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Database: PDB
Entry: 3H1L
LinkDB: 3H1L
Original site: 3H1L 
HEADER    OXIDOREDUCTASE                          12-APR-09   3H1L              
TITLE     CHICKEN CYTOCHROME BC1 COMPLEX WITH ASCOCHLORIN BOUND AT QO           
TITLE    2 AND QI SITES                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE             
COMPND   3 COMPLEX CORE PROTEIN I;                                              
COMPND   4 CHAIN: A, N;                                                         
COMPND   5 EC: 1.10.2.2;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE             
COMPND   8 COMPLEX CORE PROTEIN 2;                                              
COMPND   9 CHAIN: B, O;                                                         
COMPND  10 EC: 1.10.2.2;                                                        
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: CYTOCHROME B;                                              
COMPND  13 CHAIN: C, P;                                                         
COMPND  14 SYNONYM: UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX                    
COMPND  15 CYTOCHROME B SUBUNIT, CYTOCHROME B-C1 COMPLEX SUBUNIT 3,             
COMPND  16 COMPLEX III SUBUNIT 3, COMPLEX III SUBUNIT III;                      
COMPND  17 EC: 1.10.2.2;                                                        
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN;                 
COMPND  20 CHAIN: D, Q;                                                         
COMPND  21 EC: 1.10.2.2;                                                        
COMPND  22 MOL_ID: 5;                                                           
COMPND  23 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE,                    
COMPND  24 MITOCHONDRIAL;                                                       
COMPND  25 CHAIN: E, R;                                                         
COMPND  26 FRAGMENT: SEQUENCE DATABASE RESIDUES 77-272;                         
COMPND  27 SYNONYM: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR                
COMPND  28 SUBUNIT, RIESKE IRON-SULFUR PROTEIN, RISP, COMPLEX III               
COMPND  29 SUBUNIT 5;                                                           
COMPND  30 EC: 1.10.2.2;                                                        
COMPND  31 MOL_ID: 6;                                                           
COMPND  32 MOLECULE: MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14          
COMPND  33 KDA PROTEIN;                                                         
COMPND  34 CHAIN: F, S;                                                         
COMPND  35 EC: 1.10.2.2;                                                        
COMPND  36 MOL_ID: 7;                                                           
COMPND  37 MOLECULE: MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE             
COMPND  38 UBIQUINONE-BINDING PROTEIN QP-C;                                     
COMPND  39 CHAIN: G, T;                                                         
COMPND  40 EC: 1.10.2.2;                                                        
COMPND  41 MOL_ID: 8;                                                           
COMPND  42 MOLECULE: MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11          
COMPND  43 KDA PROTEIN, COMPLEX III SUBUNIT VIII;                               
COMPND  44 CHAIN: H, U;                                                         
COMPND  45 EC: 1.10.2.2;                                                        
COMPND  46 MOL_ID: 9;                                                           
COMPND  47 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE,                    
COMPND  48 MITOCHONDRIAL;                                                       
COMPND  49 CHAIN: I, V;                                                         
COMPND  50 FRAGMENT: SEQUENCE DATABASE RESIDUES 1-76;                           
COMPND  51 SYNONYM: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR                
COMPND  52 SUBUNIT, RIESKE IRON-SULFUR PROTEIN, RISP, COMPLEX III               
COMPND  53 SUBUNIT 5;                                                           
COMPND  54 EC: 1.10.2.2;                                                        
COMPND  55 MOL_ID: 10;                                                          
COMPND  56 MOLECULE: MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE             
COMPND  57 7.2 KDA PROTEIN;                                                     
COMPND  58 CHAIN: J, W;                                                         
COMPND  59 EC: 1.10.2.2                                                         
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;                                                
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  19 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  20 ORGANISM_TAXID: 9031;                                                
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  23 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  24 ORGANISM_TAXID: 9031;                                                
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  27 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  28 ORGANISM_TAXID: 9031;                                                
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  31 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  32 ORGANISM_TAXID: 9031;                                                
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  35 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  36 ORGANISM_TAXID: 9031;                                                
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  39 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  40 ORGANISM_TAXID: 9031                                                 
KEYWDS    CYTOCHROME BC1, MEMBRANE PROTEIN, HEME PROTEIN, RIESKE IRON           
KEYWDS   2 SULFUR PROTEIN, CYTOCHROME B, CYTOCHROME C1, COMPLEX III,            
KEYWDS   3 ASCOCHLORIN, UBIQUINONE, OXIDOREDUCTASE, REDOX ENZYME,               
KEYWDS   4 RESPIRATORY CHAIN, ELECTRON TRANSPORT, HEME, INNER MEMBRANE          
KEYWDS   5 IRON, MEMBRANE, METAL-BINDING, MITOCHONDRION,                        
KEYWDS   6 TRANSMEMBRANE, IRON, MITOCHONDRION INNER MEMBRANE,                   
KEYWDS   7 TRANSPORT, 2FE-2S, DISULFIDE BOND, IRON-SULFUR, TRANSIT              
KEYWDS   8 PEPTIDE                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.A.BERRY,L.S.HUANG,N.MINAGAWA                                        
REVDAT   2   23-FEB-10 3H1L    1       JRNL                                     
REVDAT   1   05-JAN-10 3H1L    0                                                
JRNL        AUTH   E.A.BERRY,L.S.HUANG,D.W.LEE,F.DALDAL,K.NAGAI,                
JRNL        AUTH 2 N.MINAGAWA                                                   
JRNL        TITL   ASCOCHLORIN IS A NOVEL, SPECIFIC INHIBITOR OF THE            
JRNL        TITL 2 MITOCHONDRIAL CYTOCHROME BC(1) COMPLEX.                      
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1797   360 2010              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   20025846                                                     
JRNL        DOI    10.1016/J.BBABIO.2009.12.003                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.21 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) : 3.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3437790.830                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 125125                         
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) : 0.267                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2491                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 7                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.21                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.37                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 16015                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3960                       
REMARK   3   BIN FREE R VALUE                    : 0.4040                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 358                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 31797                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 846                                     
REMARK   3   SOLVENT ATOMS            : 14                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 86.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 106.40                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 45.71000                                             
REMARK   3    B22 (A**2) : -30.70000                                            
REMARK   3    B33 (A**2) : -15.01000                                            
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) : 0.53                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.88                            
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) : 0.59                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.91                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.95                            
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) : 1.270 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.270 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.560 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.620 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.26                                                 
REMARK   3   BSOL        : 31.86                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
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  : HETERO10.PAR                                   
REMARK   3  PARAMETER FILE  3  : ACL.PAR                                        
REMARK   3  PARAMETER FILE  4  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  5  : PROSTHW.PAR                                    
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : &_1_TOPOLOGY_INFILE_1                          
REMARK   3  TOPOLOGY FILE  2   : &_1_TOPOLOGY_INFILE_2                          
REMARK   3  TOPOLOGY FILE  3   : &_1_TOPOLOGY_INFILE_3                          
REMARK   3  TOPOLOGY FILE  4   : &_1_TOPOLOGY_INFILE_4                          
REMARK   3  TOPOLOGY FILE  5   : &_1_TOPOLOGY_INFILE_5                          
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3H1L COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052576.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUL-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.77                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
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   : 125484                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.968                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.15800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.99000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.370                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RIGID BODY REFINEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 2BCC AFTER FURTHER REFINEMENT                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: FINAL CONCENTRATIONS BEFORE              
REMARK 280  DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50        
REMARK 280  G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L             
REMARK 280  UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       87.06950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      120.81300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       91.18200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      120.81300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       87.06950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       91.18200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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: EICOSAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: EICOSAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 103430 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 152600 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -699.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H, P, Q, U, S, F, R,            
REMARK 350                    AND CHAINS: E, T, G, I, A, B, V, N, O,            
REMARK 350                    AND CHAINS: W, J                                  
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     ALA A     1                                                      
REMARK 465     ARG A   445                                                      
REMARK 465     PHE A   446                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     LEU B     0                                                      
REMARK 465     LYS B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     VAL B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     LEU B    17                                                      
REMARK 465     CYS B    18                                                      
REMARK 465     ALA F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     ARG F     3                                                      
REMARK 465     ALA F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     VAL F     6                                                      
REMARK 465     ALA F     7                                                      
REMARK 465     GLY F     8                                                      
REMARK 465     GLY F     9                                                      
REMARK 465     LEU H     2                                                      
REMARK 465     ARG H     3                                                      
REMARK 465     GLY H     4                                                      
REMARK 465     SER H     5                                                      
REMARK 465     GLY H     6                                                      
REMARK 465     GLU H     7                                                      
REMARK 465     GLU H     8                                                      
REMARK 465     TYR I    78                                                      
REMARK 465     ALA N     1                                                      
REMARK 465     ALA N     2                                                      
REMARK 465     ARG N   445                                                      
REMARK 465     PHE N   446                                                      
REMARK 465     SER O    -1                                                      
REMARK 465     LEU O     0                                                      
REMARK 465     LYS O     1                                                      
REMARK 465     VAL O     2                                                      
REMARK 465     ALA O     3                                                      
REMARK 465     PRO O     4                                                      
REMARK 465     LYS O     5                                                      
REMARK 465     VAL O     6                                                      
REMARK 465     ALA O     7                                                      
REMARK 465     VAL O     8                                                      
REMARK 465     SER O     9                                                      
REMARK 465     ALA O    10                                                      
REMARK 465     ALA O    11                                                      
REMARK 465     ALA O    12                                                      
REMARK 465     GLU O    13                                                      
REMARK 465     ARG O    14                                                      
REMARK 465     VAL O    15                                                      
REMARK 465     LYS O    16                                                      
REMARK 465     LEU O    17                                                      
REMARK 465     MET P     1                                                      
REMARK 465     ALA S     1                                                      
REMARK 465     ALA S     2                                                      
REMARK 465     ARG S     3                                                      
REMARK 465     ALA S     4                                                      
REMARK 465     THR S     5                                                      
REMARK 465     VAL S     6                                                      
REMARK 465     ALA S     7                                                      
REMARK 465     GLY S     8                                                      
REMARK 465     GLY S     9                                                      
REMARK 465     ASP T    80                                                      
REMARK 465     GLN T    81                                                      
REMARK 465     LEU U     2                                                      
REMARK 465     ARG U     3                                                      
REMARK 465     GLY U     4                                                      
REMARK 465     SER U     5                                                      
REMARK 465     GLY U     6                                                      
REMARK 465     GLU U     7                                                      
REMARK 465     GLU U     8                                                      
REMARK 465     GLU U     9                                                      
REMARK 465     GLU U    10                                                      
REMARK 465     GLU U    11                                                      
REMARK 465     UNK V    26                                                      
REMARK 465     UNK V    27                                                      
REMARK 465     TYR V    78                                                      
REMARK 465     GLU W    63                                                      
REMARK 465     GLU W    64                                                      
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     ILE A 444    C    O    CB   CG1  CG2  CD1                        
REMARK 470     GLU H   9    N    CB   CG   CD   OE1  OE2                        
REMARK 470     ARG I  47    N    CB   CG   CD   NE   CZ   NH1                   
REMARK 470     ARG I  47    NH2                                                 
REMARK 470     ARG I  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE N 444    O    CG1  CG2  CD1                                  
REMARK 470     ARG V  47    N    CB   CG   CD   NE   CZ   NH1                   
REMARK 470     ARG V  47    NH2                                                 
REMARK 470     ARG V  61    CG   CD   NE   CZ   NH1  NH2                        
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   OD1  ASN R    53     O2   BOG R  3009              2.18            
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    PRO A 249   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    GLY E 143   N   -  CA  -  C   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    GLY R 143   N   -  CA  -  C   ANGL. DEV. =  15.7 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   3      144.30    -33.69                                   
REMARK 500    TYR A   4      -72.10    -36.59                                   
REMARK 500    ALA A   5      -51.71    -19.21                                   
REMARK 500    ILE A  11      128.99    -39.69                                   
REMARK 500    ALA A  43      117.54   -162.79                                   
REMARK 500    ASN A  49     -168.08   -100.66                                   
REMARK 500    THR A  67     -168.11   -112.31                                   
REMARK 500    PRO A  71     -172.81    -55.68                                   
REMARK 500    CYS A  72      -82.92    -47.94                                   
REMARK 500    SER A  91     -163.95   -115.39                                   
REMARK 500    GLN A  94      103.29    164.32                                   
REMARK 500    ALA A 155      -30.47    -37.40                                   
REMARK 500    GLN A 159      142.42    -38.12                                   
REMARK 500    THR A 161     -166.77   -115.98                                   
REMARK 500    PHE A 221      -60.37   -101.27                                   
REMARK 500    ARG A 233      151.65    -49.27                                   
REMARK 500    ASP A 245       91.22   -162.54                                   
REMARK 500    TRP A 262      -60.66    -22.00                                   
REMARK 500    ASP A 281      148.01   -172.07                                   
REMARK 500    ARG A 282      -28.63    -29.31                                   
REMARK 500    LYS A 288       -4.99    -54.31                                   
REMARK 500    SER A 306      159.43    177.03                                   
REMARK 500    THR A 317     -149.61   -129.33                                   
REMARK 500    LEU A 369       54.44   -109.10                                   
REMARK 500    ASP A 370       71.44   -112.17                                   
REMARK 500    ARG A 388     -149.55   -117.23                                   
REMARK 500    ALA A 404      -77.76    -53.03                                   
REMARK 500    ILE A 428       25.73    -77.71                                   
REMARK 500    ASP A 433      119.99     56.29                                   
REMARK 500    TRP A 443      104.63     77.19                                   
REMARK 500    GLU B  22     -141.10    -73.48                                   
REMARK 500    ILE B  26       79.05   -170.04                                   
REMARK 500    LYS B  28       29.25   -145.48                                   
REMARK 500    LEU B  29      161.37      5.01                                   
REMARK 500    PRO B  30      -75.34    -49.87                                   
REMARK 500    LEU B  38      103.74    174.61                                   
REMARK 500    PRO B  43        3.36    -69.09                                   
REMARK 500    LYS B  52       59.59    -94.99                                   
REMARK 500    SER B  55        1.81    -61.95                                   
REMARK 500    LEU B  63      151.67    -35.86                                   
REMARK 500    ARG B 102       -8.27    -53.65                                   
REMARK 500    GLU B 103       28.11   -152.75                                   
REMARK 500    LYS B 104      104.87   -165.89                                   
REMARK 500    GLU B 110      108.38   -179.93                                   
REMARK 500    PHE B 152       13.99    -64.77                                   
REMARK 500    LEU B 163      -73.18    -65.27                                   
REMARK 500    ALA B 171      -78.31     41.09                                   
REMARK 500    GLN B 190      -35.39    -36.31                                   
REMARK 500    ASN B 198      -31.52   -150.91                                   
REMARK 500    VAL B 207     -161.52    -68.90                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     345 RAMACHANDRAN OUTLIERS.                        
