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Database: PDB
Entry: 5E7C
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Original site: 5E7C 
HEADER    PHOTOSYNTHESIS                          12-OCT-15   5E7C              
TITLE     MACROMOLECULAR DIFFRACTIVE IMAGING USING IMPERFECT CRYSTALS - BRAGG   
TITLE    2 DATA                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM II PROTEIN D1 1;                               
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 SYNONYM: PSII D1 PROTEIN 1,PHOTOSYSTEM II Q(B) PROTEIN 1;            
COMPND   5 EC: 1.10.3.9;                                                        
COMPND   6 OTHER_DETAILS: PHOTOSYSTEM Q(B) PROTEIN 1;                           
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PHOTOSYSTEM II CP47 REACTION CENTER PROTEIN;               
COMPND   9 CHAIN: B, b;                                                         
COMPND  10 SYNONYM: PSII 47 KDA PROTEIN,PROTEIN CP-47;                          
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;               
COMPND  13 CHAIN: C, c;                                                         
COMPND  14 SYNONYM: PSII 43 KDA PROTEIN,PROTEIN CP-43;                          
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  17 CHAIN: D, d;                                                         
COMPND  18 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM II Q(A) PROTEIN;                
COMPND  19 EC: 1.10.3.9;                                                        
COMPND  20 MOL_ID: 5;                                                           
COMPND  21 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;                             
COMPND  22 CHAIN: E, e;                                                         
COMPND  23 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  24 MOL_ID: 6;                                                           
COMPND  25 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  26 CHAIN: F, f;                                                         
COMPND  27 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  28 MOL_ID: 7;                                                           
COMPND  29 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;                  
COMPND  30 CHAIN: H, h;                                                         
COMPND  31 SYNONYM: PSII-H;                                                     
COMPND  32 MOL_ID: 8;                                                           
COMPND  33 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  34 CHAIN: I, i;                                                         
COMPND  35 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;                                
COMPND  36 MOL_ID: 9;                                                           
COMPND  37 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;                  
COMPND  38 CHAIN: J, j;                                                         
COMPND  39 SYNONYM: PSII-J;                                                     
COMPND  40 MOL_ID: 10;                                                          
COMPND  41 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  42 CHAIN: K, k;                                                         
COMPND  43 SYNONYM: PSII-K;                                                     
COMPND  44 MOL_ID: 11;                                                          
COMPND  45 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  46 CHAIN: L, l;                                                         
COMPND  47 SYNONYM: PSII-L;                                                     
COMPND  48 MOL_ID: 12;                                                          
COMPND  49 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;                  
COMPND  50 CHAIN: M, m;                                                         
COMPND  51 SYNONYM: PSII-M;                                                     
COMPND  52 MOL_ID: 13;                                                          
COMPND  53 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  54 CHAIN: O, o;                                                         
COMPND  55 SYNONYM: MSP;                                                        
COMPND  56 MOL_ID: 14;                                                          
COMPND  57 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  58 CHAIN: T, t;                                                         
COMPND  59 SYNONYM: PSII-TC;                                                    
COMPND  60 MOL_ID: 15;                                                          
COMPND  61 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  62 CHAIN: U, u;                                                         
COMPND  63 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;              
COMPND  64 MOL_ID: 16;                                                          
COMPND  65 MOLECULE: CYTOCHROME C-550;                                          
COMPND  66 CHAIN: V, v;                                                         
COMPND  67 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND  68 MOL_ID: 17;                                                          
COMPND  69 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  70 CHAIN: Y, y;                                                         
COMPND  71 MOL_ID: 18;                                                          
COMPND  72 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  73 CHAIN: X, x;                                                         
COMPND  74 MOL_ID: 19;                                                          
COMPND  75 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  76 CHAIN: Z, z;                                                         
COMPND  77 SYNONYM: PSII-Z                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 STRAIN: BP-1;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE   7 ORGANISM_TAXID: 197221;                                              
SOURCE   8 STRAIN: BP-1;                                                        
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  11 ORGANISM_TAXID: 197221;                                              
SOURCE  12 STRAIN: BP-1;                                                        
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  15 ORGANISM_TAXID: 197221;                                              
SOURCE  16 STRAIN: BP-1;                                                        
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  19 ORGANISM_TAXID: 197221;                                              
SOURCE  20 STRAIN: BP-1;                                                        
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  23 ORGANISM_TAXID: 197221;                                              
SOURCE  24 STRAIN: BP-1;                                                        
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  27 ORGANISM_TAXID: 197221;                                              
SOURCE  28 STRAIN: BP-1;                                                        
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  31 ORGANISM_TAXID: 197221;                                              
SOURCE  32 STRAIN: BP-1;                                                        
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  35 ORGANISM_TAXID: 197221;                                              
SOURCE  36 STRAIN: BP-1;                                                        
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  39 ORGANISM_TAXID: 197221;                                              
SOURCE  40 STRAIN: BP-1;                                                        
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  43 ORGANISM_TAXID: 197221;                                              
SOURCE  44 STRAIN: BP-1;                                                        
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  47 ORGANISM_TAXID: 197221;                                              
SOURCE  48 STRAIN: BP-1;                                                        
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  51 ORGANISM_TAXID: 197221;                                              
SOURCE  52 STRAIN: BP-1;                                                        
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  55 ORGANISM_TAXID: 197221;                                              
SOURCE  56 STRAIN: BP-1;                                                        
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  59 ORGANISM_TAXID: 197221;                                              
SOURCE  60 STRAIN: BP-1;                                                        
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  63 ORGANISM_TAXID: 197221;                                              
SOURCE  64 STRAIN: BP-1;                                                        
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  67 ORGANISM_TAXID: 197221;                                              
SOURCE  68 STRAIN: BP-1;                                                        
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  71 ORGANISM_TAXID: 197221;                                              
SOURCE  72 STRAIN: BP-1;                                                        
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  75 ORGANISM_TAXID: 197221;                                              
SOURCE  76 STRAIN: BP-1                                                         
KEYWDS    PHOTOSYSTEM II, XFEL, SFX, PHOTOSYNTHESIS                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.AYYER,O.YEFANOV,D.OBERTHUER,S.ROY-CHOWDHURY,L.GALLI,V.MARIANI,      
AUTHOR   2 S.BASU,J.COE,C.E.CONRAD,R.FROMME,A.SCHAFFNER,K.DOERNER,D.JAMES,      
AUTHOR   3 C.KUPITZ,M.METZ,G.NELSON,P.L.XAVIER,K.R.BEYERLEIN,M.SCHMIDT,         
AUTHOR   4 I.SARROU,J.C.H.SPENCE,U.WEIERSTALL,T.A.WHITE,J.-H.YANG,Y.ZHAO,       
AUTHOR   5 M.LIANG,A.AQUILA,M.S.HUNTER,J.S.ROBINSON,J.E.KOGLIN,S.BOUTET,        
AUTHOR   6 P.FROMME,A.BARTY,H.N.CHAPMAN                                         
REVDAT   5   14-NOV-18 5E7C    1       REMARK                                   
REVDAT   4   24-JAN-18 5E7C    1       REMARK                                   
REVDAT   3   02-MAR-16 5E7C    1       JRNL                                     
REVDAT   2   17-FEB-16 5E7C    1       JRNL                                     
REVDAT   1   10-FEB-16 5E7C    0                                                
JRNL        AUTH   K.AYYER,O.M.YEFANOV,D.OBERTHUR,S.ROY-CHOWDHURY,L.GALLI,      
JRNL        AUTH 2 V.MARIANI,S.BASU,J.COE,C.E.CONRAD,R.FROMME,A.SCHAFFER,       
JRNL        AUTH 3 K.DORNER,D.JAMES,C.KUPITZ,M.METZ,G.NELSON,P.L.XAVIER,        
JRNL        AUTH 4 K.R.BEYERLEIN,M.SCHMIDT,I.SARROU,J.C.SPENCE,U.WEIERSTALL,    
JRNL        AUTH 5 T.A.WHITE,J.H.YANG,Y.ZHAO,M.LIANG,A.AQUILA,M.S.HUNTER,       
JRNL        AUTH 6 J.S.ROBINSON,J.E.KOGLIN,S.BOUTET,P.FROMME,A.BARTY,           
JRNL        AUTH 7 H.N.CHAPMAN                                                  
JRNL        TITL   MACROMOLECULAR DIFFRACTIVE IMAGING USING IMPERFECT CRYSTALS. 
