AAC72372        39    290             
DBREF  2FBW O    1   252  GB     3851612  AAC72372        39    290             
DBREF  2FBW D    1   103  GB     53134884 CAG32373        55    157             
DBREF  2FBW Q    1   103  GB     53134884 CAG32373        55    157             
DBREF  2FBW C    1   141  PDB    2FBW     2FBW             1    141             
DBREF  2FBW P    1   141  PDB    2FBW     2FBW             1    141             
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    BHG  C 142      18                                                       
HET    BHG  P 204      18                                                       
HET      K  A 622       1                                                       
HET      K  B 253       1                                                       
HET      K  N 622       1                                                       
HET      K  O 253       1                                                       
HET    AZI  A 623       3                                                       
HET    FAD  A1001      53                                                       
HET    FES  B1002       4                                                       
HET    SF4  B1003       8                                                       
HET    F3S  B1004       7                                                       
HET    FAD  N1001      53                                                       
HET    FES  O1002       4                                                       
HET    SF4  O1003       8                                                       
HET    F3S  O1004       7                                                       
HET    HEM  C 143      41                                                       
HET    CBE  C 144      16                                                       
HET    TEO  A1002       9                                                       
HET    PEE  D 109      24                                                       
HET    UNL  C 145       4                                                       
HET    HEM  P 201      41                                                       
HET    CBE  P 202      16                                                       
HET    TEO  N1002       9                                                       
HET    PEE  Q 210      24                                                       
HET    UNL  P 211       5                                                       
HET    UNL  N1003       4                                                       
HET    UNL  O1005       5                                                       
HET    UNL  C 214       5                                                       
HET    UNL  B1005       5                                                       
HET    UNL  A1003       6                                                       
HET    UNL  A1004       4                                                       
HET    UNL  P 218       1                                                       
HET    UNL  Q 219       1                                                       
HET    UNL  N1004       1                                                       
HET    UNL  Q 221       1                                                       
HET    UNL  N1005       1                                                       
HET    UNL  N1006       1                                                       
HET    UNL  P 224       1                                                       
HET    UNL  N1007       1                                                       
HET    UNL  N1008       1                                                       
HET    UNL  O1006       1                                                       
HET    UNL  N1009       1                                                       
HET    UNL  N1010       1                                                       
HET    UNL  N1011       1                                                       
HET    UNL  N1012       1                                                       
HET    UNL  O1007       1                                                       
HET    UNL  P 233       1                                                       
HET    UNL  Q 234       1                                                       
HET    UNL  C 235       1                                                       
HET    UNL  P 236       1                                                       
HET    UNL  Q 237       1                                                       
HET    UNL  N1013       1                                                       
HET    UNL  O1008       1                                                       
HET    UNL  C 240       1                                                       