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  76         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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     PEE A 2008                                                       
REMARK 610     CDL C 2003                                                       
REMARK 610     PEE C 2007                                                       
REMARK 610     PEE E 2005                                                       
REMARK 610     CDL G 2004                                                       
REMARK 610     CDL P 3003                                                       
REMARK 610     PEE P 3007                                                       
REMARK 610     PEE P 3008                                                       
REMARK 610     PEE R 3005                                                       
REMARK 610     CDL T 3004                                                       
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                             HEM C 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  84   NE2                                                    
REMARK 620 2 HEM C 501   NA   93.4                                              
REMARK 620 3 HEM C 501   NB   92.0  93.1                                        
REMARK 620 4 HEM C 501   NC   85.3 176.2  90.5                                  
REMARK 620 5 HEM C 501   ND   88.8  88.8 177.9  87.6                            
REMARK 620 6 HIS C 183   NE2 174.2  90.1  92.4  91.0  86.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 502  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  98   NE2                                                    
REMARK 620 2 HEM C 502   NA   90.7                                              
REMARK 620 3 HEM C 502   NB   90.8  90.1                                        
REMARK 620 4 HEM C 502   NC   87.9 178.5  90.1                                  
REMARK 620 5 HEM C 502   ND   90.0  89.0 178.8  90.8                            
REMARK 620 6 HIS C 197   NE2 173.2  91.4  95.7  90.1  83.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC D 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  41   NE2                                                    
REMARK 620 2 HEC D 501   NA   87.0                                              
REMARK 620 3 HEC D 501   NB   87.5  89.9                                        
REMARK 620 4 HEC D 501   NC   94.1 177.7  88.1                                  
REMARK 620 5 HEC D 501   ND   92.4  88.5 178.3  93.5                            
REMARK 620 6 MET D 160   SD  176.5  90.7  89.9  88.1  90.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES E 501  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 139   SG                                                     
REMARK 620 2 FES E 501   S1  113.0                                              
REMARK 620 3 FES E 501   S2  109.3 105.6                                        
REMARK 620 4 CYS E 158   SG  110.5 108.2 110.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES E 501  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E 141   ND1                                                    
REMARK 620 2 FES E 501   S1  113.6                                              
REMARK 620 3 FES E 501   S2  117.5 105.3                                        
REMARK 620 4 HIS E 161   ND1  93.8 116.2 110.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM P 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P  84   NE2                                                    
REMARK 620 2 HEM P 501   NA   89.0                                              
REMARK 620 3 HEM P 501   NB   87.2  92.0                                        
REMARK 620 4 HEM P 501   NC   89.5 175.5  92.1                                  
REMARK 620 5 HEM P 501   ND   90.5  88.8 177.5  87.0                            
REMARK 620 6 HIS P 183   NE2 178.1  92.8  92.3  88.7  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM P 502  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P  98   NE2                                                    
REMARK 620 2 HEM P 502   NA   89.8                                              
REMARK 620 3 HEM P 502   NB   94.9  88.2                                        
REMARK 620 4 HEM P 502   NC   88.7 178.5  92.2                                  
REMARK 620 5 HEM P 502   ND   88.6  87.4 174.4  92.3                            
REMARK 620 6 HIS P 197   NE2 171.4  90.6  93.6  90.8  82.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC Q 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Q  41   NE2                                                    
REMARK 620 2 HEC Q 501   NA   90.9                                              
REMARK 620 3 HEC Q 501   NB   90.0  89.9                                        
REMARK 620 4 HEC Q 501   NC   90.6 178.4  89.7                                  
REMARK 620 5 HEC Q 501   ND   89.0  87.4 177.1  93.1                            
REMARK 620 6 MET Q 160   SD  176.3  88.8  93.6  89.7  87.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES R 501  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS R 139   SG                                                     
REMARK 620 2 FES R 501   S1  113.3                                              
REMARK 620 3 FES R 501   S2  110.5 106.2                                        
REMARK 620 4 CYS R 158   SG  106.6 110.9 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES R 501  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS R 141   ND1                                                    
REMARK 620 2 FES R 501   S1  113.5                                              
REMARK 620 3 FES R 501   S2  116.9 105.8                                        
REMARK 620 4 HIS R 161   ND1  93.0 115.9 111.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE A 2008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3H1 C 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3H1 C 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL C 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE C 2007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 2010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 2104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 3015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 2011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 2009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE E 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL E 2105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL G 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM P 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM P 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL P 2015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL P 2106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3H1 P 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3H1 P 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL P 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE P 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE P 3008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL P 3010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL P 3103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL P 3104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL P 3011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC Q 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES R 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL R 2103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE R 3005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG R 3009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL T 3004                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 IN THE COORDINATES THE FIRST 15 RESIDUES IN CHAINS I AND V ARE       
REMARK 999 MODELED AS UNK BECAUSE THE SEQUENCE ALIGNMENT IS UNKNOWN FOR THE     
REMARK 999 FIRST 42 RESIDUES IN CHAINS I AND V.                                 
DBREF  3H1L C    1   380  UNP    P18946   CYB_CHICK        1    380             
DBREF  3H1L E    1   196  UNP    Q5ZLR5   UCRI_CHICK      77    272             
DBREF  3H1L I   47    78  UNP    Q5ZLR5   UCRI_CHICK      45     76             
DBREF  3H1L P    1   380  UNP    P18946   CYB_CHICK        1    380             
DBREF  3H1L R    1   196  UNP    Q5ZLR5   UCRI_CHICK      77    272             
DBREF  3H1L V   47    78  UNP    Q5ZLR5   UCRI_CHICK      45     76             
DBREF  3H1L A    1   446  PDB    3H1L     3H1L             1    446             
DBREF  3H1L N    1   446  PDB    3H1L     3H1L             1    446             
DBREF  3H1L B   -1   439  PDB    3H1L     3H1L            -1    439             
DBREF  3H1L O   -1   439  PDB    3H1L     3H1L            -1    439             
DBREF  3H1L D    1   241  PDB    3H1L     3H1L             1    241             
DBREF  3H1L Q    1   241  PDB    3H1L     3H1L             1    241             
DBREF  3H1L F    1   110  PDB    3H1L     3H1L             1    110             
DBREF  3H1L S    1   110  PDB    3H1L     3H1L             1    110             
DBREF  3H1L G    1    81  PDB    3H1L     3H1L             1     81             
DBREF  3H1L T    1    81  PDB    3H1L     3H1L             1     81             
DBREF  3H1L H    2    78  PDB    3H1L     3H1L             2     78             
DBREF  3H1L U    2    78  PDB    3H1L     3H1L             2     78             
DBREF  3H1L J    4    64  PDB    3H1L     3H1L             4     64             
DBREF  3H1L W    4    64  PDB    3H1L     3H1L             4     64             
SEQRES   1 A  446  ALA ALA THR TYR ALA GLN THR LEU GLN ASN ILE PRO GLU          
SEQRES   2 A  446  THR ASN VAL THR THR LEU ASP ASN GLY LEU ARG VAL ALA          
SEQRES   3 A  446  SER GLU GLU SER SER GLN PRO THR CYS THR VAL GLY VAL          
SEQRES   4 A  446  TRP ILE GLY ALA GLY SER ARG TYR GLU ASN GLU LYS ASN          
SEQRES   5 A  446  ASN GLY ALA GLY TYR PHE VAL GLU HIS LEU ALA PHE LYS          
SEQRES   6 A  446  GLY THR LYS LYS ARG PRO CYS ALA ALA PHE GLU LYS GLU          
SEQRES   7 A  446  VAL GLU SER MET GLY ALA HIS PHE ASN GLY TYR THR SER          
SEQRES   8 A  446  ARG GLU GLN THR ALA PHE TYR ILE LYS ALA LEU SER LYS          
SEQRES   9 A  446  ASP MET PRO LYS VAL VAL GLU LEU LEU ALA ASP VAL VAL          
SEQRES  10 A  446  GLN ASN CYS ALA LEU GLU GLU SER GLN ILE GLU LYS GLU          