JRNL        REF    NATURE                        V. 530   202 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26863980                                                     
JRNL        DOI    10.1038/NATURE16949                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 55609                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.890                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2718                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.9252 - 11.7725    1.00     2950   158  0.2845 0.3180        
REMARK   3     2 11.7725 -  9.4406    1.00     2847   140  0.1927 0.2368        
REMARK   3     3  9.4406 -  8.2761    1.00     2807   165  0.1801 0.1935        
REMARK   3     4  8.2761 -  7.5326    1.00     2819   148  0.1955 0.2146        
REMARK   3     5  7.5326 -  7.0001    1.00     2776   158  0.2230 0.2546        
REMARK   3     6  7.0001 -  6.5921    1.00     2766   168  0.2305 0.2611        
REMARK   3     7  6.5921 -  6.2651    1.00     2775   151  0.2374 0.2999        
REMARK   3     8  6.2651 -  5.9946    1.00     2785   141  0.2615 0.3106        
REMARK   3     9  5.9946 -  5.7656    1.00     2782   136  0.2576 0.2859        
REMARK   3    10  5.7656 -  5.5679    1.00     2730   143  0.2644 0.2881        
REMARK   3    11  5.5679 -  5.3948    1.00     2787   137  0.2740 0.3227        
REMARK   3    12  5.3948 -  5.2415    1.00     2758   152  0.2822 0.2971        
REMARK   3    13  5.2415 -  5.1042    1.00     2744   143  0.2862 0.3518        
REMARK   3    14  5.1042 -  4.9802    1.00     2774   129  0.2967 0.3517        
REMARK   3    15  4.9802 -  4.8675    1.00     2747   128  0.3045 0.3128        
REMARK   3    16  4.8675 -  4.7643    1.00     2754   130  0.3092 0.2868        
REMARK   3    17  4.7643 -  4.6694    1.00     2773   132  0.3242 0.3209        
REMARK   3    18  4.6694 -  4.5816    1.00     2748   118  0.3281 0.3472        
REMARK   3    19  4.5816 -  4.5000    1.00     2769   141  0.3483 0.3644        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.570            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.620           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011          51858                                  
REMARK   3   ANGLE     :  1.482          71398                                  
REMARK   3   CHIRALITY :  0.650           7190                                  
REMARK   3   PLANARITY :  0.009           7760                                  
REMARK   3   DIHEDRAL  : 22.881          21404                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5E7C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214435.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.15                             
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER                
REMARK 200  BEAMLINE                       : CXI                                
REMARK 200  X-RAY GENERATOR MODEL          : SLAC LCLS BEAMLINE CXI             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.308                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : CS-PAD CXI-2                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL                           
REMARK 200  DATA SCALING SOFTWARE          : CRYSTFEL                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55609                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 1.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.0100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.490                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: MODIFIED VERSION OF 3ARC                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM PIPES PH 7.0, 5 MM CACL2, 10 MM   
REMARK 280  TOCOPHEROL, AND 10-17% PEG 2000, LIQUID DIFFUSION, TEMPERATURE      
REMARK 280  283K                                                                
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       66.62500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      153.54500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      113.13000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      153.54500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       66.62500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      113.13000            
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: 38-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 38-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,         
REMARK 350                    AND CHAINS: L, M, O, T, U, V, Y, X, Z,            
REMARK 350                    AND CHAINS: a, b, c, d, e, f, h, i, j, k,         
REMARK 350                    AND CHAINS: l, m, o, t, u, v, y, x, z             
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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     SER b   36   CA   CB   OG                                        
REMARK 480     SER b  239   CA   CB   OG                                        
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   OG1  THR c    24     OE1  GLU c   138              2.03            
REMARK 500   OE2  GLU C   464     OG   SER D   245              2.11            
REMARK 500   OH   TYR A   235     OE1  GLU L    11              2.13            
REMARK 500   O    PHE b   432     NZ   LYS o   178              2.15            
REMARK 500   OH   TYR d   141     O4   LHG b   624              2.15            
REMARK 500   O    TYR e    56     N    ALA v     1              2.15            
REMARK 500   NE2  GLN C    28     O7   SQD A   611              2.16            
REMARK 500   OE2  GLU c   464     OG   SER d   245              2.16            
REMARK 500   OH   TYR D   141     O4   LHG B   622              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG z  35   CB  -  CG  -  CD  ANGL. DEV. =  16.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  30      -82.73    -93.46                                   
REMARK 500    LEU A 159      -54.32   -124.70                                   
REMARK 500    ILE A 259      -93.67   -101.34                                   
REMARK 500    TYR B 117       56.60    -92.67                                   
REMARK 500    PHE B 162       83.35   -150.16                                   
REMARK 500    ASP B 313       46.00    -92.93                                   
REMARK 500    PHE B 383      -78.20    -86.31                                   
REMARK 500    ASP C 107      113.87   -160.89                                   
REMARK 500    GLU C 221      -65.67   -124.82                                   
REMARK 500    TRP C 223     -138.09     47.19                                   
REMARK 500    SER C 416      -46.01    174.64                                   
REMARK 500    SER C 416      -48.38    175.61                                   
REMARK 500    ARG D  12       42.97   -156.37                                   
REMARK 500    VAL D  30      -70.25   -107.18                                   
REMARK 500    SER D  65       14.61   -147.67                                   
REMARK 500    PRO D 140       44.37    -91.56                                   
REMARK 500    ALA D 234       32.55    -77.74                                   
REMARK 500    PRO D 309        1.98    -66.51                                   
REMARK 500    ALA D 351      -52.17     71.61                                   
REMARK 500    LYS H  63       32.45    -83.67                                   
REMARK 500    LYS H  63       31.80    -83.15                                   
REMARK 500    LEU H  65      -87.75   -149.97                                   
REMARK 500    LYS I  33     -119.68   -110.38                                   
REMARK 500    SER J  39       -4.01     72.98                                   
REMARK 500    ASN O  58       -3.42    149.83                                   
REMARK 500    ARG O  73     -163.03     69.62                                   
REMARK 500    ASN U  29      -37.45   -139.10                                   
REMARK 500    TYR U 103     -144.19   -113.67                                   
REMARK 500    ASN V  49       81.74   -159.19                                   
REMARK 500    ASP V  67       36.37    -88.99                                   
REMARK 500    PHE V 101       79.83   -116.81                                   
REMARK 500    ASP X  35       69.28   -115.99                                   
REMARK 500    VAL a  30      -82.07    -93.24                                   
REMARK 500    LEU a 159      -51.84   -128.51                                   
REMARK 500    ILE a 259      -93.94   -100.97                                   
REMARK 500    TYR b 117       54.38    -96.83                                   
REMARK 500    PHE b 162       81.97   -154.65                                   
REMARK 500    ASP b 313       48.06    -92.52                                   
REMARK 500    PHE b 383      -79.08    -85.38                                   
REMARK 500    GLU b 485       48.54   -103.22                                   
REMARK 500    ASN c  25        6.27     56.00                                   
REMARK 500    ASP c 107      114.75   -164.66                                   
REMARK 500    GLU c 221      -69.18   -123.40                                   
REMARK 500    TRP c 223     -140.86     50.72                                   
REMARK 500    SER c 416      -48.20    170.48                                   
REMARK 500    SER c 416      -53.16    172.59                                   
REMARK 500    SER c 463       54.26   -142.35                                   
REMARK 500    ARG d  12       40.75   -157.53                                   
REMARK 500    VAL d  30      -67.22   -105.37                                   
REMARK 500    SER d  65       11.71   -141.71                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      69 RAMACHANDRAN OUTLIERS.                        