HET    UNL  C 241       1                                                       
HET    UNL  B1006       1                                                       
HET    UNL  A1005       1                                                       
HET    UNL  A1006       1                                                       
HET    UNL  D 245       1                                                       
HET    UNL  A1007       1                                                       
HET    UNL  D 247       1                                                       
HET    UNL  C 248       1                                                       
HET    UNL  B1007       1                                                       
HET    UNL  D 250       1                                                       
HET    UNL  C 251       1                                                       
HET    UNL  B1008       1                                                       
HET    UNL  B1009       1                                                       
HET    UNL  C 254       1                                                       
HET    UNL  D 255       1                                                       
HET    UNL  C 256       1                                                       
HET    UNL  A1008       1                                                       
HET    UNL  B 258       1                                                       
HET    UNL  C 259       1                                                       
HET    UNL  A1009       1                                                       
HET    UNL  A1010       1                                                       
HET    UNL  D 262       1                                                       
HET    UNL  D 263       1                                                       
HET    UNL  A1011       1                                                       
HET    UNL  D 265       1                                                       
HET    UNL  D 266       1                                                       
HET    UNL  C 267       1                                                       
HET    UNL  B 268       1                                                       
HET    UNL  A1012       1                                                       
HET    UNL  A1013       1                                                       
HET    UNL  A1014       1                                                       
HET    UNL  C 272       1                                                       
HET    UNL  A1015       1                                                       
HET    UNL  P 274       1                                                       
HET    UNL  A1016       1                                                       
HET    UNL  O 276       1                                                       
HET    UNL  B 277       1                                                       
HET    UNL  A1017       1                                                       
HET    UNL  A1018       1                                                       
HET    UNL  B 280       1                                                       
HET    UNL  N1014       1                                                       
HET    UNL  O 282       1                                                       
HET    UNL  A1019       1                                                       
HET    UNL  N1015       1                                                       
HET    UNL  P 285       1                                                       
HET    UNL  N1016       1                                                       
HET    UNL  Q 287       1                                                       
HET    UNL  Q 288       1                                                       
HET    UNL  C 289       1                                                       
HET    UNL  N1017       1                                                       
HET    UNL  D 291       1                                                       
HET    UNL  C 292       1                                                       
HET    UNL  C 293       1                                                       
HET    UNL  N1018       1                                                       
HET    UNL  N1019       1                                                       
HET    UNL  N1020       1                                                       
HET    UNL  B 297       1                                                       
HET    UNL  N1021       1                                                       
HET    UNL  A1020       1                                                       
HET    UNL  A1021       1                                                       
HET    UNL  A1022       1                                                       