SEQRES  11 A  446  ARG GLY VAL ILE LEU GLN GLU LEU LYS GLU MET ASP ASN          
SEQRES  12 A  446  ASP MET THR ASN VAL THR PHE ASP TYR LEU HIS ALA THR          
SEQRES  13 A  446  ALA PHE GLN GLY THR ALA LEU ALA ARG THR VAL GLU GLY          
SEQRES  14 A  446  THR THR GLU ASN ILE LYS HIS LEU THR ARG ALA ASP LEU          
SEQRES  15 A  446  ALA SER TYR ILE ASP THR HIS PHE LYS ALA PRO ARG MET          
SEQRES  16 A  446  VAL LEU ALA ALA ALA GLY GLY ILE SER HIS LYS GLU LEU          
SEQRES  17 A  446  VAL ASP ALA ALA ARG GLN HIS PHE SER GLY VAL SER PHE          
SEQRES  18 A  446  THR TYR LYS GLU ASP ALA VAL PRO ILE LEU PRO ARG CYS          
SEQRES  19 A  446  ARG PHE THR GLY SER GLU ILE ARG ALA ARG ASP ASP ALA          
SEQRES  20 A  446  LEU PRO VAL ALA HIS VAL ALA LEU ALA VAL GLU GLY PRO          
SEQRES  21 A  446  GLY TRP ALA ASP PRO ASP ASN VAL VAL LEU HIS VAL ALA          
SEQRES  22 A  446  ASN ALA ILE ILE GLY ARG TYR ASP ARG THR PHE GLY GLY          
SEQRES  23 A  446  GLY LYS HIS LEU SER SER ARG LEU ALA ALA LEU ALA VAL          
SEQRES  24 A  446  GLU HIS LYS LEU CYS HIS SER PHE GLN THR PHE ASN THR          
SEQRES  25 A  446  SER TYR SER ASP THR GLY LEU PHE GLY PHE HIS PHE VAL          
SEQRES  26 A  446  ALA ASP PRO LEU SER ILE ASP ASP MET MET PHE CYS ALA          
SEQRES  27 A  446  GLN GLY GLU TRP MET ARG LEU CYS THR SER THR THR GLU          
SEQRES  28 A  446  SER GLU VAL LYS ARG ALA LYS ASN HIS LEU ARG SER ALA          
SEQRES  29 A  446  MET VAL ALA GLN LEU ASP GLY THR THR PRO VAL CYS GLU          
SEQRES  30 A  446  THR ILE GLY SER HIS LEU LEU ASN TYR GLY ARG ARG ILE          
SEQRES  31 A  446  SER LEU GLU GLU TRP ASP SER ARG ILE SER ALA VAL ASP          
SEQRES  32 A  446  ALA ARG MET VAL ARG ASP VAL CYS SER LYS TYR ILE TYR          
SEQRES  33 A  446  ASP LYS CYS PRO ALA LEU ALA ALA VAL GLY PRO ILE GLU          
SEQRES  34 A  446  GLN LEU LEU ASP TYR ASN ARG ILE ARG SER GLY MET TYR          
SEQRES  35 A  446  TRP ILE ARG PHE                                              
SEQRES   1 B  441  SER LEU LYS VAL ALA PRO LYS VAL ALA VAL SER ALA ALA          
SEQRES   2 B  441  ALA GLU ARG VAL LYS LEU CYS PRO GLY ALA GLU ASP LEU          
SEQRES   3 B  441  GLU ILE THR LYS LEU PRO ASN GLY LEU ILE ILE ALA SER          
SEQRES   4 B  441  LEU GLU ASN PHE SER PRO ALA SER ARG ILE GLY VAL PHE          
SEQRES   5 B  441  ILE LYS ALA GLY SER ARG TYR GLU THR THR ALA ASN LEU          
SEQRES   6 B  441  GLY THR ALA HIS LEU LEU ARG LEU ALA SER PRO LEU THR          
SEQRES   7 B  441  THR LYS GLY ALA SER SER PHE ARG ILE THR ARG GLY ILE          
SEQRES   8 B  441  GLU ALA VAL GLY GLY SER LEU SER VAL TYR SER THR ARG          
SEQRES   9 B  441  GLU LYS MET THR TYR CYS VAL GLU CYS LEU ARG ASP HIS          
SEQRES  10 B  441  VAL ASP THR VAL MET GLU TYR LEU LEU ASN VAL THR THR          
SEQRES  11 B  441  ALA PRO GLU PHE ARG PRO TRP GLU VAL THR ASP LEU GLN          
SEQRES  12 B  441  PRO GLN LEU LYS VAL ASP LYS ALA VAL ALA PHE GLN SER          
SEQRES  13 B  441  PRO GLN VAL GLY VAL LEU GLU ASN LEU HIS ALA ALA ALA          
SEQRES  14 B  441  TYR LYS THR ALA LEU ALA ASN PRO LEU TYR CYS PRO ASP          
SEQRES  15 B  441  TYR ARG ILE GLY LYS ILE THR SER GLU GLN LEU HIS HIS          
SEQRES  16 B  441  PHE VAL GLN ASN ASN PHE THR SER ALA ARG MET ALA LEU          
SEQRES  17 B  441  VAL GLY ILE GLY VAL LYS HIS SER ASP LEU LYS GLN VAL          
SEQRES  18 B  441  ALA GLU GLN PHE LEU ASN ILE ARG SER GLY ALA GLY THR          
SEQRES  19 B  441  SER SER ALA LYS ALA THR TYR TRP GLY GLY GLU ILE ARG          
SEQRES  20 B  441  GLU GLN ASN GLY HIS SER LEU VAL HIS ALA ALA VAL VAL          
SEQRES  21 B  441  THR GLU GLY ALA ALA VAL GLY SER ALA GLU ALA ASN ALA          
SEQRES  22 B  441  PHE SER VAL LEU GLN HIS VAL LEU GLY ALA GLY PRO LEU          
SEQRES  23 B  441  ILE LYS ARG GLY SER SER VAL THR SER LYS LEU TYR GLN          
SEQRES  24 B  441  GLY VAL ALA LYS ALA THR THR GLN PRO PHE ASP ALA SER          
SEQRES  25 B  441  ALA PHE ASN VAL ASN TYR SER ASP SER GLY LEU PHE GLY          
SEQRES  26 B  441  PHE TYR THR ILE SER GLN ALA ALA HIS ALA GLY GLU VAL          
SEQRES  27 B  441  ILE ARG ALA ALA MET ASN GLN LEU LYS ALA ALA ALA GLN          
SEQRES  28 B  441  GLY GLY VAL THR GLU GLU ASP VAL THR LYS ALA LYS ASN          
SEQRES  29 B  441  GLN LEU LYS ALA THR TYR LEU MET SER VAL GLU THR ALA          
SEQRES  30 B  441  GLN GLY LEU LEU ASN GLU ILE GLY SER GLU ALA LEU LEU          
SEQRES  31 B  441  SER GLY THR HIS THR ALA PRO SER VAL VAL ALA GLN LYS          
SEQRES  32 B  441  ILE ASP SER VAL THR SER ALA ASP VAL VAL ASN ALA ALA          
SEQRES  33 B  441  LYS LYS PHE VAL SER GLY LYS LYS SER MET ALA ALA SER          
SEQRES  34 B  441  GLY ASP LEU GLY SER THR PRO PHE LEU ASP GLU LEU              
SEQRES   1 C  380  MET ALA PRO ASN ILE ARG LYS SER HIS PRO LEU LEU LYS          
SEQRES   2 C  380  MET ILE ASN ASN SER LEU ILE ASP LEU PRO ALA PRO SER          
SEQRES   3 C  380  ASN ILE SER ALA TRP TRP ASN PHE GLY SER LEU LEU ALA          
SEQRES   4 C  380  VAL CYS LEU MET THR GLN ILE LEU THR GLY LEU LEU LEU          
SEQRES   5 C  380  ALA MET HIS TYR THR ALA ASP THR SER LEU ALA PHE SER          
SEQRES   6 C  380  SER VAL ALA HIS THR CYS ARG ASN VAL GLN TYR GLY TRP          
SEQRES   7 C  380  LEU ILE ARG ASN LEU HIS ALA ASN GLY ALA SER PHE PHE          
SEQRES   8 C  380  PHE ILE CYS ILE PHE LEU HIS ILE GLY ARG GLY LEU TYR          
SEQRES   9 C  380  TYR GLY SER TYR LEU TYR LYS GLU THR TRP ASN THR GLY          
SEQRES  10 C  380  VAL ILE LEU LEU LEU THR LEU MET ALA THR ALA PHE VAL          
SEQRES  11 C  380  GLY TYR VAL LEU PRO TRP GLY GLN MET SER PHE TRP GLY          
SEQRES  12 C  380  ALA THR VAL ILE THR ASN LEU PHE SER ALA ILE PRO TYR          
SEQRES  13 C  380  ILE GLY HIS THR LEU VAL GLU TRP ALA TRP GLY GLY PHE          
SEQRES  14 C  380  SER VAL ASP ASN PRO THR LEU THR ARG PHE PHE ALA LEU          
SEQRES  15 C  380  HIS PHE LEU LEU PRO PHE ALA ILE ALA GLY ILE THR ILE          
SEQRES  16 C  380  ILE HIS LEU THR PHE LEU HIS GLU SER GLY SER ASN ASN          
SEQRES  17 C  380  PRO LEU GLY ILE SER SER ASP SER ASP LYS ILE PRO PHE          
SEQRES  18 C  380  HIS PRO TYR TYR SER PHE LYS ASP ILE LEU GLY LEU THR          
SEQRES  19 C  380  LEU MET LEU THR PRO PHE LEU THR LEU ALA LEU PHE SER          
SEQRES  20 C  380  PRO ASN LEU LEU GLY ASP PRO GLU ASN PHE THR PRO ALA          
SEQRES  21 C  380  ASN PRO LEU VAL THR PRO PRO HIS ILE LYS PRO GLU TRP          
SEQRES  22 C  380  TYR PHE LEU PHE ALA TYR ALA ILE LEU ARG SER ILE PRO          
SEQRES  23 C  380  ASN LYS LEU GLY GLY VAL LEU ALA LEU ALA ALA SER VAL          
SEQRES  24 C  380  LEU ILE LEU PHE LEU ILE PRO PHE LEU HIS LYS SER LYS          
SEQRES  25 C  380  GLN ARG THR MET THR PHE ARG PRO LEU SER GLN THR LEU          
SEQRES  26 C  380  PHE TRP LEU LEU VAL ALA ASN LEU LEU ILE LEU THR TRP          
SEQRES  27 C  380  ILE GLY SER GLN PRO VAL GLU HIS PRO PHE ILE ILE ILE          
SEQRES  28 C  380  GLY GLN MET ALA SER LEU SER TYR PHE THR ILE LEU LEU          
SEQRES  29 C  380  ILE LEU PHE PRO THR ILE GLY THR LEU GLU ASN LYS MET          
SEQRES  30 C  380  LEU ASN TYR                                                  
SEQRES   1 D  241  GLY GLU LEU GLU LEU HIS PRO PRO ALA PHE PRO TRP SER          
SEQRES   2 D  241  HIS GLY GLY PRO LEU SER ALA LEU ASP HIS SER SER VAL          
SEQRES   3 D  241  ARG ARG GLY PHE GLN VAL TYR LYS GLN VAL CYS SER ALA          
SEQRES   4 D  241  CYS HIS SER MET ASP TYR VAL ALA PHE ARG ASN LEU ILE          
SEQRES   5 D  241  GLY VAL THR HIS THR GLU ALA GLU ALA LYS ALA LEU ALA          
SEQRES   6 D  241  GLU GLU VAL GLU VAL GLN ASP GLY PRO ASP GLU ASN GLY          
SEQRES   7 D  241  GLU LEU PHE MET ARG PRO GLY LYS ILE SER ASP TYR PHE          
SEQRES   8 D  241  PRO LYS PRO TYR PRO ASN PRO GLU ALA ALA ARG ALA ALA          
SEQRES   9 D  241  ASN ASN GLY ALA LEU PRO PRO ASP LEU SER TYR ILE VAL          
SEQRES  10 D  241  ASN ALA ARG HIS GLY GLY GLU ASP TYR VAL PHE SER LEU          
SEQRES  11 D  241  LEU THR GLY TYR CYS ASP PRO PRO ALA GLY VAL VAL VAL          
SEQRES  12 D  241  ARG GLU GLY LEU HIS TYR ASN PRO TYR PHE PRO GLY GLN          
SEQRES  13 D  241  ALA ILE GLY MET ALA PRO PRO ILE TYR ASN GLU ILE LEU          
SEQRES  14 D  241  GLU TYR ASP ASP GLY THR PRO ALA THR MET SER GLN ILE          
SEQRES  15 D  241  ALA LYS ASP VAL CYS THR PHE LEU ARG TRP ALA ALA GLU          
SEQRES  16 D  241  PRO GLU HIS ASP GLN ARG LYS ARG MET GLY LEU LYS MET          
SEQRES  17 D  241  LEU LEU ILE SER ALA LEU LEU THR SER LEU LEU TYR TYR          
SEQRES  18 D  241  MET LYS ARG HIS LYS TRP SER VAL LEU LYS SER ARG LYS          
SEQRES  19 D  241  MET ALA TYR ARG PRO PRO LYS                                  
SEQRES   1 E  196  VAL HIS ASN ASP VAL THR VAL PRO ASP PHE SER ALA TYR          
SEQRES   2 E  196  ARG ARG GLU ASP VAL MET ASP ALA THR THR SER SER GLN          
SEQRES   3 E  196  THR SER SER GLU ASP ARG LYS GLY PHE SER TYR LEU VAL          
SEQRES   4 E  196  THR ALA THR ALA CYS VAL ALA THR ALA TYR ALA ALA LYS          
SEQRES   5 E  196  ASN VAL VAL THR GLN PHE ILE SER SER LEU SER ALA SER          
SEQRES   6 E  196  ALA ASP VAL LEU ALA LEU SER LYS ILE GLU ILE LYS LEU          
SEQRES   7 E  196  SER ASP ILE PRO GLU GLY LYS ASN VAL ALA PHE LYS TRP          
SEQRES   8 E  196  ARG GLY LYS PRO LEU PHE VAL ARG HIS ARG THR GLN ALA          
SEQRES   9 E  196  GLU ILE ASN GLN GLU ALA GLU VAL ASP VAL SER LYS LEU          
SEQRES  10 E  196  ARG ASP PRO GLN HIS ASP LEU ASP ARG VAL LYS LYS PRO          
SEQRES  11 E  196  GLU TRP VAL ILE LEU VAL GLY VAL CYS THR HIS LEU GLY          
SEQRES  12 E  196  CYS VAL PRO ILE ALA ASN SER GLY ASP PHE GLY GLY TYR          
SEQRES  13 E  196  TYR CYS PRO CYS HIS GLY SER HIS TYR ASP ALA SER GLY          
SEQRES  14 E  196  ARG ILE ARG LYS GLY PRO ALA PRO TYR ASN LEU GLU VAL          
SEQRES  15 E  196  PRO THR TYR GLN PHE VAL GLY ASP ASP LEU VAL VAL VAL          
SEQRES  16 E  196  GLY                                                          
SEQRES   1 F  110  ALA ALA ARG ALA THR VAL ALA GLY GLY GLY ARG LEU MET          
SEQRES   2 F  110  ASP ARG ILE ARG LYS TRP TYR TYR ASN ALA ALA GLY PHE          
SEQRES   3 F  110  ASN LYS TYR GLY LEU MET ARG ASP ASP THR LEU TYR GLU          
SEQRES   4 F  110  ASP ASP ASP VAL LYS GLU ALA LEU LYS ARG LEU PRO LYS          
SEQRES   5 F  110  ASP LEU TYR ASN GLU ARG MET PHE ARG ILE LYS ARG ALA          