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     LMG A  612                                                       
REMARK 610     LMG B  621                                                       
REMARK 610     DGD C  516                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     DGD C  518                                                       
REMARK 610     LMG C  519                                                       
REMARK 610     LMG C  520                                                       
REMARK 610     DGD D  406                                                       
REMARK 610     LHG E  101                                                       
REMARK 610     DGD H  102                                                       
REMARK 610     LMG J  101                                                       
REMARK 610     SQD X  101                                                       
REMARK 610     LMG Z  101                                                       
REMARK 610     LMG a  611                                                       
REMARK 610     LMG b  623                                                       
REMARK 610     DGD c  517                                                       
REMARK 610     DGD c  518                                                       
REMARK 610     DGD c  519                                                       
REMARK 610     LMG c  520                                                       
REMARK 610     LMG c  521                                                       
REMARK 610     DGD d  405                                                       
REMARK 610     LHG e  101                                                       
REMARK 610     DGD h  102                                                       
REMARK 610     LMG j  101                                                       
REMARK 610     SQD x  101                                                       
REMARK 610     LMG z  101                                                       
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                             OEX A 601  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD1                                                    
REMARK 620 2 OEX A 601   O1  155.0                                              
REMARK 620 3 OEX A 601   O2   90.8  75.2                                        
REMARK 620 4 OEX A 601   O5  120.6  76.8  76.7                                  
REMARK 620 5 ASP A 170   OD2  42.0 153.1  87.6  79.2                            
REMARK 620 6 ALA A 344   O    80.2  77.5  82.7 150.4 121.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD2                                                    
REMARK 620 2 OEX A 601   O5   95.0                                              
REMARK 620 3 OEX A 601   O4   87.7  92.5                                        
REMARK 620 4 GLU A 333   OE2 166.0  77.3 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 OEX A 601   O1   92.6                                              
REMARK 620 3 OEX A 601   O5   81.8  82.4                                        
REMARK 620 4 OEX A 601   O3  162.1  92.0  81.6                                  
REMARK 620 5 HIS A 332   NE2  92.3 173.3 102.7  84.7                            
REMARK 620 6 ASP A 342   OD2 106.7  87.8 167.4  90.8  86.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 613  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2  95.1                                              
REMARK 620 3 HIS D 214   NE2  96.0  83.4                                        
REMARK 620 4 HIS D 268   NE2  87.4 168.5  85.2                                  
REMARK 620 5 BCT A 604   O1  168.5  80.1  93.8  99.4                            
REMARK 620 6 BCT A 604   O2  115.2  92.8 148.8  96.3  55.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 OEX A 601   O2  172.6                                              
REMARK 620 3 OEX A 601   O3   80.7  93.2                                        
REMARK 620 4 OEX A 601   O4  102.8  83.2 175.9                                  
REMARK 620 5 OEX A 601   O5   82.7  92.4  81.5  96.6                            
REMARK 620 6 GLU C 354   OE2  83.9  99.3  81.8 100.8 160.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 OEX A 601   O1   88.3                                              
REMARK 620 3 OEX A 601   O2  173.4  89.0                                        
REMARK 620 4 OEX A 601   O3   98.6  78.9  86.8                                  
REMARK 620 5 ALA A 344   OXT  80.7  89.8  93.2 168.7                            
REMARK 620 6 GLU C 354   OE1  89.5 157.8  95.2  79.6 111.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  39   OD1                                                    
REMARK 620 2 CLA C 511   NA  107.9                                              
REMARK 620 3 CLA C 511   NB   87.5  93.2                                        
REMARK 620 4 CLA C 511   NC   79.6 172.2  89.3                                  
REMARK 620 5 CLA C 511   ND   85.5  90.9 172.7  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 102  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM E 102   NA  101.5                                              
REMARK 620 3 HEM E 102   NB  114.1  90.2                                        
REMARK 620 4 HEM E 102   NC   82.7 174.0  92.0                                  
REMARK 620 5 HEM E 102   ND   61.8  90.4 175.8  87.9                            
REMARK 620 6 HIS F  24   NE2 140.6  82.0 105.1  92.1  79.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY J  31   O                                                      
REMARK 620 2 ALA J  34   O    68.1                                              
REMARK 620 3 LEU J  36   O    93.2 110.8                                        
REMARK 620 4 LMG J 101   O4   60.5 127.2  84.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA O 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR O 138   O                                                      
REMARK 620 2 ASN O 200   OD1 113.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM V 202  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  41   NE2                                                    
REMARK 620 2 HEM V 202   NA  100.3                                              
REMARK 620 3 HEM V 202   NB   88.2  93.0                                        
REMARK 620 4 HEM V 202   NC   72.8 173.1  87.6                                  
REMARK 620 5 HEM V 202   ND   79.9  89.5 168.1  88.5                            
REMARK 620 6 HIS V  92   NE2 156.6 102.1  97.3  84.7  93.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD1                                                    
REMARK 620 2 OEX a 601   O1  154.0                                              
REMARK 620 3 OEX a 601   O2   91.7  75.2                                        
REMARK 620 4 OEX a 601   O5  122.6  76.8  76.7                                  
REMARK 620 5 ASP a 170   OD2  42.5 153.6  86.7  80.4                            
REMARK 620 6 ALA a 344   O    78.2  78.7  86.8 153.3 120.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD2                                                    
REMARK 620 2 OEX a 601   O5   93.7                                              
REMARK 620 3 OEX a 601   O4   85.6  92.5                                        
REMARK 620 4 GLU a 333   OE2 163.3  78.7 109.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 OEX a 601   O1   98.1                                              
REMARK 620 3 OEX a 601   O5   89.6  82.4                                        
REMARK 620 4 OEX a 601   O3  165.7  92.0  81.6                                  
REMARK 620 5 HIS a 332   NE2  78.5 173.5 103.0  92.3                            
REMARK 620 6 ASP a 342   OD2  96.8  91.1 171.4  93.1  83.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a 615  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS a 272   NE2  86.6                                              
REMARK 620 3 HIS d 214   NE2 105.3  87.3                                        
REMARK 620 4 HIS d 268   NE2  95.0 176.5  95.3                                  
REMARK 620 5 BCT a 603   O1  161.8  94.0  92.8  83.5                            
REMARK 620 6 BCT a 603   O2  107.4  95.3 147.2  81.2  54.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 OEX a 601   O2  171.9                                              
REMARK 620 3 OEX a 601   O3   85.6  93.2                                        
REMARK 620 4 OEX a 601   O4   97.7  83.2 175.9                                  
REMARK 620 5 OEX a 601   O5   79.6  92.4  81.5  96.6                            
REMARK 620 6 GLU c 354   OE2  85.5 101.9  76.4 106.2 154.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 342   OD1                                                    
REMARK 620 2 OEX a 601   O1   85.9                                              
REMARK 620 3 OEX a 601   O2  174.1  89.0                                        
REMARK 620 4 OEX a 601   O3   95.1  78.9  86.8                                  
REMARK 620 5 ALA a 344   OXT  85.4  85.0  91.3 163.8                            
REMARK 620 6 GLU c 354   OE1  85.5 152.3 100.4  75.7 120.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 512  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c  39   OD1                                                    
REMARK 620 2 CLA c 512   NA  103.2                                              
REMARK 620 3 CLA c 512   NB   89.0  92.7                                        
REMARK 620 4 CLA c 512   NC   84.7 171.8  89.6                                  
REMARK 620 5 CLA c 512   ND   83.9  91.4 172.4  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM e 102  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e  23   NE2                                                    
REMARK 620 2 HEM e 102   NA  109.6                                              
REMARK 620 3 HEM e 102   NB  112.3  88.0                                        
REMARK 620 4 HEM e 102   NC   79.8 170.1  91.0                                  
REMARK 620 5 HEM e 102   ND   67.3  91.9 179.5  89.2                            
REMARK 620 6 HIS f  24   NE2 159.6  73.4  87.8  96.7  92.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA f 102  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG f  45   O                                                      
REMARK 620 2 ARG f  45   OXT  42.7                                              
REMARK 620 3 GLU v  23   OE1 150.4 146.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG j 102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY j  31   O                                                      
REMARK 620 2 ALA j  34   O    85.8                                              
REMARK 620 3 LEU j  36   O   102.9 110.7                                        
REMARK 620 4 LMG j 101   O4   69.4 154.6  81.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA o 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR o 138   O                                                      
REMARK 620 2 ASN o 200   OD1 159.6                                              
REMARK 620 3 VAL o 201   O    84.4  75.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM v 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS v  41   NE2                                                    
REMARK 620 2 HEM v 201   NA   93.2                                              
REMARK 620 3 HEM v 201   NB   79.8  90.4                                        
REMARK 620 4 HEM v 201   NC   81.1 174.4  88.8                                  
REMARK 620 5 HEM v 201   ND   90.3  92.1 169.9  87.7                            
REMARK 620 6 HIS v  92   NE2 163.3 103.1  96.4  82.5  92.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR F 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG J 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG L 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD X 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG Z 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA b 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG b 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL c 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA f 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG j 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG j 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG l 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA o 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR t 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM v 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD x 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG z 101                 