HET    UNL  N1022       1                                                       
HET    UNL  A1023       1                                                       
HET    UNL  N1023       1                                                       
HET    GOL  C 294       6                                                       
HET    GOL  B1010       6                                                       
HET    GOL  O1009       6                                                       
HET    GOL  P 208       6                                                       
HETNAM     BHG 2-HEXYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL          
HETNAM       K POTASSIUM ION                                                    
HETNAM     AZI AZIDE ION                                                        
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CBE 2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-                   
HETNAM   2 CBE  CARBOXAMIDE                                                     
HETNAM     TEO MALATE LIKE INTERMEDIATE                                         
HETNAM     PEE 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE                    
HETNAM     UNL UNKNOWN LIGAND                                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     HEM HEME                                                             
HETSYN     CBE 5,6-DIHYDRO-2-METHYL-1,4-OXATHIIN-3-CARBOXANILID;                
HETSYN   2 CBE  CARBOXIN; CBX                                                   
HETSYN     PEE DOPE                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9  BHG    2(C12 H24 O6)                                                
FORMUL  11    K    4(K 1+)                                                      
FORMUL  15  AZI    N3 1-                                                        
FORMUL  16  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  17  FES    2(FE2 S2)                                                    
FORMUL  18  SF4    2(FE4 S4)                                                    
FORMUL  19  F3S    2(FE3 S4)                                                    
FORMUL  24  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL  25  CBE    2(C12 H13 N O2 S)                                            
FORMUL  26  TEO    2(C4 H4 O5 2-)                                               
FORMUL  27  PEE    2(C41 H83 N O8 P 1+)                                         
FORMUL  27  GOL    4(C3 H8 O3)                                                  
FORMUL  31  HOH   *2000(H2 O)                                                   
HELIX    1   1 GLY A   27  ALA A   40  1                                  14    
HELIX    2   2 PHE A   51  ALA A   60  5                                  10    
HELIX    3   3 ASN A   75  SER A   87  1                                  13    
HELIX    4   4 ASP A   92  TYR A  113  1                                  22    
HELIX    5   5 ARG A  152  LEU A  166  1                                  15    
HELIX    6   6 TYR A  216  TYR A  220  5                                   5    
HELIX    7   7 GLY A  231  ALA A  240  1                                  10    
HELIX    8   8 GLU A  266  GLU A  271  1                                   6    
HELIX    9   9 PHE A  283  ALA A  288  1                                   6    
HELIX   10  10 ALA A  291  ALA A  295  5                                   5    
HELIX   11  11 SER A  296  GLU A  310  1                                  15    
HELIX   12  12 PRO A  329  LEU A  337  1                                   9    
HELIX   13  13 LEU A  337  GLY A  349  1                                  13    
HELIX   14  14 ASN A  412  GLU A  430  1                                  19    
HELIX   15  15 GLY A  446  PHE A  458  1                                  13    
HELIX   16  16 THR A  465  ALA A  480  1                                  16    
HELIX   17  17 THR A  485  LEU A  503  1                                  19    
HELIX   18  18 ASN A  516  ARG A  542  1                                  27    
HELIX   19  19 PRO A  574  HIS A  578  5                                   5    
HELIX   20  20 ASN B   38  CYS B   40  5                                   3    
HELIX   21  21 MET B   43  LEU B   55  1                                  13    
HELIX   22  22 CYS B   85  LYS B   87  5                                   3    
HELIX   23  23 LEU B  115  ILE B  125  1                                  11    
HELIX   24  24 SER B  145  LYS B  151  1                                   7    
HELIX   25  25 CYS B  164  SER B  167  5                                   4    
HELIX   26  26 CYS B  168  GLY B  175  1                                   8    
HELIX   27  27 GLY B  180  ILE B  192  1                                  13    