SEQRES   6 F  110  LEU ASP LEU SER LEU LYS HIS ARG ILE LEU PRO LYS GLU          
SEQRES   7 F  110  GLN TRP VAL LYS TYR GLU GLU ASP LYS PRO TYR LEU GLU          
SEQRES   8 F  110  PRO TYR LEU LYS GLU VAL ILE ARG GLU ARG LEU GLU ARG          
SEQRES   9 F  110  GLU ALA TRP ASN LYS LYS                                      
SEQRES   1 G   81  GLY ILE HIS PHE GLY ASN LEU ALA ARG VAL ARG HIS ILE          
SEQRES   2 G   81  ILE THR TYR SER LEU SER PRO PHE GLU GLN ARG ALA ILE          
SEQRES   3 G   81  PRO ASN ILE PHE SER ASP ALA LEU PRO ASN VAL TRP ARG          
SEQRES   4 G   81  ARG PHE SER SER GLN VAL PHE LYS VAL ALA PRO PRO PHE          
SEQRES   5 G   81  LEU GLY ALA TYR LEU LEU TYR SER TRP GLY THR GLN GLU          
SEQRES   6 G   81  PHE GLU ARG LEU LYS ARG LYS ASN PRO ALA ASP TYR GLU          
SEQRES   7 G   81  ASN ASP GLN                                                  
SEQRES   1 H   77  LEU ARG GLY SER GLY GLU GLU GLU GLU GLU GLU LEU VAL          
SEQRES   2 H   77  ASP PRO LEU THR THR ILE ARG GLU HIS CYS GLU GLN THR          
SEQRES   3 H   77  GLU LYS CYS VAL LYS ALA ARG GLU ARG LEU GLU LEU CYS          
SEQRES   4 H   77  ASP ALA ARG VAL SER SER ARG SER HIS THR GLU GLU GLN          
SEQRES   5 H   77  CYS THR GLU GLU LEU PHE ASP PHE LEU HIS ALA ARG ASP          
SEQRES   6 H   77  HIS CYS VAL ALA HIS LYS LEU PHE ASN LYS LEU LYS              
SEQRES   1 I   47  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 I   47  UNK UNK ARG PRO LEU LEU CYS ARG GLU SER MET SER GLY          
SEQRES   3 I   47  ARG SER ALA ARG ARG ASP LEU VAL ALA GLY ILE SER LEU          
SEQRES   4 I   47  ASN ALA PRO ALA SER VAL ARG TYR                              
SEQRES   1 J   61  ALA LEU LEU ARG GLN ALA TYR SER ALA LEU PHE ARG ARG          
SEQRES   2 J   61  THR SER THR PHE ALA LEU THR VAL VAL LEU GLY ALA VAL          
SEQRES   3 J   61  LEU PHE GLU ARG ALA PHE ASP GLN GLY ALA ASP ALA ILE          
SEQRES   4 J   61  PHE GLU HIS LEU ASN GLU GLY LYS LEU TRP LYS HIS ILE          
SEQRES   5 J   61  LYS HIS LYS TYR GLU ALA SER GLU GLU                          
SEQRES   1 N  446  ALA ALA THR TYR ALA GLN THR LEU GLN ASN ILE PRO GLU          
SEQRES   2 N  446  THR ASN VAL THR THR LEU ASP ASN GLY LEU ARG VAL ALA          
SEQRES   3 N  446  SER GLU GLU SER SER GLN PRO THR CYS THR VAL GLY VAL          
SEQRES   4 N  446  TRP ILE GLY ALA GLY SER ARG TYR GLU ASN GLU LYS ASN          
SEQRES   5 N  446  ASN GLY ALA GLY TYR PHE VAL GLU HIS LEU ALA PHE LYS          
SEQRES   6 N  446  GLY THR LYS LYS ARG PRO CYS ALA ALA PHE GLU LYS GLU          
SEQRES   7 N  446  VAL GLU SER MET GLY ALA HIS PHE ASN GLY TYR THR SER          
SEQRES   8 N  446  ARG GLU GLN THR ALA PHE TYR ILE LYS ALA LEU SER LYS          
SEQRES   9 N  446  ASP MET PRO LYS VAL VAL GLU LEU LEU ALA ASP VAL VAL          
SEQRES  10 N  446  GLN ASN CYS ALA LEU GLU GLU SER GLN ILE GLU LYS GLU          
SEQRES  11 N  446  ARG GLY VAL ILE LEU GLN GLU LEU LYS GLU MET ASP ASN          
SEQRES  12 N  446  ASP MET THR ASN VAL THR PHE ASP TYR LEU HIS ALA THR          
SEQRES  13 N  446  ALA PHE GLN GLY THR ALA LEU ALA ARG THR VAL GLU GLY          
SEQRES  14 N  446  THR THR GLU ASN ILE LYS HIS LEU THR ARG ALA ASP LEU          
SEQRES  15 N  446  ALA SER TYR ILE ASP THR HIS PHE LYS ALA PRO ARG MET          
SEQRES  16 N  446  VAL LEU ALA ALA ALA GLY GLY ILE SER HIS LYS GLU LEU          
SEQRES  17 N  446  VAL ASP ALA ALA ARG GLN HIS PHE SER GLY VAL SER PHE          
SEQRES  18 N  446  THR TYR LYS GLU ASP ALA VAL PRO ILE LEU PRO ARG CYS          
SEQRES  19 N  446  ARG PHE THR GLY SER GLU ILE ARG ALA ARG ASP ASP ALA          
SEQRES  20 N  446  LEU PRO VAL ALA HIS VAL ALA LEU ALA VAL GLU GLY PRO          
SEQRES  21 N  446  GLY TRP ALA ASP PRO ASP ASN VAL VAL LEU HIS VAL ALA          
SEQRES  22 N  446  ASN ALA ILE ILE GLY ARG TYR ASP ARG THR PHE GLY GLY          
SEQRES  23 N  446  GLY LYS HIS LEU SER SER ARG LEU ALA ALA LEU ALA VAL          
SEQRES  24 N  446  GLU HIS LYS LEU CYS HIS SER PHE GLN THR PHE ASN THR          
SEQRES  25 N  446  SER TYR SER ASP THR GLY LEU PHE GLY PHE HIS PHE VAL          
SEQRES  26 N  446  ALA ASP PRO LEU SER ILE ASP ASP MET MET PHE CYS ALA          
SEQRES  27 N  446  GLN GLY GLU TRP MET ARG LEU CYS THR SER THR THR GLU          
SEQRES  28 N  446  SER GLU VAL LYS ARG ALA LYS ASN HIS LEU ARG SER ALA          
SEQRES  29 N  446  MET VAL ALA GLN LEU ASP GLY THR THR PRO VAL CYS GLU          
SEQRES  30 N  446  THR ILE GLY SER HIS LEU LEU ASN TYR GLY ARG ARG ILE          
SEQRES  31 N  446  SER LEU GLU GLU TRP ASP SER ARG ILE SER ALA VAL ASP          
SEQRES  32 N  446  ALA ARG MET VAL ARG ASP VAL CYS SER LYS TYR ILE TYR          
SEQRES  33 N  446  ASP LYS CYS PRO ALA LEU ALA ALA VAL GLY PRO ILE GLU          
SEQRES  34 N  446  GLN LEU LEU ASP TYR ASN ARG ILE ARG SER GLY MET TYR          
SEQRES  35 N  446  TRP ILE ARG PHE                                              
SEQRES   1 O  441  SER LEU LYS VAL ALA PRO LYS VAL ALA VAL SER ALA ALA          
SEQRES   2 O  441  ALA GLU ARG VAL LYS LEU CYS PRO GLY ALA GLU ASP LEU          
SEQRES   3 O  441  GLU ILE THR LYS LEU PRO ASN GLY LEU ILE ILE ALA SER          
SEQRES   4 O  441  LEU GLU ASN PHE SER PRO ALA SER ARG ILE GLY VAL PHE          
SEQRES   5 O  441  ILE LYS ALA GLY SER ARG TYR GLU THR THR ALA ASN LEU          
SEQRES   6 O  441  GLY THR ALA HIS LEU LEU ARG LEU ALA SER PRO LEU THR          
SEQRES   7 O  441  THR LYS GLY ALA SER SER PHE ARG ILE THR ARG GLY ILE          
SEQRES   8 O  441  GLU ALA VAL GLY GLY SER LEU SER VAL TYR SER THR ARG          
SEQRES   9 O  441  GLU LYS MET THR TYR CYS VAL GLU CYS LEU ARG ASP HIS          
SEQRES  10 O  441  VAL ASP THR VAL MET GLU TYR LEU LEU ASN VAL THR THR          
SEQRES  11 O  441  ALA PRO GLU PHE ARG PRO TRP GLU VAL THR ASP LEU GLN          
SEQRES  12 O  441  PRO GLN LEU LYS VAL ASP LYS ALA VAL ALA PHE GLN SER          
SEQRES  13 O  441  PRO GLN VAL GLY VAL LEU GLU ASN LEU HIS ALA ALA ALA          
SEQRES  14 O  441  TYR LYS THR ALA LEU ALA ASN PRO LEU TYR CYS PRO ASP          
SEQRES  15 O  441  TYR ARG ILE GLY LYS ILE THR SER GLU GLN LEU HIS HIS          
SEQRES  16 O  441  PHE VAL GLN ASN ASN PHE THR SER ALA ARG MET ALA LEU          
SEQRES  17 O  441  VAL GLY ILE GLY VAL LYS HIS SER ASP LEU LYS GLN VAL          
SEQRES  18 O  441  ALA GLU GLN PHE LEU ASN ILE ARG SER GLY ALA GLY THR          
SEQRES  19 O  441  SER SER ALA LYS ALA THR TYR TRP GLY GLY GLU ILE ARG          
SEQRES  20 O  441  GLU GLN ASN GLY HIS SER LEU VAL HIS ALA ALA VAL VAL          
SEQRES  21 O  441  THR GLU GLY ALA ALA VAL GLY SER ALA GLU ALA ASN ALA          
SEQRES  22 O  441  PHE SER VAL LEU GLN HIS VAL LEU GLY ALA GLY PRO LEU          
SEQRES  23 O  441  ILE LYS ARG GLY SER SER VAL THR SER LYS LEU TYR GLN          
SEQRES  24 O  441  GLY VAL ALA LYS ALA THR THR GLN PRO PHE ASP ALA SER          
SEQRES  25 O  441  ALA PHE ASN VAL ASN TYR SER ASP SER GLY LEU PHE GLY          
SEQRES  26 O  441  PHE TYR THR ILE SER GLN ALA ALA HIS ALA GLY GLU VAL          
SEQRES  27 O  441  ILE ARG ALA ALA MET ASN GLN LEU LYS ALA ALA ALA GLN          
SEQRES  28 O  441  GLY GLY VAL THR GLU GLU ASP VAL THR LYS ALA LYS ASN          
SEQRES  29 O  441  GLN LEU LYS ALA THR TYR LEU MET SER VAL GLU THR ALA          
SEQRES  30 O  441  GLN GLY LEU LEU ASN GLU ILE GLY SER GLU ALA LEU LEU          
SEQRES  31 O  441  SER GLY THR HIS THR ALA PRO SER VAL VAL ALA GLN LYS          
SEQRES  32 O  441  ILE ASP SER VAL THR SER ALA ASP VAL VAL ASN ALA ALA          
SEQRES  33 O  441  LYS LYS PHE VAL SER GLY LYS LYS SER MET ALA ALA SER          
SEQRES  34 O  441  GLY ASP LEU GLY SER THR PRO PHE LEU ASP GLU LEU              
SEQRES   1 P  380  MET ALA PRO ASN ILE ARG LYS SER HIS PRO LEU LEU LYS          
SEQRES   2 P  380  MET ILE ASN ASN SER LEU ILE ASP LEU PRO ALA PRO SER          
SEQRES   3 P  380  ASN ILE SER ALA TRP TRP ASN PHE GLY SER LEU LEU ALA          
SEQRES   4 P  380  VAL CYS LEU MET THR GLN ILE LEU THR GLY LEU LEU LEU          
SEQRES   5 P  380  ALA MET HIS TYR THR ALA ASP THR SER LEU ALA PHE SER          
SEQRES   6 P  380  SER VAL ALA HIS THR CYS ARG ASN VAL GLN TYR GLY TRP          
SEQRES   7 P  380  LEU ILE ARG ASN LEU HIS ALA ASN GLY ALA SER PHE PHE          
SEQRES   8 P  380  PHE ILE CYS ILE PHE LEU HIS ILE GLY ARG GLY LEU TYR          
SEQRES   9 P  380  TYR GLY SER TYR LEU TYR LYS GLU THR TRP ASN THR GLY          
SEQRES  10 P  380  VAL ILE LEU LEU LEU THR LEU MET ALA THR ALA PHE VAL          
SEQRES  11 P  380  GLY TYR VAL LEU PRO TRP GLY GLN MET SER PHE TRP GLY          
SEQRES  12 P  380  ALA THR VAL ILE THR ASN LEU PHE SER ALA ILE PRO TYR          
SEQRES  13 P  380  ILE GLY HIS THR LEU VAL GLU TRP ALA TRP GLY GLY PHE          
SEQRES  14 P  380  SER VAL ASP ASN PRO THR LEU THR ARG PHE PHE ALA LEU          
SEQRES  15 P  380  HIS PHE LEU LEU PRO PHE ALA ILE ALA GLY ILE THR ILE          
SEQRES  16 P  380  ILE HIS LEU THR PHE LEU HIS GLU SER GLY SER ASN ASN          
SEQRES  17 P  380  PRO LEU GLY ILE SER SER ASP SER ASP LYS ILE PRO PHE          
SEQRES  18 P  380  HIS PRO TYR TYR SER PHE LYS ASP ILE LEU GLY LEU THR          
SEQRES  19 P  380  LEU MET LEU THR PRO PHE LEU THR LEU ALA LEU PHE SER          
SEQRES  20 P  380  PRO ASN LEU LEU GLY ASP PRO GLU ASN PHE THR PRO ALA          
SEQRES  21 P  380  ASN PRO LEU VAL THR PRO PRO HIS ILE LYS PRO GLU TRP          
SEQRES  22 P  380  TYR PHE LEU PHE ALA TYR ALA ILE LEU ARG SER ILE PRO          
SEQRES  23 P  380  ASN LYS LEU GLY GLY VAL LEU ALA LEU ALA ALA SER VAL          
SEQRES  24 P  380  LEU ILE LEU PHE LEU ILE PRO PHE LEU HIS LYS SER LYS          
SEQRES  25 P  380  GLN ARG THR MET THR PHE ARG PRO LEU SER GLN THR LEU          
SEQRES  26 P  380  PHE TRP LEU LEU VAL ALA ASN LEU LEU ILE LEU THR TRP          
SEQRES  27 P  380  ILE GLY SER GLN PRO VAL GLU HIS PRO PHE ILE ILE ILE          
SEQRES  28 P  380  GLY GLN MET ALA SER LEU SER TYR PHE THR ILE LEU LEU          
SEQRES  29 P  380  ILE LEU PHE PRO THR ILE GLY THR LEU GLU ASN LYS MET          
SEQRES  30 P  380  LEU ASN TYR                                                  
SEQRES   1 Q  241  GLY GLU LEU GLU LEU HIS PRO PRO ALA PHE PRO TRP SER          
SEQRES   2 Q  241  HIS GLY GLY PRO LEU SER ALA LEU ASP HIS SER SER VAL          
SEQRES   3 Q  241  ARG ARG GLY PHE GLN VAL TYR LYS GLN VAL CYS SER ALA          
SEQRES   4 Q  241  CYS HIS SER MET ASP TYR VAL ALA PHE ARG ASN LEU ILE          
SEQRES   5 Q  241  GLY VAL THR HIS THR GLU ALA GLU ALA LYS ALA LEU ALA          