DBREF  5E7C A   11   344  UNP    P0A444   PSBA1_THEEB     11    344             
DBREF  5E7C B    2   505  UNP    Q8DIQ1   PSBB_THEEB       2    505             
DBREF  5E7C C   23   473  UNP    Q8DIF8   PSBC_THEEB      11    461             
DBREF  5E7C D   11   352  UNP    Q8CM25   PSBD_THEEB      11    352             
DBREF  5E7C E    4    84  UNP    Q8DIP0   PSBE_THEEB       4     84             
DBREF  5E7C F   12    45  UNP    Q8DIN9   PSBF_THEEB      12     45             
DBREF  5E7C H    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  5E7C I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  5E7C J    3    40  UNP    P59087   PSBJ_THEEB       3     40             
DBREF  5E7C K   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  5E7C L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5E7C M    1    34  UNP    Q8DHA7   PSBM_THEEB       1     34             
DBREF  5E7C O    4   246  UNP    P0A431   PSBO_THEEB      30    272             
DBREF  5E7C T    1    30  UNP    Q8DIQ0   PSBT_THEEB       1     30             
DBREF  5E7C U    8   104  UNP    Q9F1L5   PSBU_THEEB      38    134             
DBREF  5E7C V    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  5E7C Y   18    46  UNP    Q8DJI1   YCF12_THEEB     18     46             
DBREF  5E7C X    2    40  UNP    Q9F1R6   PSBX_THEEB       2     40             
DBREF  5E7C Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  5E7C a   11   344  UNP    P0A444   PSBA1_THEEB     11    344             
DBREF  5E7C b    2   505  UNP    Q8DIQ1   PSBB_THEEB       2    505             
DBREF  5E7C c   23   473  UNP    Q8DIF8   PSBC_THEEB      11    461             
DBREF  5E7C d   11   352  UNP    Q8CM25   PSBD_THEEB      11    352             
DBREF  5E7C e    4    84  UNP    Q8DIP0   PSBE_THEEB       4     84             
DBREF  5E7C f   12    45  UNP    Q8DIN9   PSBF_THEEB      12     45             
DBREF  5E7C h    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  5E7C i    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  5E7C j    3    40  UNP    P59087   PSBJ_THEEB       3     40             
DBREF  5E7C k   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  5E7C l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5E7C m    1    34  UNP    Q8DHA7   PSBM_THEEB       1     34             
DBREF  5E7C o    4   246  UNP    P0A431   PSBO_THEEB      30    272             
DBREF  5E7C t    1    30  UNP    Q8DIQ0   PSBT_THEEB       1     30             
DBREF  5E7C u    8   104  UNP    Q9F1L5   PSBU_THEEB      38    134             
DBREF  5E7C v    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  5E7C y   18    46  UNP    Q8DJI1   YCF12_THEEB     18     46             
DBREF  5E7C x    2    40  UNP    Q9F1R6   PSBX_THEEB       2     40             
DBREF  5E7C z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
SEQADV 5E7C ALA A  286  UNP  P0A444    THR   286 CONFLICT                       
SEQADV 5E7C ALA a  286  UNP  P0A444    THR   286 CONFLICT                       
SEQRES   1 A  334  ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER          
SEQRES   2 A  334  THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE          
SEQRES   3 A  334  MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL          
SEQRES   4 A  334  ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY          
SEQRES   5 A  334  ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN          
SEQRES   6 A  334  ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA          
SEQRES   7 A  334  ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER          
SEQRES   8 A  334  LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU          
SEQRES   9 A  334  ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET          
SEQRES  10 A  334  GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG          
SEQRES  11 A  334  PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER          
SEQRES  12 A  334  ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY          
SEQRES  13 A  334  SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR          
SEQRES  14 A  334  PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE          
SEQRES  15 A  334  LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL          
SEQRES  16 A  334  PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU          
SEQRES  17 A  334  VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU          
SEQRES  18 A  334  SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU          
SEQRES  19 A  334  THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG          
SEQRES  20 A  334  LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER          
SEQRES  21 A  334  LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL          
SEQRES  22 A  334  TRP PHE ALA ALA LEU GLY ILE SER THR MET ALA PHE ASN          
SEQRES  23 A  334  LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA          
SEQRES  24 A  334  LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN          
SEQRES  25 A  334  ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN          
SEQRES  26 A  334  ALA HIS ASN PHE PRO LEU ASP LEU ALA                          
SEQRES   1 B  504  GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN          
SEQRES   2 B  504  ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR          
SEQRES   3 B  504  ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR          
SEQRES   4 B  504  GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN          
SEQRES   5 B  504  PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET          
SEQRES   6 B  504  ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER          
SEQRES   7 B  504  ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER          
SEQRES   8 B  504  PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY          
SEQRES   9 B  504  LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP          
SEQRES  10 B  504  ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO          
SEQRES  11 B  504  ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE          
SEQRES  12 B  504  LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS          
SEQRES  13 B  504  LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP          
SEQRES  14 B  504  PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO          
SEQRES  15 B  504  GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY          
SEQRES  16 B  504  GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY          
SEQRES  17 B  504  ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO          
SEQRES  18 B  504  GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU          
SEQRES  19 B  504  THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA          
SEQRES  20 B  504  ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA          
SEQRES  21 B  504  THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN          
SEQRES  22 B  504  TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG          
SEQRES  23 B  504  VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU          
SEQRES  24 B  504  ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP          
SEQRES  25 B  504  TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG          
SEQRES  26 B  504  THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA          
SEQRES  27 B  504  TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU          
SEQRES  28 B  504  GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER          
SEQRES  29 B  504  PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS          
SEQRES  30 B  504  ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER          
SEQRES  31 B  504  PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY          
SEQRES  32 B  504  GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL          
SEQRES  33 B  504  LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE          
SEQRES  34 B  504  GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE          
SEQRES  35 B  504  ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA          
SEQRES  36 B  504  VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS          
SEQRES  37 B  504  GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE          
SEQRES  38 B  504  ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE          
SEQRES  39 B  504  TYR GLN LYS VAL GLY ASP VAL THR THR ARG                      
SEQRES   1 C  451  ALA THR ASN ARG ASP GLN GLU SER SER GLY PHE ALA TRP          
SEQRES   2 C  451  TRP ALA GLY ASN ALA ARG LEU ILE ASN LEU SER GLY LYS          
SEQRES   3 C  451  LEU LEU GLY ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL          
SEQRES   4 C  451  PHE TRP ALA GLY ALA MET THR LEU PHE GLU LEU ALA HIS          
SEQRES   5 C  451  PHE ILE PRO GLU LYS PRO MET TYR GLU GLN GLY LEU ILE          
SEQRES   6 C  451  LEU ILE PRO HIS ILE ALA THR LEU GLY TRP GLY VAL GLY          
SEQRES   7 C  451  PRO GLY GLY GLU VAL VAL ASP THR PHE PRO PHE PHE VAL          
SEQRES   8 C  451  VAL GLY VAL VAL HIS LEU ILE SER SER ALA VAL LEU GLY          
SEQRES   9 C  451  PHE GLY GLY VAL TYR HIS ALA ILE ARG GLY PRO GLU THR          
SEQRES  10 C  451  LEU GLU GLU TYR SER SER PHE PHE GLY TYR ASP TRP LYS          
SEQRES  11 C  451  ASP LYS ASN LYS MET THR THR ILE LEU GLY PHE HIS LEU          
SEQRES  12 C  451  ILE VAL LEU GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS          
SEQRES  13 C  451  ALA MET PHE PHE GLY GLY LEU TYR ASP THR TRP ALA PRO          
SEQRES  14 C  451  GLY GLY GLY ASP VAL ARG VAL ILE THR ASN PRO THR LEU          
SEQRES  15 C  451  ASP PRO ARG VAL ILE PHE GLY TYR LEU LEU LYS SER PRO          
SEQRES  16 C  451  PHE GLY GLY GLU GLY TRP ILE VAL SER VAL ASN ASN LEU          
SEQRES  17 C  451  GLU ASP VAL VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE          
SEQRES  18 C  451  CYS ILE ALA GLY GLY ILE TRP HIS ILE LEU THR THR PRO          
SEQRES  19 C  451  PHE GLY TRP ALA ARG ARG ALA PHE ILE TRP SER GLY GLU          
SEQRES  20 C  451  ALA TYR LEU SER TYR SER LEU GLY ALA LEU SER MET MET          
SEQRES  21 C  451  GLY PHE ILE ALA THR CYS PHE VAL TRP PHE ASN ASN THR          
SEQRES  22 C  451  VAL TYR PRO SER GLU PHE TYR GLY PRO THR GLY PRO GLU          
SEQRES  23 C  451  ALA SER GLN ALA GLN ALA MET THR PHE LEU ILE ARG ASP          
SEQRES  24 C  451  GLN LYS LEU GLY ALA ASN VAL GLY SER ALA GLN GLY PRO          
SEQRES  25 C  451  THR GLY LEU GLY LYS TYR LEU MET ARG SER PRO THR GLY          
SEQRES  26 C  451  GLU ILE ILE PHE GLY GLY GLU THR MET ARG PHE TRP ASP          
SEQRES  27 C  451  PHE ARG GLY PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN          
SEQRES  28 C  451  GLY LEU ASP LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO          
SEQRES  29 C  451  TRP GLN GLU ARG ARG ALA ALA GLU TYR MET THR HIS ALA          
SEQRES  30 C  451  PRO LEU GLY SER LEU ASN SER VAL GLY GLY VAL ALA THR          
SEQRES  31 C  451  GLU ILE ASN SER VAL ASN PHE VAL SER PRO ARG SER TRP          
SEQRES  32 C  451  LEU ALA THR SER HIS PHE VAL LEU ALA PHE PHE PHE LEU          
SEQRES  33 C  451  VAL GLY HIS LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA          
SEQRES  34 C  451  ALA ALA GLY PHE GLU LYS GLY ILE ASP ARG GLU SER GLU          
SEQRES  35 C  451  PRO VAL LEU SER MET PRO SER LEU ASP                          
SEQRES   1 D  342  GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS          
SEQRES   2 D  342  ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU          
SEQRES   3 D  342  LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU          
SEQRES   4 D  342  THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY          
SEQRES   5 D  342  LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR          
SEQRES   6 D  342  VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER          
SEQRES   7 D  342  LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE          
SEQRES   8 D  342  THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE          
SEQRES   9 D  342  ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU          
SEQRES  10 D  342  ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO          
SEQRES  11 D  342  TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE          