HELIX   28  28 TYR B  198  GLN B  205  1                                   8    
HELIX   29  29 MET B  219  CYS B  225  1                                   7    
HELIX   30  30 ASN B  230  TYR B  245  1                                  16    
HELIX   31  31 THR C    4  LYS C   18  1                                  15    
HELIX   32  32 SER C   33  LEU C   63  1                                  31    
HELIX   33  33 GLN C   66  LEU C   77  1                                  12    
HELIX   34  34 SER C   80  MET C  110  1                                  31    
HELIX   35  35 LYS C  115  ALA C  139  1                                  25    
HELIX   36  36 LYS D    4  TYR D   30  1                                  27    
HELIX   37  37 GLY D   32  VAL D   59  1                                  28    
HELIX   38  38 GLY D   61  ASP D   90  1                                  30    
HELIX   39  39 GLY D   92  TRP D  101  1                                  10    
HELIX   40  40 GLY N   27  ALA N   40  1                                  14    
HELIX   41  41 PHE N   51  ALA N   60  5                                  10    
HELIX   42  42 ASN N   75  SER N   87  1                                  13    
HELIX   43  43 ASP N   92  TYR N  113  1                                  22    
HELIX   44  44 ARG N  152  LEU N  166  1                                  15    
HELIX   45  45 TYR N  216  TYR N  220  5                                   5    
HELIX   46  46 GLY N  231  ALA N  240  1                                  10    
HELIX   47  47 GLU N  266  GLU N  271  1                                   6    
HELIX   48  48 PHE N  283  ALA N  288  1                                   6    
HELIX   49  49 ALA N  291  ALA N  295  5                                   5    
HELIX   50  50 SER N  296  GLU N  310  1                                  15    
HELIX   51  51 PRO N  329  LEU N  337  1                                   9    
HELIX   52  52 LEU N  337  GLY N  349  1                                  13    
HELIX   53  53 ASN N  412  GLU N  430  1                                  19    
HELIX   54  54 GLY N  446  PHE N  458  1                                  13    
HELIX   55  55 THR N  465  ALA N  480  1                                  16    
HELIX   56  56 THR N  485  LEU N  503  1                                  19    
HELIX   57  57 ASN N  516  ARG N  542  1                                  27    
HELIX   58  58 PRO N  574  HIS N  578  5                                   5    
HELIX   59  59 ASN O   38  CYS O   40  5                                   3    
HELIX   60  60 MET O   43  LEU O   55  1                                  13    
HELIX   61  61 CYS O   85  LYS O   87  5                                   3    
HELIX   62  62 LEU O  115  ILE O  125  1                                  11    
HELIX   63  63 SER O  145  LYS O  151  1                                   7    
HELIX   64  64 CYS O  164  SER O  167  5                                   4    
HELIX   65  65 CYS O  168  GLY O  175  1                                   8    
HELIX   66  66 GLY O  180  ILE O  192  1                                  13    
HELIX   67  67 TYR O  198  GLN O  205  1                                   8    
HELIX   68  68 MET O  219  CYS O  225  1                                   7    
HELIX   69  69 ASN O  230  TYR O  245  1                                  16    
HELIX   70  70 THR P    4  LYS P   18  1                                  15    
HELIX   71  71 SER P   33  LEU P   63  1                                  31    
HELIX   72  72 GLN P   66  LEU P   77  1                                  12    
HELIX   73  73 SER P   80  MET P  110  1                                  31    
HELIX   74  74 LYS P  115  ALA P  139  1                                  25    
HELIX   75  75 LYS Q    4  TYR Q   30  1                                  27    
HELIX   76  76 GLY Q   32  VAL Q   59  1                                  28    
HELIX   77  77 GLY Q   61  ASP Q   90  1                                  30    
HELIX   78  78 GLY Q   92  TRP Q  101  1                                  10    
SHEET    1   A 6 SER A 171  VAL A 174  0                                        
SHEET    2   A 6 THR A  44  THR A  48  1  N  THR A  44   O  SER A 171           
SHEET    3   A 6 VAL A  14  VAL A  24  1  N  VAL A  23   O  ALA A  45           
SHEET    4   A 6 ILE A 201  ILE A 211  1  O  VAL A 210   N  VAL A  24           
SHEET    5   A 6 GLU A 187  CYS A 195 -1  N  VAL A 191   O  PHE A 204           
SHEET    6   A 6 TYR A 176  GLU A 184 -1  N  LEU A 182   O  ARG A 189           
SHEET    1   B 6 SER A 171  VAL A 174  0                                        
SHEET    2   B 6 THR A  44  THR A  48  1  N  THR A  44   O  SER A 171           
SHEET    3   B 6 VAL A  14  VAL A  24  1  N  VAL A  23   O  ALA A  45           
SHEET    4   B 6 ILE A 201  ILE A 211  1  O  VAL A 210   N  VAL A  24           