SEQRES   6 Q  241  GLU GLU VAL GLU VAL GLN ASP GLY PRO ASP GLU ASN GLY          
SEQRES   7 Q  241  GLU LEU PHE MET ARG PRO GLY LYS ILE SER ASP TYR PHE          
SEQRES   8 Q  241  PRO LYS PRO TYR PRO ASN PRO GLU ALA ALA ARG ALA ALA          
SEQRES   9 Q  241  ASN ASN GLY ALA LEU PRO PRO ASP LEU SER TYR ILE VAL          
SEQRES  10 Q  241  ASN ALA ARG HIS GLY GLY GLU ASP TYR VAL PHE SER LEU          
SEQRES  11 Q  241  LEU THR GLY TYR CYS ASP PRO PRO ALA GLY VAL VAL VAL          
SEQRES  12 Q  241  ARG GLU GLY LEU HIS TYR ASN PRO TYR PHE PRO GLY GLN          
SEQRES  13 Q  241  ALA ILE GLY MET ALA PRO PRO ILE TYR ASN GLU ILE LEU          
SEQRES  14 Q  241  GLU TYR ASP ASP GLY THR PRO ALA THR MET SER GLN ILE          
SEQRES  15 Q  241  ALA LYS ASP VAL CYS THR PHE LEU ARG TRP ALA ALA GLU          
SEQRES  16 Q  241  PRO GLU HIS ASP GLN ARG LYS ARG MET GLY LEU LYS MET          
SEQRES  17 Q  241  LEU LEU ILE SER ALA LEU LEU THR SER LEU LEU TYR TYR          
SEQRES  18 Q  241  MET LYS ARG HIS LYS TRP SER VAL LEU LYS SER ARG LYS          
SEQRES  19 Q  241  MET ALA TYR ARG PRO PRO LYS                                  
SEQRES   1 R  196  VAL HIS ASN ASP VAL THR VAL PRO ASP PHE SER ALA TYR          
SEQRES   2 R  196  ARG ARG GLU ASP VAL MET ASP ALA THR THR SER SER GLN          
SEQRES   3 R  196  THR SER SER GLU ASP ARG LYS GLY PHE SER TYR LEU VAL          
SEQRES   4 R  196  THR ALA THR ALA CYS VAL ALA THR ALA TYR ALA ALA LYS          
SEQRES   5 R  196  ASN VAL VAL THR GLN PHE ILE SER SER LEU SER ALA SER          
SEQRES   6 R  196  ALA ASP VAL LEU ALA LEU SER LYS ILE GLU ILE LYS LEU          
SEQRES   7 R  196  SER ASP ILE PRO GLU GLY LYS ASN VAL ALA PHE LYS TRP          
SEQRES   8 R  196  ARG GLY LYS PRO LEU PHE VAL ARG HIS ARG THR GLN ALA          
SEQRES   9 R  196  GLU ILE ASN GLN GLU ALA GLU VAL ASP VAL SER LYS LEU          
SEQRES  10 R  196  ARG ASP PRO GLN HIS ASP LEU ASP ARG VAL LYS LYS PRO          
SEQRES  11 R  196  GLU TRP VAL ILE LEU VAL GLY VAL CYS THR HIS LEU GLY          
SEQRES  12 R  196  CYS VAL PRO ILE ALA ASN SER GLY ASP PHE GLY GLY TYR          
SEQRES  13 R  196  TYR CYS PRO CYS HIS GLY SER HIS TYR ASP ALA SER GLY          
SEQRES  14 R  196  ARG ILE ARG LYS GLY PRO ALA PRO TYR ASN LEU GLU VAL          
SEQRES  15 R  196  PRO THR TYR GLN PHE VAL GLY ASP ASP LEU VAL VAL VAL          
SEQRES  16 R  196  GLY                                                          
SEQRES   1 S  110  ALA ALA ARG ALA THR VAL ALA GLY GLY GLY ARG LEU MET          
SEQRES   2 S  110  ASP ARG ILE ARG LYS TRP TYR TYR ASN ALA ALA GLY PHE          
SEQRES   3 S  110  ASN LYS TYR GLY LEU MET ARG ASP ASP THR LEU TYR GLU          
SEQRES   4 S  110  ASP ASP ASP VAL LYS GLU ALA LEU LYS ARG LEU PRO LYS          
SEQRES   5 S  110  ASP LEU TYR ASN GLU ARG MET PHE ARG ILE LYS ARG ALA          
SEQRES   6 S  110  LEU ASP LEU SER LEU LYS HIS ARG ILE LEU PRO LYS GLU          
SEQRES   7 S  110  GLN TRP VAL LYS TYR GLU GLU ASP LYS PRO TYR LEU GLU          
SEQRES   8 S  110  PRO TYR LEU LYS GLU VAL ILE ARG GLU ARG LEU GLU ARG          
SEQRES   9 S  110  GLU ALA TRP ASN LYS LYS                                      
SEQRES   1 T   81  GLY ILE HIS PHE GLY ASN LEU ALA ARG VAL ARG HIS ILE          
SEQRES   2 T   81  ILE THR TYR SER LEU SER PRO PHE GLU GLN ARG ALA ILE          
SEQRES   3 T   81  PRO ASN ILE PHE SER ASP ALA LEU PRO ASN VAL TRP ARG          
SEQRES   4 T   81  ARG PHE SER SER GLN VAL PHE LYS VAL ALA PRO PRO PHE          
SEQRES   5 T   81  LEU GLY ALA TYR LEU LEU TYR SER TRP GLY THR GLN GLU          
SEQRES   6 T   81  PHE GLU ARG LEU LYS ARG LYS ASN PRO ALA ASP TYR GLU          
SEQRES   7 T   81  ASN ASP GLN                                                  
SEQRES   1 U   77  LEU ARG GLY SER GLY GLU GLU GLU GLU GLU GLU LEU VAL          
SEQRES   2 U   77  ASP PRO LEU THR THR ILE ARG GLU HIS CYS GLU GLN THR          
SEQRES   3 U   77  GLU LYS CYS VAL LYS ALA ARG GLU ARG LEU GLU LEU CYS          
SEQRES   4 U   77  ASP ALA ARG VAL SER SER ARG SER HIS THR GLU GLU GLN          
SEQRES   5 U   77  CYS THR GLU GLU LEU PHE ASP PHE LEU HIS ALA ARG ASP          
SEQRES   6 U   77  HIS CYS VAL ALA HIS LYS LEU PHE ASN LYS LEU LYS              
SEQRES   1 V   47  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 V   47  UNK UNK ARG PRO LEU LEU CYS ARG GLU SER MET SER GLY          
SEQRES   3 V   47  ARG SER ALA ARG ARG ASP LEU VAL ALA GLY ILE SER LEU          
SEQRES   4 V   47  ASN ALA PRO ALA SER VAL ARG TYR                              
SEQRES   1 W   61  ALA LEU LEU ARG GLN ALA TYR SER ALA LEU PHE ARG ARG          
SEQRES   2 W   61  THR SER THR PHE ALA LEU THR VAL VAL LEU GLY ALA VAL          
SEQRES   3 W   61  LEU PHE GLU ARG ALA PHE ASP GLN GLY ALA ASP ALA ILE          
SEQRES   4 W   61  PHE GLU HIS LEU ASN GLU GLY LYS LEU TRP LYS HIS ILE          
SEQRES   5 W   61  LYS HIS LYS TYR GLU ALA SER GLU GLU                          
HET    PEE  A2008      21                                                       
HET    UNL  A3016       1                                                       
HET    HEM  C 501      43                                                       
HET    HEM  C 502      43                                                       
HET    3H1  C2001      28                                                       
HET    3H1  C2002      28                                                       
HET    CDL  C2003      50                                                       
HET    PEE  C2007      49                                                       
HET    UNL  C2010       1                                                       
HET    UNL  C2104       1                                                       
HET    UNL  C3015       1                                                       
HET    UNL  C3106       1                                                       
HET    GOL  C2011       6                                                       
HET    HEC  D 501      43                                                       
HET    BOG  D2009      20                                                       
HET    FES  E 501       4                                                       
HET    PEE  E2005      50                                                       
HET    UNL  E2105       1                                                       
HET    CDL  G2004      40                                                       
HET    HEM  P 501      43                                                       
HET    HEM  P 502      43                                                       
HET    UNL  P2015       1                                                       
HET    UNL  P2106       1                                                       
HET    3H1  P3001      28                                                       
HET    3H1  P3002      28                                                       
HET    CDL  P3003      50                                                       
HET    PEE  P3007      49                                                       
HET    PEE  P3008       5                                                       
HET    UNL  P3010       1                                                       
HET    UNL  P3103       1                                                       
HET    UNL  P3104       1                                                       
HET    GOL  P3011       6                                                       
HET    HEC  Q 501      43                                                       
HET    FES  R 501       4                                                       
HET    UNL  R2103       1                                                       
HET    PEE  R3005      50                                                       
HET    BOG  R3009      20                                                       
HET    CDL  T3004      40                                                       
HETNAM     PEE PHOSPHATIDYLETHANOLAMINE                                         
HETNAM     UNL UNKNOWN LIGAND                                                   
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     3H1 3-CHLORO-4,6-DIHYDROXY-2-METHYL-5-{(2E,4E)-3-METHYL-5-           
HETNAM   2 3H1  [(1R,2R,6R)-1,2,6-TRIMETHYL-3-OXOCYCLOHEXYL]PENTA-2,4-          
HETNAM   3 3H1  DIEN-1-YL}BENZALDEHYDE                                          
HETNAM     CDL CARDIOLIPIN                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     HEC HEME C                                                           
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETSYN     PEE D-GLYCEROL-1-[(2-AMINO-ETHYL)PHOSPHATE]-2,3-                     
HETSYN   2 PEE  DIOCTADECANOATE, 2,3-DIOCTADECANOYL-GLYCEROL-1-[(2-             
HETSYN   3 PEE  AMINO-ETHYL)PHOSPHATE]                                          
HETSYN     HEM HEME                                                             
HETSYN     3H1 ASCOCHLORIN                                                      
HETSYN     CDL DIPHOSPHATIDYL GLYCEROL; BIS-(1,2-DIACYL-SN-GLYCERO-3-           
HETSYN   2 CDL  PHOSPHO)-1',3'-SN-GLYCEROL                                      
FORMUL  21  PEE    6(C41 H83 N O8 P 1+)                                         
FORMUL  23  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  25  3H1    4(C23 H29 CL O4)                                             
FORMUL  27  CDL    4(C81 H156 O17 P2 2-)                                        
FORMUL  33  GOL    2(C3 H8 O3)                                                  
FORMUL  34  HEC    2(C34 H34 FE N4 O4)                                          
FORMUL  35  BOG    2(C14 H28 O6)                                                
FORMUL  36  FES    2(FE2 S2)                                                    
FORMUL  59  HOH   *14(H2 O)                                                     
HELIX    1   1 THR A    3  ILE A   11  1                                   9    
HELIX    2   2 GLY A   54  HIS A   61  1                                   8    
HELIX    3   3 PRO A   71  SER A   81  1                                  11    
HELIX    4   4 ASP A  105  ASN A  119  1                                  15    
HELIX    5   5 GLU A  123  GLU A  128  1                                   6    
HELIX    6   6 LYS A  129  ASP A  142  1                                  14    
HELIX    7   7 ASP A  144  PHE A  158  1                                  15    