SEQRES  12 D  342  VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER          
SEQRES  13 D  342  TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE          
SEQRES  14 D  342  ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR          
SEQRES  15 D  342  LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU          
SEQRES  16 D  342  GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL          
SEQRES  17 D  342  GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR          
SEQRES  18 D  342  PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR          
SEQRES  19 D  342  SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE          
SEQRES  20 D  342  GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE          
SEQRES  21 D  342  MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA          
SEQRES  22 D  342  ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR          
SEQRES  23 D  342  ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO          
SEQRES  24 D  342  GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN          
SEQRES  25 D  342  GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO          
SEQRES  26 D  342  HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG          
SEQRES  27 D  342  GLY ASN ALA LEU                                              
SEQRES   1 E   81  THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER          
SEQRES   2 E   81  VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA          
SEQRES   3 E   81  LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU          
SEQRES   4 E   81  ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR          
SEQRES   5 E   81  TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP          
SEQRES   6 E   81  ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU          
SEQRES   7 E   81  GLN LEU LYS                                                  
SEQRES   1 F   34  SER TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS          
SEQRES   2 F   34  THR LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE          
SEQRES   3 F   34  ALA ALA MET GLN PHE ILE GLN ARG                              
SEQRES   1 H   65  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 H   65  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 H   65  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 H   65  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 H   65  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY          
SEQRES   1 I   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 I   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 I   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 J   38  SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL ALA THR          
SEQRES   2 J   38  VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY LEU PHE          
SEQRES   3 J   38  PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER LEU              
SEQRES   1 K   37  LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL          
SEQRES   2 K   37  ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU          
SEQRES   3 K   37  ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG                  
SEQRES   1 L   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 L   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 L   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 M   34  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 M   34  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 M   34  VAL GLN THR GLU SER GLN GLN LYS                              
SEQRES   1 O  243  THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA          
SEQRES   2 O  243  ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA          
SEQRES   3 O  243  TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG          
SEQRES   4 O  243  LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU          
SEQRES   5 O  243  PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR          
SEQRES   6 O  243  LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE          
SEQRES   7 O  243  GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR          
SEQRES   8 O  243  PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR          
SEQRES   9 O  243  VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE          
SEQRES  10 O  243  THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL          
SEQRES  11 O  243  THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE          
SEQRES  12 O  243  ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO          
SEQRES  13 O  243  LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE          
SEQRES  14 O  243  ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA          
SEQRES  15 O  243  ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER          
SEQRES  16 O  243  LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE          
SEQRES  17 O  243  ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP          
SEQRES  18 O  243  MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY          
SEQRES  19 O  243  VAL PHE TYR ALA SER ILE GLU PRO ALA                          
SEQRES   1 T   30  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 T   30  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 T   30  PRO ARG ILE THR                                              
SEQRES   1 U   97  GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA          
SEQRES   2 U   97  TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA          
SEQRES   3 U   97  ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA          
SEQRES   4 U   97  LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU          
SEQRES   5 U   97  ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS          
SEQRES   6 U   97  GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR          
SEQRES   7 U   97  GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR          
SEQRES   8 U   97  ASN ASN GLY LEU TYR LYS                                      
SEQRES   1 V  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 V  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 V  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 V  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 V  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 V  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 V  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 V  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 V  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 V  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 V  137  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 Y   29  VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE          
SEQRES   2 Y   29  ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG          
SEQRES   3 Y   29  GLY ASN LEU                                                  
SEQRES   1 X   39  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 X   39  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 X   39  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER          
SEQRES   1 Z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 Z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 Z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 Z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 Z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
SEQRES   1 a  334  ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER          
SEQRES   2 a  334  THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE          
SEQRES   3 a  334  MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL          
SEQRES   4 a  334  ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY          
SEQRES   5 a  334  ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN          
SEQRES   6 a  334  ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA          
SEQRES   7 a  334  ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER          
SEQRES   8 a  334  LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU          
SEQRES   9 a  334  ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET          
SEQRES  10 a  334  GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG          
SEQRES  11 a  334  PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER          
SEQRES  12 a  334  ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY          
SEQRES  13 a  334  SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR          
SEQRES  14 a  334  PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE          
SEQRES  15 a  334  LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL          
SEQRES  16 a  334  PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU          
SEQRES  17 a  334  VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU          
SEQRES  18 a  334  SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU          
SEQRES  19 a  334  THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG          
SEQRES  20 a  334  LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER          
SEQRES  21 a  334  LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL          
SEQRES  22 a  334  TRP PHE ALA ALA LEU GLY ILE SER THR MET ALA PHE ASN          
SEQRES  23 a  334  LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA          
SEQRES  24 a  334  LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN          
SEQRES  25 a  334  ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN          
SEQRES  26 a  334  ALA HIS ASN PHE PRO LEU ASP LEU ALA                          
SEQRES   1 b  504  GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN          
SEQRES   2 b  504  ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR          
SEQRES   3 b  504  ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR          
SEQRES   4 b  504  GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN          
SEQRES   5 b  504  PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET          
SEQRES   6 b  504  ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER          
SEQRES   7 b  504  ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER          
SEQRES   8 b  504  PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY          
SEQRES   9 b  504  LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP          
SEQRES  10 b  504  ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO          
SEQRES  11 b  504  ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE          
SEQRES  12 b  504  LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS          
SEQRES  13 b  504  LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP          
SEQRES  14 b  504  PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO          
SEQRES  15 b  504  GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY          
SEQRES  16 b  504  GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY          
SEQRES  17 b  504  ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO          
SEQRES  18 b  504  GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU          
SEQRES  19 b  504  THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA          
SEQRES  20 b  504  ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA          
SEQRES  21 b  504  THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN          
SEQRES  22 b  504  TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG          
SEQRES  23 b  504  VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU          
SEQRES  24 b  504  ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP          
SEQRES  25 b  504  TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG          
SEQRES  26 b  504  THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA          
SEQRES  27 b  504  TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU          
SEQRES  28 b  504  GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER          
SEQRES  29 b  504  PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS          
SEQRES  30 b  504  ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER          
SEQRES  31 b  504  PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY          
SEQRES  32 b  504  GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL          
SEQRES  33 b  504  LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE          
SEQRES  34 b  504  GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE          