SHEET    5   B 6 GLU A 385  ALA A 394  1  O  TYR A 393   N  THR A 209           
SHEET    6   B 6 GLN A 377  VAL A 382 -1  N  THR A 380   O  LYS A 387           
SHEET    1   C 3 ILE A  64  ASN A  65  0                                        
SHEET    2   C 3 GLN A 142  CYS A 147 -1  O  CYS A 147   N  ILE A  64           
SHEET    3   C 3 GLN A 127  SER A 134 -1  N  ARG A 128   O  CYS A 146           
SHEET    1   D 3 CYS A 244  GLN A 245  0                                        
SHEET    2   D 3 LYS A 581  ASP A 588 -1  O  SER A 585   N  CYS A 244           
SHEET    3   D 3 LYS A 593  PRO A 600 -1  O  LYS A 597   N  LEU A 584           
SHEET    1   E 4 VAL A 250  ILE A 257  0                                        
SHEET    2   E 4 ILE A 357  ASN A 366 -1  O  THR A 362   N  HIS A 253           
SHEET    3   E 4 VAL A 321  GLN A 324 -1  N  LEU A 323   O  ILE A 357           
SHEET    4   E 4 ILE A 274  ILE A 276 -1  N  ILE A 274   O  GLN A 324           
SHEET    1   F 2 ILE A 370  PRO A 371  0                                        
SHEET    2   F 2 ALA A 399  SER A 400  1  O  SER A 400   N  ILE A 370           
SHEET    1   G 2 ILE A 463  ARG A 464  0                                        
SHEET    2   G 2 LEU A 506  LYS A 507  1  O  LYS A 507   N  ILE A 463           
SHEET    1   H 5 ARG B  29  ASP B  36  0                                        
SHEET    2   H 5 ILE B  11  ARG B  18 -1  N  LYS B  12   O  VAL B  35           
SHEET    3   H 5 THR B  97  TYR B 100  1  O  ILE B  99   N  SER B  15           
SHEET    4   H 5 ALA B  74  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   H 5 GLY B  80  LEU B  83 -1  O  THR B  82   N  MET B  75           
SHEET    1   I 2 VAL B 107  LYS B 109  0                                        
SHEET    2   I 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  LYS B 109           
SHEET    1   J 4 VAL N  14  GLU N  18  0                                        
SHEET    2   J 4 ILE N 201  ARG N 205  1  O  ILE N 201   N  VAL N  15           
SHEET    3   J 4 GLU N 187  CYS N 195 -1  N  VAL N 191   O  PHE N 204           
SHEET    4   J 4 TYR N 176  GLU N 184 -1  N  LEU N 182   O  ARG N 189           
SHEET    1   K 6 SER N 171  VAL N 174  0                                        
SHEET    2   K 6 THR N  44  THR N  48  1  N  THR N  44   O  SER N 171           
SHEET    3   K 6 ALA N  21  VAL N  24  1  N  VAL N  23   O  ALA N  45           
SHEET    4   K 6 ASN N 208  ILE N 211  1  O  VAL N 210   N  VAL N  24           
SHEET    5   K 6 GLU N 385  ALA N 394  1  O  TYR N 393   N  THR N 209           
SHEET    6   K 6 GLN N 377  VAL N 382 -1  N  THR N 380   O  LYS N 387           
SHEET    1   L 3 ILE N  64  ASN N  65  0                                        
SHEET    2   L 3 GLN N 142  CYS N 147 -1  O  CYS N 147   N  ILE N  64           
SHEET    3   L 3 GLN N 127  SER N 134 -1  N  ARG N 128   O  CYS N 146           
SHEET    1   M 3 CYS N 244  GLN N 245  0                                        
SHEET    2   M 3 LYS N 581  VAL N 587 -1  O  SER N 585   N  CYS N 244           
SHEET    3   M 3 VAL N 594  PRO N 600 -1  O  LYS N 597   N  LEU N 584           
SHEET    1   N 4 VAL N 250  ILE N 257  0                                        
SHEET    2   N 4 ILE N 357  ASN N 366 -1  O  THR N 362   N  HIS N 253           
SHEET    3   N 4 VAL N 321  GLN N 324 -1  N  VAL N 321   O  VAL N 359           
SHEET    4   N 4 ILE N 274  ILE N 276 -1  N  ILE N 274   O  GLN N 324           
SHEET    1   O 2 ILE N 370  PRO N 371  0                                        
SHEET    2   O 2 ALA N 399  SER N 400  1  O  SER N 400   N  ILE N 370           
SHEET    1   P 2 ILE N 463  ARG N 464  0                                        
SHEET    2   P 2 LEU N 506  LYS N 507  1  O  LYS N 507   N  ILE N 463           
SHEET    1   Q 5 ARG O  29  ASP O  36  0                                        
SHEET    2   Q 5 ILE O  11  ARG O  18 -1  N  LYS O  12   O  VAL O  35           
SHEET    3   Q 5 THR O  97  TYR O 100  1  O  ILE O  99   N  SER O  15           
SHEET    4   Q 5 ALA O  74  ILE O  77 -1  N  ASN O  76   O  TYR O 100           
SHEET    5   Q 5 GLY O  80  LEU O  83 -1  O  THR O  82   N  MET O  75           
SHEET    1   R 2 VAL O 107  LYS O 109  0                                        
SHEET    2   R 2 VAL O 112  PRO O 113 -1  O  VAL O 112   N  VAL O 108           
LINK         C8M FAD A1001                 NE2 HIS A  56     1555   1555  1.43  
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  65     1555   1555  2.27  
LINK        FE2  FES B1002                 SG  CYS B  70     1555   1555  2.25  
LINK        FE1  SF4 B1003                 SG  CYS B 164     1555   1555  2.24  
LINK        FE2  SF4 B1003                 SG  CYS B 158     1555   1555  2.28  
LINK        FE3  SF4 B1003                 SG  CYS B 225     1555   1555  2.23  