HELIX    8   8 THR A  170  LEU A  177  1                                   8    
HELIX    9   9 THR A  178  PHE A  190  1                                  13    
HELIX   10  10 LYS A  191  ARG A  194  5                                   4    
HELIX   11  11 SER A  204  PHE A  216  1                                  13    
HELIX   12  12 PRO A  265  GLY A  278  1                                  14    
HELIX   13  13 GLY A  286  LEU A  290  5                                   5    
HELIX   14  14 SER A  292  LYS A  302  1                                  11    
HELIX   15  15 ASP A  327  LEU A  329  5                                   3    
HELIX   16  16 SER A  330  SER A  348  1                                  19    
HELIX   17  17 THR A  350  ALA A  367  1                                  18    
HELIX   18  18 GLN A  368  ASP A  370  5                                   3    
HELIX   19  19 GLY A  371  GLY A  387  1                                  17    
HELIX   20  20 SER A  391  VAL A  402  1                                  12    
HELIX   21  21 ASP A  403  ILE A  415  1                                  13    
HELIX   22  22 ASP A  433  GLY A  440  1                                   8    
HELIX   23  23 GLY B   64  ALA B   72  1                                   9    
HELIX   24  24 SER B   81  ALA B   91  1                                  11    
HELIX   25  25 HIS B  115  ALA B  129  1                                  15    
HELIX   26  26 ARG B  133  GLN B  141  1                                   9    
HELIX   27  27 PRO B  142  PHE B  152  1                                  11    
HELIX   28  28 SER B  154  TYR B  168  1                                  15    
HELIX   29  29 THR B  170  ASN B  174  5                                   5    
HELIX   30  30 PRO B  179  ILE B  183  5                                   5    
HELIX   31  31 THR B  187  ASN B  197  1                                  11    
HELIX   32  32 LYS B  212  LEU B  224  1                                  13    
HELIX   33  33 GLU B  268  GLY B  280  1                                  13    
HELIX   34  34 SER B  293  LYS B  301  1                                   9    
HELIX   35  35 HIS B  332  ALA B  346  1                                  15    
HELIX   36  36 GLU B  355  VAL B  372  1                                  18    
HELIX   37  37 THR B  374  LEU B  388  1                                  15    
HELIX   38  38 SER B  396  SER B  404  1                                   9    
HELIX   39  39 THR B  406  GLY B  420  1                                  15    
HELIX   40  40 ASP B  429  THR B  433  5                                   5    
HELIX   41  41 PHE B  435  LEU B  439  5                                   5    
HELIX   42  42 LEU C   11  SER C   18  1                                   8    
HELIX   43  43 SER C   29  TRP C   32  5                                   4    
HELIX   44  44 ASN C   33  MET C   54  1                                  22    
HELIX   45  45 LEU C   62  ASN C   73  1                                  12    
HELIX   46  46 TYR C   76  TYR C  105  1                                  30    
HELIX   47  47 GLY C  106  LEU C  109  5                                   4    
HELIX   48  48 TYR C  110  LEU C  134  1                                  25    
HELIX   49  49 GLY C  137  LEU C  150  1                                  14    
HELIX   50  50 PHE C  151  ILE C  154  5                                   4    
HELIX   51  51 TYR C  156  GLY C  167  1                                  12    
HELIX   52  52 ASP C  172  GLY C  205  1                                  34    
HELIX   53  53 PHE C  221  SER C  247  1                                  27    
HELIX   54  54 PRO C  254  THR C  258  5                                   5    
HELIX   55  55 GLU C  272  TYR C  274  5                                   3    
HELIX   56  56 PHE C  275  ARG C  283  1                                   9    
HELIX   57  57 ASN C  287  ILE C  301  1                                  15    
HELIX   58  58 LEU C  302  HIS C  309  5                                   8    
HELIX   59  59 ARG C  319  SER C  341  1                                  23    
HELIX   60  60 PRO C  347  ILE C  365  1                                  19    
HELIX   61  61 ILE C  365  LEU C  378  1                                  14    
HELIX   62  62 ASP D   22  VAL D   36  1                                  15    
HELIX   63  63 CYS D   37  CYS D   40  5                                   4    
HELIX   64  64 ALA D   47  ILE D   52  1                                   6    
HELIX   65  65 THR D   57  GLU D   67  1                                  11    
HELIX   66  66 ASN D   97  ALA D  104  1                                   8    
HELIX   67  67 TYR D  115  ARG D  120  1                                   6    
HELIX   68  68 GLY D  122  GLY D  133  1                                  12    
HELIX   69  69 THR D  178  GLU D  195  1                                  18    
HELIX   70  70 GLU D  197  ARG D  233  1                                  37    
HELIX   71  71 ARG E   15  MET E   19  5                                   5    
HELIX   72  72 SER E   25  SER E   60  1                                  36    
HELIX   73  73 THR E  102  ASN E  107  1                                   6    
HELIX   74  74 GLN E  108  GLU E  111  5                                   4    
HELIX   75  75 HIS E  122  ARG E  126  5                                   5    
HELIX   76  76 ARG F   11  GLY F   25  1                                  15    
HELIX   77  77 PHE F   26  GLY F   30  5                                   5    
HELIX   78  78 MET F   32  LEU F   37  5                                   6    
HELIX   79  79 ASP F   40  ARG F   49  1                                  10    
HELIX   80  80 PRO F   51  HIS F   72  1                                  22    
HELIX   81  81 PRO F   76  TRP F   80  5                                   5    
HELIX   82  82 LEU F   90  ASN F  108  1                                  19    
HELIX   83  83 PRO G   20  GLN G   23  5                                   4    
HELIX   84  84 ASP G   32  PHE G   46  1                                  15    
HELIX   85  85 VAL G   48  LEU G   69  1                                  22    
HELIX   86  86 ASN G   73  TYR G   77  5                                   5    
HELIX   87  87 ASP H   15  GLU H   25  1                                  11    
HELIX   88  88 THR H   27  ARG H   47  1                                  21    
HELIX   89  89 CYS H   54  HIS H   71  1                                  18    
HELIX   90  90 LYS H   72  LEU H   77  1                                   6    
HELIX   91  91 CYS I   51  SER I   56  1                                   6    
HELIX   92  92 ALA J    4  LEU J   13  1                                  10    
HELIX   93  93 ARG J   16  ASN J   47  1                                  32    
HELIX   94  94 LEU J   51  LYS J   56  1                                   6    
HELIX   95  95 HIS J   57  TYR J   59  5                                   3    
HELIX   96  96 THR N    3  ILE N   11  1                                   9    
HELIX   97  97 GLY N   54  HIS N   61  1                                   8    
HELIX   98  98 PRO N   71  SER N   81  1                                  11    
HELIX   99  99 ASP N  105  GLN N  118  1                                  14    
HELIX  100 100 LYS N  129  ASP N  142  1                                  14    
HELIX  101 101 ASP N  144  PHE N  158  1                                  15    
HELIX  102 102 THR N  170  LEU N  177  1                                   8    
HELIX  103 103 THR N  178  PHE N  190  1                                  13    
HELIX  104 104 LYS N  191  ARG N  194  5                                   4    
HELIX  105 105 SER N  204  PHE N  216  1                                  13    
HELIX  106 106 TYR N  223  ALA N  227  5                                   5    
HELIX  107 107 PRO N  265  GLY N  278  1                                  14    
HELIX  108 108 GLY N  286  LEU N  290  5                                   5    
HELIX  109 109 SER N  292  LYS N  302  1                                  11    
HELIX  110 110 ASP N  327  LEU N  329  5                                   3    
HELIX  111 111 SER N  330  THR N  349  1                                  20    
HELIX  112 112 THR N  350  ALA N  367  1                                  18    
HELIX  113 113 GLN N  368  ASP N  370  5                                   3    
HELIX  114 114 GLY N  371  GLY N  387  1                                  17    
HELIX  115 115 SER N  391  VAL N  402  1                                  12    
HELIX  116 116 ASP N  403  ILE N  415  1                                  13    
HELIX  117 117 ASP N  433  GLY N  440  1                                   8    
HELIX  118 118 GLY O   64  ALA O   72  1                                   9    
HELIX  119 119 SER O   81  ALA O   91  1                                  11    
HELIX  120 120 HIS O  115  ALA O  129  1                                  15    
HELIX  121 121 ARG O  133  GLN O  141  1                                   9    
HELIX  122 122 PRO O  142  PHE O  152  1                                  11    
HELIX  123 123 SER O  154  TYR O  168  1                                  15    
HELIX  124 124 THR O  170  ASN O  174  5                                   5    
HELIX  125 125 PRO O  179  ILE O  183  5                                   5    
HELIX  126 126 THR O  187  ASN O  197  1                                  11    
HELIX  127 127 LYS O  212  PHE O  223  1                                  12    
HELIX  128 128 ALA O  267  GLY O  280  1                                  14    
HELIX  129 129 SER O  293  LYS O  301  1                                   9    
HELIX  130 130 HIS O  332  ALA O  346  1                                  15    
HELIX  131 131 GLU O  355  VAL O  372  1                                  18    
HELIX  132 132 THR O  374  SER O  389  1                                  16    
HELIX  133 133 SER O  396  SER O  404  1                                   9    
HELIX  134 134 THR O  406  GLY O  420  1                                  15    
HELIX  135 135 ASP O  429  THR O  433  5                                   5    
HELIX  136 136 PHE O  435  LEU O  439  5                                   5    