SEQRES  35 b  504  ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA          
SEQRES  36 b  504  VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS          
SEQRES  37 b  504  GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE          
SEQRES  38 b  504  ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE          
SEQRES  39 b  504  TYR GLN LYS VAL GLY ASP VAL THR THR ARG                      
SEQRES   1 c  451  ALA THR ASN ARG ASP GLN GLU SER SER GLY PHE ALA TRP          
SEQRES   2 c  451  TRP ALA GLY ASN ALA ARG LEU ILE ASN LEU SER GLY LYS          
SEQRES   3 c  451  LEU LEU GLY ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL          
SEQRES   4 c  451  PHE TRP ALA GLY ALA MET THR LEU PHE GLU LEU ALA HIS          
SEQRES   5 c  451  PHE ILE PRO GLU LYS PRO MET TYR GLU GLN GLY LEU ILE          
SEQRES   6 c  451  LEU ILE PRO HIS ILE ALA THR LEU GLY TRP GLY VAL GLY          
SEQRES   7 c  451  PRO GLY GLY GLU VAL VAL ASP THR PHE PRO PHE PHE VAL          
SEQRES   8 c  451  VAL GLY VAL VAL HIS LEU ILE SER SER ALA VAL LEU GLY          
SEQRES   9 c  451  PHE GLY GLY VAL TYR HIS ALA ILE ARG GLY PRO GLU THR          
SEQRES  10 c  451  LEU GLU GLU TYR SER SER PHE PHE GLY TYR ASP TRP LYS          
SEQRES  11 c  451  ASP LYS ASN LYS MET THR THR ILE LEU GLY PHE HIS LEU          
SEQRES  12 c  451  ILE VAL LEU GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS          
SEQRES  13 c  451  ALA MET PHE PHE GLY GLY LEU TYR ASP THR TRP ALA PRO          
SEQRES  14 c  451  GLY GLY GLY ASP VAL ARG VAL ILE THR ASN PRO THR LEU          
SEQRES  15 c  451  ASP PRO ARG VAL ILE PHE GLY TYR LEU LEU LYS SER PRO          
SEQRES  16 c  451  PHE GLY GLY GLU GLY TRP ILE VAL SER VAL ASN ASN LEU          
SEQRES  17 c  451  GLU ASP VAL VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE          
SEQRES  18 c  451  CYS ILE ALA GLY GLY ILE TRP HIS ILE LEU THR THR PRO          
SEQRES  19 c  451  PHE GLY TRP ALA ARG ARG ALA PHE ILE TRP SER GLY GLU          
SEQRES  20 c  451  ALA TYR LEU SER TYR SER LEU GLY ALA LEU SER MET MET          
SEQRES  21 c  451  GLY PHE ILE ALA THR CYS PHE VAL TRP PHE ASN ASN THR          
SEQRES  22 c  451  VAL TYR PRO SER GLU PHE TYR GLY PRO THR GLY PRO GLU          
SEQRES  23 c  451  ALA SER GLN ALA GLN ALA MET THR PHE LEU ILE ARG ASP          
SEQRES  24 c  451  GLN LYS LEU GLY ALA ASN VAL GLY SER ALA GLN GLY PRO          
SEQRES  25 c  451  THR GLY LEU GLY LYS TYR LEU MET ARG SER PRO THR GLY          
SEQRES  26 c  451  GLU ILE ILE PHE GLY GLY GLU THR MET ARG PHE TRP ASP          
SEQRES  27 c  451  PHE ARG GLY PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN          
SEQRES  28 c  451  GLY LEU ASP LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO          
SEQRES  29 c  451  TRP GLN GLU ARG ARG ALA ALA GLU TYR MET THR HIS ALA          
SEQRES  30 c  451  PRO LEU GLY SER LEU ASN SER VAL GLY GLY VAL ALA THR          
SEQRES  31 c  451  GLU ILE ASN SER VAL ASN PHE VAL SER PRO ARG SER TRP          
SEQRES  32 c  451  LEU ALA THR SER HIS PHE VAL LEU ALA PHE PHE PHE LEU          
SEQRES  33 c  451  VAL GLY HIS LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA          
SEQRES  34 c  451  ALA ALA GLY PHE GLU LYS GLY ILE ASP ARG GLU SER GLU          
SEQRES  35 c  451  PRO VAL LEU SER MET PRO SER LEU ASP                          
SEQRES   1 d  342  GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS          
SEQRES   2 d  342  ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU          
SEQRES   3 d  342  LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU          
SEQRES   4 d  342  THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY          
SEQRES   5 d  342  LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR          
SEQRES   6 d  342  VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER          
SEQRES   7 d  342  LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE          
SEQRES   8 d  342  THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE          
SEQRES   9 d  342  ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU          
SEQRES  10 d  342  ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO          
SEQRES  11 d  342  TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE          
SEQRES  12 d  342  VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER          
SEQRES  13 d  342  TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE          
SEQRES  14 d  342  ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR          
SEQRES  15 d  342  LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU          
SEQRES  16 d  342  GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL          
SEQRES  17 d  342  GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR          
SEQRES  18 d  342  PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR          
SEQRES  19 d  342  SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE          
SEQRES  20 d  342  GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE          
SEQRES  21 d  342  MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA          
SEQRES  22 d  342  ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR          
SEQRES  23 d  342  ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO          
SEQRES  24 d  342  GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN          
SEQRES  25 d  342  GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO          
SEQRES  26 d  342  HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG          
SEQRES  27 d  342  GLY ASN ALA LEU                                              
SEQRES   1 e   81  THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER          
SEQRES   2 e   81  VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA          
SEQRES   3 e   81  LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU          
SEQRES   4 e   81  ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR          
SEQRES   5 e   81  TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP          
SEQRES   6 e   81  ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU          
SEQRES   7 e   81  GLN LEU LYS                                                  
SEQRES   1 f   34  SER TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS          
SEQRES   2 f   34  THR LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE          
SEQRES   3 f   34  ALA ALA MET GLN PHE ILE GLN ARG                              
SEQRES   1 h   65  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 h   65  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 h   65  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 h   65  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 h   65  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY          
SEQRES   1 i   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 i   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 i   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 j   38  SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL ALA THR          
SEQRES   2 j   38  VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY LEU PHE          
SEQRES   3 j   38  PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER LEU              
SEQRES   1 k   37  LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL          
SEQRES   2 k   37  ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU          
SEQRES   3 k   37  ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG                  
SEQRES   1 l   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 l   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 l   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 m   34  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 m   34  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 m   34  VAL GLN THR GLU SER GLN GLN LYS                              
SEQRES   1 o  243  THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA          
SEQRES   2 o  243  ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA          
SEQRES   3 o  243  TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG          
SEQRES   4 o  243  LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU          
SEQRES   5 o  243  PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR          
SEQRES   6 o  243  LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE          
SEQRES   7 o  243  GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR          
SEQRES   8 o  243  PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR          
SEQRES   9 o  243  VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE          
SEQRES  10 o  243  THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL          
SEQRES  11 o  243  THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE          
SEQRES  12 o  243  ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO          
SEQRES  13 o  243  LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE          
SEQRES  14 o  243  ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA          
SEQRES  15 o  243  ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER          
SEQRES  16 o  243  LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE          
SEQRES  17 o  243  ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP          
SEQRES  18 o  243  MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY          
SEQRES  19 o  243  VAL PHE TYR ALA SER ILE GLU PRO ALA                          
SEQRES   1 t   30  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 t   30  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 t   30  PRO ARG ILE THR                                              
SEQRES   1 u   97  GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA          
SEQRES   2 u   97  TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA          
SEQRES   3 u   97  ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA          
SEQRES   4 u   97  LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU          
SEQRES   5 u   97  ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS          
SEQRES   6 u   97  GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR          
SEQRES   7 u   97  GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR          
SEQRES   8 u   97  ASN ASN GLY LEU TYR LYS                                      
SEQRES   1 v  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 v  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 v  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 v  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 v  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 v  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 v  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 v  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 v  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 v  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 v  137  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 y   29  VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE          
SEQRES   2 y   29  ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG          
SEQRES   3 y   29  GLY ASN LEU                                                  
SEQRES   1 x   39  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 x   39  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 x   39  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER          
SEQRES   1 z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
HET    OEX  A 601      10                                                       
HET     CL  A 602       1                                                       
HET     CL  A 603       1                                                       
HET    BCT  A 604       4                                                       
HET    CLA  A 605      65                                                       
HET    CLA  A 606      65                                                       
HET    PHO  A 607      64                                                       
HET    CLA  A 608      65                                                       
HET    BCR  A 609      40                                                       
HET    PL9  A 610      55                                                       
HET    SQD  A 611      54                                                       
HET    LMG  A 612      51                                                       
HET    FE2  A 613       1                                                       
HET     CA  B 601       1                                                       