LINK        FE4  SF4 B1003                 SG  CYS B 161     1555   1555  2.27  
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         C8M FAD N1001                 NE2 HIS N  56     1555   1555  1.41  
LINK        FE1  FES O1002                 SG  CYS O  73     1555   1555  2.22  
LINK        FE1  FES O1002                 SG  CYS O  85     1555   1555  2.22  
LINK        FE2  FES O1002                 SG  CYS O  65     1555   1555  2.26  
LINK        FE2  FES O1002                 SG  CYS O  70     1555   1555  2.27  
LINK        FE1  SF4 O1003                 SG  CYS O 164     1555   1555  2.22  
LINK        FE2  SF4 O1003                 SG  CYS O 158     1555   1555  2.23  
LINK        FE3  SF4 O1003                 SG  CYS O 225     1555   1555  2.24  
LINK        FE4  SF4 O1003                 SG  CYS O 161     1555   1555  2.27  
LINK        FE1  F3S O1004                 SG  CYS O 215     1555   1555  2.26  
LINK        FE3  F3S O1004                 SG  CYS O 221     1555   1555  2.25  
LINK        FE4  F3S O1004                 SG  CYS O 168     1555   1555  2.19  
LINK        FE   HEM P 201                 NE2 HIS P  98     1555   1555  2.00  
LINK        FE   HEM P 201                 NE2 HIS Q  46     1555   1555  2.00  
LINK         O   ASN A 366                 K     K A 622     1555   1555  2.59  
LINK         O   GLY A 368                 K     K A 622     1555   1555  2.91  
LINK         O   GLU A 397                 K     K A 622     1555   1555  2.70  
LINK         O   ALA A 399                 K     K A 622     1555   1555  2.81  
LINK         O   MET B 191                 K     K B 253     1555   1555  2.86  
LINK         O   ASP B 193                 K     K B 253     1555   1555  2.75  
LINK         O   ASP B 196                 K     K B 253     1555   1555  2.94  
LINK         OG1 THR B 199                 K     K B 253     1555   1555  2.99  
LINK         O   ASN N 366                 K     K N 622     1555   1555  2.55  
LINK         O   GLY N 368                 K     K N 622     1555   1555  2.83  
LINK         O   GLU N 397                 K     K N 622     1555   1555  2.72  
LINK         O   ALA N 399                 K     K N 622     1555   1555  2.80  
LINK         O   MET O 191                 K     K O 253     1555   1555  2.99  
LINK         O   ASP O 193                 K     K O 253     1555   1555  2.82  
LINK         O   ASP O 196                 K     K O 253     1555   1555  2.83  
LINK         OG1 THR O 199                 K     K O 253     1555   1555  2.95  
LINK         K     K B 253                 O   HOH B1900     1555   1555  2.96  
LINK         K     K O 253                 O   HOH O1041     1555   1555  3.01  
LINK         O   MET N 367                 K     K N 622     1555   1555  3.05  
LINK         O   MET A 367                 K     K A 622     1555   1555  3.08  
LINK         K     K B 253                 O   HOH B1795     1555   1555  3.17  
LINK         K     K B 253                 O   HOH B1777     1555   1555  3.27  
LINK         K     K O 253                 O   HOH O1049     1555   1555  3.29  
LINK         K     K B 253                 O   HOH B2905     1555   1555  3.31  
LINK         K     K B 253                 O   HOH B1861     1555   1555  3.34  
LINK         OH  TYR A 365                 K     K A 622     1555   1555  3.35  
LINK         OH  TYR N 365                 K     K N 622     1555   1555  3.43  
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 10 LYS C  31  TRP C  32  SER C  33  LEU C  34                    
SITE     2 AC1 10 PRO C  35  GLU C 120  UNL C 289  HOH C1750                    
SITE     3 AC1 10 HOH C2605  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 P1172  HOH P2485  HOH P2548                    
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 B1900                                                     
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 O1041                                                     
SITE     1 AC7  3 TYR A 172  VAL A 174  HOH A1854                               
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  TEO A1002                    
SITE    10 AC8 40 HOH A1692  HOH A1708  HOH A1735  HOH A1880                    
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  TEO N1002  HOH N1026                    
SITE    10 BC3 40 HOH N1038  HOH N1051  HOH N1054  HOH N1133                    
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  8 CYS O 158  ILE O 159  CYS O 161  ALA O 162                    
SITE     2 BC5  8 CYS O 164  ALA O 182  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 C1879  HOH C1903  HOH C2103  ARG D  14                    
SITE     4 BC7 16 LEU D  20  LEU D  43  HIS D  46  GLY D  50                    
SITE     1 BC8 11 PRO B 169  TRP B 173  HIS B 216  ILE C  27                    