HELIX  137 137 LEU P   11  SER P   18  1                                   8    
HELIX  138 138 SER P   29  TRP P   32  5                                   4    
HELIX  139 139 ASN P   33  MET P   54  1                                  22    
HELIX  140 140 ASP P   59  ASN P   73  1                                  15    
HELIX  141 141 TYR P   76  TYR P  105  1                                  30    
HELIX  142 142 GLY P  106  LEU P  109  5                                   4    
HELIX  143 143 TYR P  110  LEU P  134  1                                  25    
HELIX  144 144 GLY P  137  LEU P  150  1                                  14    
HELIX  145 145 PHE P  151  ILE P  154  5                                   4    
HELIX  146 146 GLY P  158  GLY P  167  1                                  10    
HELIX  147 147 ASP P  172  GLY P  205  1                                  34    
HELIX  148 148 PHE P  221  SER P  247  1                                  27    
HELIX  149 149 PRO P  254  THR P  258  5                                   5    
HELIX  150 150 GLU P  272  TYR P  274  5                                   3    
HELIX  151 151 PHE P  275  ARG P  283  1                                   9    
HELIX  152 152 ASN P  287  ILE P  301  1                                  15    
HELIX  153 153 LEU P  302  HIS P  309  5                                   8    
HELIX  154 154 ARG P  319  SER P  341  1                                  23    
HELIX  155 155 PRO P  347  ILE P  365  1                                  19    
HELIX  156 156 ILE P  365  LEU P  378  1                                  14    
HELIX  157 157 ASP Q   22  VAL Q   36  1                                  15    
HELIX  158 158 CYS Q   37  CYS Q   40  5                                   4    
HELIX  159 159 ALA Q   47  ILE Q   52  1                                   6    
HELIX  160 160 THR Q   57  GLU Q   67  1                                  11    
HELIX  161 161 ASN Q   97  ALA Q  104  1                                   8    
HELIX  162 162 TYR Q  115  ARG Q  120  1                                   6    
HELIX  163 163 GLY Q  122  GLY Q  133  1                                  12    
HELIX  164 164 THR Q  178  GLU Q  195  1                                  18    
HELIX  165 165 GLU Q  197  SER Q  232  1                                  36    
HELIX  166 166 VAL R    1  VAL R    5  5                                   5    
HELIX  167 167 ARG R   15  MET R   19  5                                   5    
HELIX  168 168 SER R   28  SER R   61  1                                  34    
HELIX  169 169 THR R  102  ASN R  107  1                                   6    
HELIX  170 170 GLN R  108  GLU R  111  5                                   4    
HELIX  171 171 HIS R  122  ARG R  126  5                                   5    
HELIX  172 172 LEU S   12  GLY S   25  1                                  14    
HELIX  173 173 PHE S   26  GLY S   30  5                                   5    
HELIX  174 174 MET S   32  THR S   36  5                                   5    
HELIX  175 175 ASP S   40  ARG S   49  1                                  10    
HELIX  176 176 PRO S   51  HIS S   72  1                                  22    
HELIX  177 177 PRO S   76  TRP S   80  5                                   5    
HELIX  178 178 LEU S   90  LYS S  110  1                                  21    
HELIX  179 179 PRO T   20  GLN T   23  5                                   4    
HELIX  180 180 ASP T   32  PHE T   46  1                                  15    
HELIX  181 181 VAL T   48  LEU T   69  1                                  22    
HELIX  182 182 ASN T   73  TYR T   77  5                                   5    
HELIX  183 183 ASP U   15  GLU U   25  1                                  11    
HELIX  184 184 THR U   27  ARG U   47  1                                  21    
HELIX  185 185 CYS U   54  PHE U   74  1                                  21    
HELIX  186 186 CYS V   51  MET V   55  5                                   5    
HELIX  187 187 ALA W    4  LEU W   13  1                                  10    
HELIX  188 188 ARG W   16  ASN W   47  1                                  32    
HELIX  189 189 LEU W   51  LYS W   56  1                                   6    
HELIX  190 190 HIS W   57  TYR W   59  5                                   3    
SHEET    1   A 6 ASN A  15  THR A  18  0                                        
SHEET    2   A 6 ARG A  24  GLU A  29 -1  O  VAL A  25   N  THR A  17           
SHEET    3   A 6 VAL A 196  GLY A 201  1  O  LEU A 197   N  ALA A  26           
SHEET    4   A 6 THR A  34  VAL A  39 -1  N  GLY A  38   O  ALA A 198           
SHEET    5   A 6 THR A  95  LEU A 102 -1  O  ILE A  99   N  VAL A  37           
SHEET    6   A 6 HIS A  85  THR A  90 -1  N  HIS A  85   O  LYS A 100           
SHEET    1   B 8 ARG A 279  ASP A 281  0                                        
SHEET    2   B 8 SER A 306  SER A 313 -1  O  PHE A 307   N  TYR A 280           
SHEET    3   B 8 GLY A 318  ALA A 326 -1  O  LEU A 319   N  THR A 312           
SHEET    4   B 8 ALA A 251  GLU A 258 -1  N  ALA A 251   O  ALA A 326           
SHEET    5   B 8 ALA A 421  GLY A 426 -1  O  VAL A 425   N  HIS A 252           
SHEET    6   B 8 SER A 239  ASP A 245  1  N  ALA A 243   O  ALA A 424           
SHEET    7   B 8 ARG G  11  LEU G  18 -1  O  THR G  15   N  ARG A 242           
SHEET    8   B 8 LYS D 234  TYR D 237 -1  N  LYS D 234   O  TYR G  16           
SHEET    1   C 2 ILE B  26  THR B  27  0                                        
SHEET    2   C 2 ILE B  35  ALA B  36 -1  O  ILE B  35   N  THR B  27           
SHEET    1   D 2 ALA B  44  SER B  45  0                                        
SHEET    2   D 2 CYS B 111  LEU B 112 -1  O  CYS B 111   N  SER B  45           
SHEET    1   E 5 MET B 204  LEU B 206  0                                        
SHEET    2   E 5 GLY B  48  ILE B  51 -1  N  PHE B  50   O  ALA B 205           
SHEET    3   E 5 LYS B 104  VAL B 109 -1  O  TYR B 107   N  VAL B  49           
SHEET    4   E 5 LEU B  96  THR B 101 -1  N  TYR B  99   O  THR B 106           
SHEET    5   E 5 ALA I  66  SER I  69 -1  O  ALA I  66   N  SER B 100           
SHEET    1   F 5 GLU B 243  GLN B 247  0                                        
SHEET    2   F 5 SER B 423  GLY B 428  1  O  ALA B 426   N  GLU B 246           
SHEET    3   F 5 LEU B 252  GLU B 260 -1  N  VAL B 258   O  SER B 423           
SHEET    4   F 5 SER B 319  GLN B 329 -1  O  THR B 326   N  ALA B 255           
SHEET    5   F 5 PHE B 307  TYR B 316 -1  N  PHE B 312   O  GLY B 323           
SHEET    1   G 2 PRO C  23  PRO C  25  0                                        
SHEET    2   G 2 LYS C 218  PRO C 220 -1  O  ILE C 219   N  ALA C  24           
SHEET    1   H 2 HIS D 148  TYR D 149  0                                        
SHEET    2   H 2 ALA D 157  ILE D 158 -1  O  ILE D 158   N  HIS D 148           
SHEET    1   I 3 ILE E  74  ILE E  76  0                                        
SHEET    2   I 3 VAL E 193  VAL E 195 -1  O  VAL E 193   N  ILE E  76           
SHEET    3   I 3 TYR E 185  GLN E 186 -1  N  GLN E 186   O  VAL E 194           
SHEET    1   J 3 LYS E  85  PHE E  89  0                                        
SHEET    2   J 3 LEU E  96  HIS E 100 -1  O  LEU E  96   N  PHE E  89           
SHEET    3   J 3 TRP E 132  LEU E 135 -1  O  LEU E 135   N  PHE E  97           
SHEET    1   K 4 ILE E 147  ALA E 148  0                                        
SHEET    2   K 4 TYR E 156  CYS E 158 -1  O  TYR E 157   N  ILE E 147           
SHEET    3   K 4 SER E 163  TYR E 165 -1  O  TYR E 165   N  TYR E 156           
SHEET    4   K 4 ILE E 171  LYS E 173 -1  O  LYS E 173   N  HIS E 164           
SHEET    1   L 6 ASN N  15  THR N  18  0                                        
SHEET    2   L 6 ARG N  24  GLU N  29 -1  O  VAL N  25   N  THR N  17           
SHEET    3   L 6 VAL N 196  GLY N 201  1  O  GLY N 201   N  GLU N  28           
SHEET    4   L 6 THR N  34  ILE N  41 -1  N  TRP N  40   O  VAL N 196           
SHEET    5   L 6 THR N  95  LEU N 102 -1  O  ILE N  99   N  VAL N  37           
SHEET    6   L 6 HIS N  85  THR N  90 -1  N  HIS N  85   O  LYS N 100           
SHEET    1   M 8 ARG N 279  ASP N 281  0                                        
SHEET    2   M 8 SER N 306  SER N 313 -1  O  PHE N 307   N  TYR N 280           
SHEET    3   M 8 GLY N 318  ALA N 326 -1  O  LEU N 319   N  THR N 312           
SHEET    4   M 8 ALA N 251  GLU N 258 -1  N  ALA N 251   O  ALA N 326           
SHEET    5   M 8 ALA N 421  GLY N 426 -1  O  ALA N 421   N  ALA N 256           
SHEET    6   M 8 SER N 239  ASP N 245  1  N  ALA N 243   O  ALA N 424           
SHEET    7   M 8 ARG T  11  LEU T  18 -1  O  THR T  15   N  ARG N 242           
SHEET    8   M 8 LYS Q 234  TYR Q 237 -1  N  LYS Q 234   O  TYR T  16           
SHEET    1   N 2 ILE O  26  LYS O  28  0                                        
SHEET    2   N 2 ILE O  34  ALA O  36 -1  O  ILE O  35   N  THR O  27           
SHEET    1   O 3 CYS O 111  LEU O 112  0                                        
SHEET    2   O 3 ALA O  44  ILE O  51 -1  N  SER O  45   O  CYS O 111           
SHEET    3   O 3 MET O 204  ILE O 209 -1  O  ALA O 205   N  PHE O  50           
SHEET    1   P 5 CYS O 111  LEU O 112  0                                        
SHEET    2   P 5 ALA O  44  ILE O  51 -1  N  SER O  45   O  CYS O 111           
SHEET    3   P 5 LYS O 104  VAL O 109 -1  O  TYR O 107   N  VAL O  49           
SHEET    4   P 5 LEU O  96  THR O 101 -1  N  TYR O  99   O  THR O 106           
SHEET    5   P 5 ALA V  66  SER V  69 -1  O  ILE V  68   N  VAL O  98           
SHEET    1   Q 5 GLU O 243  GLN O 247  0                                        
SHEET    2   Q 5 LYS O 422  GLY O 428  1  O  ALA O 426   N  GLU O 246           
SHEET    3   Q 5 LEU O 252  GLU O 260 -1  N  VAL O 258   O  SER O 423           
SHEET    4   Q 5 SER O 319  GLN O 329 -1  O  THR O 326   N  ALA O 255           
SHEET    5   Q 5 PHE O 307  TYR O 316 -1  N  PHE O 312   O  GLY O 323           
SHEET    1   R 2 PRO P  23  PRO P  25  0                                        
SHEET    2   R 2 LYS P 218  PRO P 220 -1  O  ILE P 219   N  ALA P  24           
SHEET    1   S 2 HIS Q 148  TYR Q 149  0                                        
SHEET    2   S 2 ALA Q 157  ILE Q 158 -1  O  ILE Q 158   N  HIS Q 148           
SHEET    1   T 3 ILE R  74  ILE R  76  0                                        