HET    CLA  B 602      65                                                       
HET    CLA  B 603      65                                                       
HET    CLA  B 604      65                                                       
HET    CLA  B 605      65                                                       
HET    CLA  B 606      65                                                       
HET    CLA  B 607     130                                                       
HET    CLA  B 608      65                                                       
HET    CLA  B 609      65                                                       
HET    CLA  B 610      65                                                       
HET    CLA  B 611      65                                                       
HET    CLA  B 612      65                                                       
HET    CLA  B 613      65                                                       
HET    CLA  B 614      65                                                       
HET    CLA  B 615      65                                                       
HET    CLA  B 616      65                                                       
HET    CLA  B 617      65                                                       
HET    BCR  B 618      40                                                       
HET    BCR  B 619      40                                                       
HET    BCR  B 620      40                                                       
HET    LMG  B 621      51                                                       
HET    LHG  B 622      49                                                       
HET    SQD  B 623      54                                                       
HET    CLA  C 501      65                                                       
HET    CLA  C 502      65                                                       
HET    CLA  C 503      65                                                       
HET    CLA  C 504      65                                                       
HET    CLA  C 505      65                                                       
HET    CLA  C 506      65                                                       
HET    CLA  C 507      65                                                       
HET    CLA  C 508      65                                                       
HET    CLA  C 509      65                                                       
HET    CLA  C 510      65                                                       
HET    CLA  C 511      65                                                       
HET    CLA  C 512      65                                                       
HET    CLA  C 513      65                                                       
HET    BCR  C 514      40                                                       
HET    BCR  C 515      40                                                       
HET    DGD  C 516      62                                                       
HET    DGD  C 517      62                                                       
HET    DGD  C 518      62                                                       
HET    LMG  C 519      51                                                       
HET    LMG  C 520      51                                                       
HET    BCR  C 521      40                                                       
HET    PHO  D 401      64                                                       
HET    CLA  D 402      65                                                       
HET    CLA  D 403      65                                                       
HET    CLA  D 404      65                                                       
HET    PL9  D 405      55                                                       
HET    DGD  D 406      62                                                       
HET    LHG  D 407      49                                                       
HET    LHG  D 408      49                                                       
HET    LHG  E 101      42                                                       
HET    HEM  E 102      43                                                       
HET    BCR  F 101      40                                                       
HET     CA  F 102       1                                                       
HET    BCR  H 101      40                                                       
HET    DGD  H 102      62                                                       
HET    LMG  J 101      51                                                       
HET     MG  J 102       1                                                       
HET    BCR  K 101      40                                                       
HET    LHG  L 101      49                                                       
HET     CA  O 301       1                                                       
HET    BCR  T 101      40                                                       
HET     CL  V 201       1                                                       
HET    HEM  V 202      43                                                       
HET    SQD  X 101      43                                                       
HET    LMG  Z 101      37                                                       
HET    OEX  a 601      10                                                       
HET     CL  a 602       1                                                       
HET    BCT  a 603       4                                                       
HET    CLA  a 604      65                                                       
HET    CLA  a 605      65                                                       
HET    PHO  a 606      64                                                       
HET    CLA  a 607      65                                                       
HET    BCR  a 608      40                                                       
HET    PL9  a 609      55                                                       
HET    SQD  a 610      54                                                       
HET    LMG  a 611      51                                                       
HET    SQD  a 612      54                                                       
HET    CLA  a 613      65                                                       
HET    LHG  a 614      49                                                       
HET    FE2  a 615       1                                                       
HET    SQD  b 601      54                                                       
HET    SQD  b 602      54                                                       
HET     CA  b 603       1                                                       
HET    CLA  b 604      65                                                       
HET    CLA  b 605      65                                                       
HET    CLA  b 606      65                                                       
HET    CLA  b 607      65                                                       
HET    CLA  b 608      65                                                       
HET    CLA  b 609     130                                                       
HET    CLA  b 610      65                                                       
HET    CLA  b 611      65                                                       
HET    CLA  b 612      65                                                       
HET    CLA  b 613      65                                                       
HET    CLA  b 614      65                                                       
HET    CLA  b 615      65                                                       
HET    CLA  b 616      65                                                       
HET    CLA  b 617      65                                                       
HET    CLA  b 618      65                                                       
HET    CLA  b 619      65                                                       
HET    BCR  b 620      40                                                       
HET    BCR  b 621      40                                                       
HET    BCR  b 622      40                                                       
HET    LMG  b 623      51                                                       
HET    LHG  b 624      49                                                       
HET     CL  c 501       1                                                       
HET    CLA  c 502      65                                                       
HET    CLA  c 503      65                                                       
HET    CLA  c 504      65                                                       
HET    CLA  c 505      65                                                       
HET    CLA  c 506      65                                                       
HET    CLA  c 507      65                                                       
HET    CLA  c 508      65                                                       
HET    CLA  c 509      65                                                       
HET    CLA  c 510      65                                                       
HET    CLA  c 511      65                                                       
HET    CLA  c 512      65                                                       
HET    CLA  c 513      65                                                       
HET    CLA  c 514      65                                                       
HET    BCR  c 515      40                                                       
HET    BCR  c 516      40                                                       
HET    DGD  c 517      62                                                       
HET    DGD  c 518      62                                                       
HET    DGD  c 519      62                                                       
HET    LMG  c 520      51                                                       
HET    LMG  c 521      51                                                       
HET    BCR  c 522      40                                                       
HET    PHO  d 401      64                                                       
HET    CLA  d 402      65                                                       
HET    CLA  d 403      65                                                       
HET    PL9  d 404      55                                                       
HET    DGD  d 405      62                                                       
HET    LHG  d 406      49                                                       
HET    LHG  e 101      42                                                       
HET    HEM  e 102      43                                                       
HET    BCR  f 101      40                                                       
HET     CA  f 102       1                                                       
HET    BCR  h 101      40                                                       
HET    DGD  h 102      62                                                       
HET    LMG  j 101      51                                                       
HET     MG  j 102       1                                                       
HET    BCR  k 101      40                                                       
HET    LHG  l 101      49                                                       
HET     CA  o 301       1                                                       
HET    BCR  t 101      40                                                       
HET     CL  u 201       1                                                       
HET    HEM  v 201      43                                                       
HET    SQD  x 101      43                                                       
HET    LMG  z 101      37                                                       
HETNAM     OEX CA-MN4-O5 CLUSTER                                                
HETNAM      CL CHLORIDE ION                                                     
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN A                                                     
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,           
HETNAM   2 PL9  6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-               