SITE     2 BC8 11 TRP C  32  MET C  36  SER C  39  ILE C  40                    
SITE     3 BC8 11 ARG C  43  HOH C1687  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  1 HOH C2865                                                     
SITE     1 CC3 17 HOH O1079  HIS P  42  ARG P  43  GLY P  46                    
SITE     2 CC3 17 LEU P  49  SER P  50  HIS P  98  THR P  99                    
SITE     3 CC3 17 GLY P 102  HIS P 105  HOH P1002  HOH P1199                    
SITE     4 CC3 17 ARG Q  14  LEU Q  20  LEU Q  43  HIS Q  46                    
SITE     5 CC3 17 GLY Q  50                                                     
SITE     1 CC4 12 PRO O 169  TRP O 173  HIS O 216  ILE O 218                    
SITE     2 CC4 12 ILE P  27  TRP P  32  MET P  36  SER P  39                    
SITE     3 CC4 12 ILE P  40  ARG P  43  HOH P1004  TYR Q  58                    
SITE     1 CC5 11 GLY N  62  HIS N 253  LEU N 263  THR N 265                    
SITE     2 CC5 11 GLU N 266  ARG N 297  HIS N 364  ARG N 408                    
SITE     3 CC5 11 GLY N 410  ALA N 411  FAD N1001                               
SITE     1 CC6  6 SER P 141  GOL P 208  UNL P 211  ALA Q  27                    
SITE     2 CC6  6 VAL Q  97  TRP Q 101                                          
SITE     1 CC7  2 GOL P 208  PEE Q 210                                          
SITE     1 CC8  4 GLN N  11  TYR N  12  GLN N 136  ARG N 457                    
SITE     1 CC9  2 ASP O 176  TRP P  13                                          
SITE     1 DC1  3 TYR C  85  HOH C2876  LEU P 127                               
SITE     1 DC2  4 ALA B  78  HOH B1906  HOH B2343  LYS C  31                    
SITE     1 DC3  3 PHE A 137  SER A 612  HOH A2231                               
SITE     1 DC4  2 GLY A 272  HOH A2942                                          
SITE     1 DC5  1 GLN N  11                                                     
SITE     1 DC6  1 GLN P 118                                                     
SITE     1 DC7  1 GLU N 608                                                     
SITE     1 DC8  1 TYR N 258                                                     
SITE     1 DC9  1 PHE O 210                                                     
SITE     1 EC1  1 THR C  41                                                     
SITE     1 EC2  1 TYR D  73                                                     
SITE     1 EC3  1 UNL C 251                                                     
SITE     1 EC4  1 UNL C 248                                                     
SITE     1 EC5  1 ASP B  46                                                     
SITE     1 EC6  2 LYS A 442  ASN A 444                                          
SITE     1 EC7  1 HOH A2810                                                     
SITE     1 EC8  1 PRO B 209                                                     
SITE     1 EC9  2 LYS A 354  GLU A 355                                          
SITE     1 FC1  3 HOH A2544  HOH A2640  HOH A2892                               
SITE     1 FC2  1 LYS A 593                                                     
SITE     1 FC3  1 TYR A 500                                                     
SITE     1 FC4  1 ARG B  10                                                     
SITE     1 FC5  3 ALA A 451  ASP A 454  LYS A 455                               
SITE     1 FC6  1 TYR Q  73                                                     
SITE     1 FC7  1 BHG C 142                                                     
SITE     1 FC8  2 PHE N 137  SER N 612                                          
SITE     1 FC9  1 GLU N 491                                                     
SITE     1 GC1  2 GLU N  18  HOH N1566                                          
SITE     1 GC2  1 LYS N 474                                                     
SITE     1 GC3  2 PRO A  13  GLY A 199                                          
SITE     1 GC4  3 HIS A 326  HIS A 327  HOH A2959                               
SITE     1 GC5  1 LYS N 474                                                     
SITE     1 GC6  2 LEU A 567  PRO A 615                                          
SITE     1 GC7  3 PHE C  56  ILE D  93  PEE D 109                               
SITE     1 GC8  9 HIS B 104  MET B 105  TYR B 171  HOH B1772                    
SITE     2 GC8  9 HOH B1792  HOH B1821  HOH B1952  HOH B2154                    
SITE     3 GC8  9 TRP C  13                                                     
SITE     1 GC9 10 HIS O 104  MET O 105  GLY O 175  HOH O1039                    
SITE     2 GC9 10 HOH O1047  HOH O1055  HOH O1099  HOH O1156                    
SITE     3 GC9 10 PHE P  12  TRP P  13                                          
SITE     1 HC1  3 LEU P  91  UNL P 211  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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