SHEET    2   T 3 VAL R 193  VAL R 195 -1  O  VAL R 193   N  ILE R  76           
SHEET    3   T 3 TYR R 185  PHE R 187 -1  N  GLN R 186   O  VAL R 194           
SHEET    1   U 3 LYS R  85  PHE R  89  0                                        
SHEET    2   U 3 LEU R  96  HIS R 100 -1  O  LEU R  96   N  PHE R  89           
SHEET    3   U 3 TRP R 132  LEU R 135 -1  O  LEU R 135   N  PHE R  97           
SHEET    1   V 4 ILE R 147  ALA R 148  0                                        
SHEET    2   V 4 TYR R 156  CYS R 158 -1  O  TYR R 157   N  ILE R 147           
SHEET    3   V 4 SER R 163  TYR R 165 -1  O  TYR R 165   N  TYR R 156           
SHEET    4   V 4 ILE R 171  LYS R 173 -1  O  LYS R 173   N  HIS R 164           
SSBOND   1 CYS E  144    CYS E  160                          1555   1555  2.03  
SSBOND   2 CYS H   24    CYS H   68                          1555   1555  2.06  
SSBOND   3 CYS H   40    CYS H   54                          1555   1555  2.06  
SSBOND   4 CYS R  144    CYS R  160                          1555   1555  2.03  
SSBOND   5 CYS U   24    CYS U   68                          1555   1555  2.04  
SSBOND   6 CYS U   40    CYS U   54                          1555   1555  2.04  
LINK         NE2 HIS C  84                FE   HEM C 501     1555   1555  2.00  
LINK         NE2 HIS C  98                FE   HEM C 502     1555   1555  2.01  
LINK         NE2 HIS C 183                FE   HEM C 501     1555   1555  2.01  
LINK         NE2 HIS C 197                FE   HEM C 502     1555   1555  2.00  
LINK         NE2 HIS D  41                FE   HEC D 501     1555   1555  2.00  
LINK         SD  MET D 160                FE   HEC D 501     1555   1555  2.19  
LINK         SG  CYS E 139                FE1  FES E 501     1555   1555  2.29  
LINK         ND1 HIS E 141                FE2  FES E 501     1555   1555  2.11  
LINK         SG  CYS E 158                FE1  FES E 501     1555   1555  2.25  
LINK         ND1 HIS E 161                FE2  FES E 501     1555   1555  2.07  
LINK         NE2 HIS P  84                FE   HEM P 501     1555   1555  2.00  
LINK         NE2 HIS P  98                FE   HEM P 502     1555   1555  2.01  
LINK         NE2 HIS P 183                FE   HEM P 501     1555   1555  2.00  
LINK         NE2 HIS P 197                FE   HEM P 502     1555   1555  2.00  
LINK         NE2 HIS Q  41                FE   HEC Q 501     1555   1555  2.00  
LINK         SD  MET Q 160                FE   HEC Q 501     1555   1555  2.13  
LINK         SG  CYS R 139                FE1  FES R 501     1555   1555  2.26  
LINK         ND1 HIS R 141                FE2  FES R 501     1555   1555  2.10  
LINK         SG  CYS R 158                FE1  FES R 501     1555   1555  2.23  
LINK         ND1 HIS R 161                FE2  FES R 501     1555   1555  2.09  
CISPEP   1 HIS C  222    PRO C  223          0         0.66                     
CISPEP   2 HIS C  346    PRO C  347          0        -0.05                     
CISPEP   3 GLY D   73    PRO D   74          0         0.11                     
CISPEP   4 ALA P    2    PRO P    3          0        -0.19                     
CISPEP   5 HIS P  222    PRO P  223          0         0.13                     
CISPEP   6 HIS P  346    PRO P  347          0         0.03                     
CISPEP   7 GLY Q   73    PRO Q   74          0         0.18                     
SITE     1 AC1  3 TYR A 442  HIS C 222  PEE E2005                               
SITE     1 AC2 15 GLN C  45  GLY C  49  LEU C  50  LEU C  52                    
SITE     2 AC2 15 ARG C  81  HIS C  84  LEU C 124  THR C 127                    
SITE     3 AC2 15 ALA C 128  GLY C 131  TYR C 132  LEU C 134                    
SITE     4 AC2 15 PRO C 135  HIS C 183  PRO C 187                               
SITE     1 AC3 18 TRP C  32  GLY C  35  LEU C  38  ALA C  39                    
SITE     2 AC3 18 HIS C  98  ILE C  99  ARG C 101  SER C 107                    
SITE     3 AC3 18 GLY C 117  LEU C 120  THR C 194  HIS C 197                    
SITE     4 AC3 18 LEU C 198  LEU C 201  ASN C 207  HOH C 381                    
SITE     5 AC3 18 HOH C 384  3H1 C2002                                          
SITE     1 AC4 11 ALA C 126  GLY C 143  VAL C 146  ILE C 147                    
SITE     2 AC4 11 PRO C 271  PHE C 275  TYR C 279  LEU C 282                    
SITE     3 AC4 11 UNL C2010  CYS R 160  HIS R 161                               
SITE     1 AC5 13 LEU C  19  LEU C  22  SER C  36  ALA C  39                    
SITE     2 AC5 13 LEU C 198  LEU C 201  HIS C 202  SER C 206                    
SITE     3 AC5 13 ASP C 229  ILE C 230  HOH C 383  HOH C 385                    
SITE     4 AC5 13 HEM C 502                                                     
SITE     1 AC6 11 ALA C  30  GLY C 232  MET C 236  TYR D 220                    
SITE     2 AC6 11 LYS D 223  ARG D 224  HIS F  72  ARG F  73                    
SITE     3 AC6 11 ALA G  33  ARG G  40  CDL G2004                               
SITE     1 AC7 10 TRP C  31  PHE C  96  TYR C 104  TYR C 105                    
SITE     2 AC7 10 PHE C 277  THR C 317  TRP C 327  TYR F  29                    
SITE     3 AC7 10 GLN G  44  CDL G2004                                          
SITE     1 AC8  2 TYR C 132  3H1 C2001                                          
SITE     1 AC9  2 ASN C 149  UNL R2103                                          
SITE     1 BC1  1 THR C 199                                                     
SITE     1 BC2  5 PHE C  64  ARG C  81  ASN C 256  PHE C 257                    
SITE     2 BC2  5 TYR D 115                                                     
SITE     1 BC3 14 VAL D  36  CYS D  37  CYS D  40  HIS D  41                    
SITE     2 BC3 14 ASN D 105  ALA D 108  PRO D 110  ARG D 120                    
SITE     3 BC3 14 TYR D 126  LEU D 131  PHE D 153  GLY D 159                    
SITE     4 BC3 14 MET D 160  PRO D 163                                          
SITE     1 BC4  6 TYR C  76  GLN D 200  ARG D 203  LYS D 207                    
SITE     2 BC4  6 ASN E  53  GLN E  57                                          
SITE     1 BC5  6 CYS E 139  HIS E 141  LEU E 142  CYS E 158                    
SITE     2 BC5  6 HIS E 161  SER E 163                                          
SITE     1 BC6  5 PEE A2008  PHE C 227  LYS D 226  TYR E  37                    
SITE     2 BC6  5 THR E  40                                                     
SITE     1 BC7  1 TYR E 178                                                     
SITE     1 BC8  9 SER C  29  ALA C  30  TRP C  31  TYR C 105                    
SITE     2 BC8  9 CDL C2003  PEE C2007  HIS F  72  ARG G  40                    
SITE     3 BC8  9 GLN G  44                                                     
SITE     1 BC9 15 GLN P  45  GLY P  49  LEU P  50  LEU P  52                    
SITE     2 BC9 15 ARG P  81  HIS P  84  LEU P 124  THR P 127                    
SITE     3 BC9 15 ALA P 128  GLY P 131  TYR P 132  LEU P 134                    
SITE     4 BC9 15 PRO P 135  HIS P 183  PRO P 187                               
SITE     1 CC1 16 TRP P  32  GLY P  35  LEU P  38  ALA P  39                    
SITE     2 CC1 16 HIS P  98  ARG P 101  SER P 107  GLY P 117                    
SITE     3 CC1 16 LEU P 120  THR P 194  HIS P 197  LEU P 201                    
SITE     4 CC1 16 ASN P 207  HOH P 381  HOH P 384  3H1 P3002                    
SITE     1 CC2  1 THR P 199                                                     
SITE     1 CC3  1 LEU P 250                                                     
SITE     1 CC4 12 CYS E 160  HIS E 161  MET P 125  ALA P 126                    
SITE     2 CC4 12 PHE P 129  GLY P 143  VAL P 146  PRO P 271                    
SITE     3 CC4 12 GLU P 272  PHE P 275  TYR P 279  LEU P 282                    
SITE     1 CC5 15 LEU P  19  LEU P  22  SER P  36  ALA P  39                    
SITE     2 CC5 15 LEU P 198  LEU P 201  HIS P 202  SER P 206                    
SITE     3 CC5 15 PHE P 221  TYR P 225  ASP P 229  ILE P 230                    
SITE     4 CC5 15 HOH P 382  HEM P 502  HOH P 959                               
SITE     1 CC6 10 ALA P  30  GLY P 232  MET P 236  TYR Q 220                    
SITE     2 CC6 10 LYS Q 223  ARG Q 224  HIS S  72  ARG S  73                    
SITE     3 CC6 10 ARG T  40  CDL T3004                                          
SITE     1 CC7 12 TRP P  31  TYR P 104  TYR P 105  PHE P 277                    
SITE     2 CC7 12 THR P 317  TRP P 327  LEU P 333  TYR S  29                    
SITE     3 CC7 12 GLN T  44  VAL T  48  PHE T  52  CDL T3004                    
SITE     1 CC8  2 TYR N 442  HIS P 222                                          
SITE     1 CC9  2 ALA P  85  TYR P 274                                          
SITE     1 DC1  1 ASN P 149                                                     
SITE     1 DC2  2 ASN P 149  VAL P 162                                          
SITE     1 DC3  6 PHE P  64  ARG P  81  PRO P 135  ASN P 256                    
SITE     2 DC3  6 PHE P 257  TYR Q 115                                          
SITE     1 DC4 12 VAL Q  36  CYS Q  37  CYS Q  40  HIS Q  41                    
SITE     2 DC4 12 ASN Q 105  ALA Q 108  ARG Q 120  TYR Q 126                    
SITE     3 DC4 12 PHE Q 153  GLY Q 159  MET Q 160  PRO Q 163                    
SITE     1 DC5  6 CYS R 139  HIS R 141  LEU R 142  CYS R 158                    
SITE     2 DC5  6 HIS R 161  SER R 163                                          
SITE     1 DC6  1 UNL C2104                                                     
SITE     1 DC7  8 PHE P 227  LEU P 233  LYS Q 226  TYR R  37                    
SITE     2 DC7  8 THR R  40  PHE W  14  ARG W  15  THR W  17                    
SITE     1 DC8  6 TYR P  76  GLN Q 200  ARG Q 203  LYS Q 207                    
SITE     2 DC8  6 ASN R  53  GLN R  57                                          
SITE     1 DC9  7 ALA P  30  TRP P  31  TYR P 105  CDL P3003                    
SITE     2 DC9  7 PEE P3007  ARG T  40  GLN T  44                               
CRYST1  174.139  182.364  241.626  90.00  90.00  90.00 P 21 21 21    8          
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      0.005743  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005484  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004139        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system