HETNAM   3 PL9  CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-          
HETNAM   4 PL9  BENZOQUINONE                                                    
HETNAM     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM     FE2 FE (II) ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     HEM HEME                                                             
FORMUL  39  OEX    2(CA MN4 O5)                                                 
FORMUL  40   CL    6(CL 1-)                                                     
FORMUL  42  BCT    2(C H O3 1-)                                                 
FORMUL  43  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  45  PHO    4(C55 H74 N4 O5)                                             
FORMUL  47  BCR    22(C40 H56)                                                  
FORMUL  48  PL9    4(C53 H80 O2)                                                
FORMUL  49  SQD    8(C41 H78 O12 S)                                             
FORMUL  50  LMG    12(C45 H86 O10)                                              
FORMUL  51  FE2    2(FE 2+)                                                     
FORMUL  52   CA    6(CA 2+)                                                     
FORMUL  73  LHG    10(C38 H75 O10 P)                                            
FORMUL  90  DGD    10(C51 H96 O15)                                              
FORMUL  05  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  11   MG    2(MG 2+)                                                     
HELIX    1 AA1 ASN A   12  THR A   22  1                                  11    
HELIX    2 AA2 VAL A   30  ALA A   55  1                                  26    
HELIX    3 AA3 SER A   70  GLY A   74  5                                   5    
HELIX    4 AA4 PRO A   95  ALA A   99  5                                   5    
HELIX    5 AA5 SER A  101  ASN A  108  1                                   8    
HELIX    6 AA6 GLY A  109  LEU A  137  1                                  29    
HELIX    7 AA7 TRP A  142  LEU A  159  1                                  18    
HELIX    8 AA8 LEU A  159  GLY A  166  1                                   8    
HELIX    9 AA9 SER A  167  GLY A  171  5                                   5    
HELIX   10 AB1 ILE A  176  ASN A  191  1                                  16    
HELIX   11 AB2 ILE A  192  MET A  194  5                                   3    
HELIX   12 AB3 HIS A  195  SER A  222  1                                  28    
HELIX   13 AB4 SER A  232  TYR A  237  5                                   6    
HELIX   14 AB5 ASN A  247  ILE A  259  1                                  13    
HELIX   15 AB6 PHE A  260  SER A  264  5                                   5    
HELIX   16 AB7 ASN A  267  ALA A  294  1                                  28    
HELIX   17 AB8 THR A  316  HIS A  332  1                                  17    
HELIX   18 AB9 TYR B    6  ILE B   13  5                                   8    
HELIX   19 AC1 ASP B   15  PHE B   45  1                                  31    
HELIX   20 AC2 PRO B   54  GLN B   58  5                                   5    
HELIX   21 AC3 VAL B   62  LEU B   69  1                                   8    
HELIX   22 AC4 SER B   92  TYR B  117  1                                  26    
HELIX   23 AC5 LEU B  120  ARG B  124  5                                   5    
HELIX   24 AC6 ASP B  134  PHE B  156  1                                  23    
HELIX   25 AC7 GLY B  186  ASN B  191  5                                   6    
HELIX   26 AC8 ASN B  194  VAL B  219  1                                  26    
HELIX   27 AC9 PRO B  222  LEU B  229  1                                   8    
HELIX   28 AD1 ASN B  233  GLY B  259  1                                  27    
HELIX   29 AD2 PRO B  264  GLY B  269  1                                   6    
HELIX   30 AD3 THR B  271  SER B  277  1                                   7    
HELIX   31 AD4 SER B  278  SER B  294  1                                  17    
HELIX   32 AD5 THR B  297  ALA B  304  1                                   8    
HELIX   33 AD6 PRO B  306  ASP B  313  1                                   8    
HELIX   34 AD7 TYR B  314  GLY B  322  5                                   9    
HELIX   35 AD8 PRO B  329  GLY B  333  5                                   5    
HELIX   36 AD9 SER B  391  GLY B  396  1                                   6    
HELIX   37 AE1 ASP B  413  ILE B  425  1                                  13    
HELIX   38 AE2 SER B  446  PHE B  475  1                                  30    
HELIX   39 AE3 ARG B  476  PHE B  479  5                                   4    
HELIX   40 AE4 SER B  487  VAL B  491  5                                   5    
HELIX   41 AE5 ASP B  501  ARG B  505  5                                   5    
HELIX   42 AE6 ASP C   27  GLY C   32  1                                   6    
HELIX   43 AE7 ALA C   34  ILE C   43  5                                  10    
HELIX   44 AE8 LEU C   45  PHE C   75  1                                  31    
HELIX   45 AE9 PRO C   80  GLN C   84  5                                   5    
HELIX   46 AF1 ILE C   87  LEU C   95  1                                   9    
HELIX   47 AF2 GLY C  100  GLU C  104  5                                   5    
HELIX   48 AF3 THR C  108  ARG C  135  1                                  28    
HELIX   49 AF4 ASP C  153  PHE C  182  1                                  30    
HELIX   50 AF5 ASP C  205  LEU C  214  1                                  10    
HELIX   51 AF6 GLY C  222  VAL C  227  5                                   6    
HELIX   52 AF7 ASN C  229  THR C  254  1                                  26    
HELIX   53 AF8 PHE C  257  PHE C  264  1                                   8    
HELIX   54 AF9 SER C  267  ASN C  293  1                                  27    
HELIX   55 AG1 PRO C  298  GLY C  303  1                                   6    
HELIX   56 AG2 THR C  305  LEU C  324  1                                  20    
HELIX   57 AG3 GLY C  353  TRP C  359  5                                   7    
HELIX   58 AG4 LEU C  366  PRO C  368  5                                   3    
HELIX   59 AG5 ASP C  376  ASP C  383  1                                   8    
HELIX   60 AG6 GLN C  385  THR C  397  1                                  13    
HELIX   61 AG7 SER C  421  GLY C  454  1                                  34    
HELIX   62 AG8 ASP C  460  MET C  469  5                                  10    
HELIX   63 AG9 GLY D   13  LYS D   23  1                                  11    
HELIX   64 AH1 VAL D   30  VAL D   55  1                                  26    
HELIX   65 AH2 SER D   66  GLY D   70  5                                   5    
HELIX   66 AH3 ALA D   82  GLY D   86  5                                   5    
HELIX   67 AH4 ASP D  100  LEU D  107  1                                   8    
HELIX   68 AH5 GLY D  108  GLY D  137  1                                  30    
HELIX   69 AH6 PRO D  140  LEU D  158  1                                  19    
HELIX   70 AH7 LEU D  158  GLN D  164  1                                   7    
HELIX   71 AH8 SER D  166  ALA D  170  5                                   5    
HELIX   72 AH9 VAL D  175  ASN D  190  1                                  16    
HELIX   73 AI1 TRP D  191  LEU D  193  5                                   3    
HELIX   74 AI2 ASN D  194  ASN D  220  1                                  27    
HELIX   75 AI3 THR D  231  PHE D  235  5                                   5    
HELIX   76 AI4 SER D  245  PHE D  257  1                                  13    
HELIX   77 AI5 ASN D  263  ALA D  290  1                                  28    
HELIX   78 AI6 PHE D  298  ASP D  308  1                                  11    
HELIX   79 AI7 THR D  313  GLN D  334  1                                  22    
HELIX   80 AI8 PRO D  335  ASN D  338  5                                   4    
HELIX   81 AI9 PRO D  342  LEU D  346  5                                   5    
HELIX   82 AJ1 PRO E    9  THR E   15  1                                   7    
HELIX   83 AJ2 SER E   16  THR E   40  1                                  25    
HELIX   84 AJ3 GLY E   41  GLY E   48  1                                   8    
HELIX   85 AJ4 GLU E   71  GLN E   82  1                                  12    
HELIX   86 AJ5 THR F   17  GLN F   41  1                                  25    
HELIX   87 AJ6 THR H    5  ARG H   12  1                                   8    
HELIX   88 AJ7 PRO H   13  SER H   16  5                                   4    
HELIX   89 AJ8 THR H   27  ASN H   50  1                                  24    
HELIX   90 AJ9 SER H   61  LEU H   65  5                                   5    
HELIX   91 AK1 GLU I    2  SER I   25  1                                  24    
HELIX   92 AK2 GLY I   26  ARG I   30  5                                   5    
HELIX   93 AK3 PRO J    9  TYR J   33  1                                  25    
HELIX   94 AK4 PRO K   12  ILE K   17  5                                   6    
HELIX   95 AK5 PHE K   18  LEU K   25  1                                   8    
HELIX   96 AK6 VAL K   27  VAL K   43  1                                  17    
HELIX   97 AK7 ASN L   13  ASN L   37  1                                  25    
HELIX   98 AK8 LEU M    6  SER M   31  1                                  26    
HELIX   99 AK9 THR O    6  VAL O   11  1                                   6    
HELIX  100 AL1 GLY O   14  LYS O   18  5                                   5    
HELIX  101 AL2 GLU O  179  GLU O  181  5                                   3    
HELIX  102 AL3 LEU O  182  VAL O  187  1                                   6    
HELIX  103 AL4 GLU T    2  PHE T   23  1                                  22    
HELIX  104 AL5 ASN U   11  GLY U   18  1                                   8    
HELIX  105 AL6 THR U   19  GLU U   23  5                                   5    
HELIX  106 AL7 ASN U   31  TYR U   38  5                                   8    
HELIX  107 AL8 PRO U   43  ALA U   53  1                                  11    
HELIX  108 AL9 SER U   57  ILE U   64  5                                   8    
HELIX  109 AM1 THR U   68  LEU U   79  1                                  12    
HELIX  110 AM2 GLU U   88  GLU U   93  1                                   6    
HELIX  111 AM3 GLY U   94  ASP U   96  5                                   3    
HELIX  112 AM4 THR V   22  CYS V   37  1                                  16    
HELIX  113 AM5 CYS V   37  VAL V   42  1                                   6    
HELIX  114 AM6 GLY V   43  ILE V   45  5                                   3    
HELIX  115 AM7 ARG V   55  ALA V   62  1                                   8    
HELIX  116 AM8 ASN V   68  ASN V   78  1                                  11    
HELIX  117 AM9 PHE V  101  ARG V  105  5                                   5    
HELIX  118 AN1 THR V  108  GLY V  127  1                                  20    
HELIX  119 AN2 ASP V  128  TRP V  130  5                                   3    
HELIX  120 AN3 GLY V  133  TYR V  137  5                                   5    
HELIX  121 AN4 ILE Y   19  ARG Y   42  1                                  24    
HELIX  122 AN5 THR X    4  ASP X   35  1                                  32    
HELIX  123 AN6 THR Z    2  SER Z   29  1                                  28    
HELIX  124 AN7 ASP Z   32  ASN Z   58  1                                  27    
HELIX  125 AN8 PHE Z   59  VAL Z   61  5                                   3    
HELIX  126 AN9 ASN a   12  THR a   22  1                                  11    
HELIX  127 AO1 VAL a   30  ALA a   55  1                                  26    
HELIX  128 AO2 PRO a   95  ALA a   99  5                                   5    
HELIX  129 AO3 SER a  101  ASN a  108  1                                   8    
HELIX  130 AO4 GLY a  109  LEU a  137  1                                  29    
HELIX  131 AO5 TRP a  142  LEU a  159  1                                  18    
HELIX  132 AO6 LEU a  159  GLY a  166  1                                   8    
HELIX  133 AO7 SER a  167  GLY a  171  5                                   5    
HELIX  134 AO8 ILE a  176  ASN a  191  1                                  16    
HELIX  135 AO9 ILE a  192  MET a  194  5                                   3    
HELIX  136 AP1 HIS a  195  SER a  222  1                                  28    
HELIX  137 AP2 SER a  232  TYR a  237  5                                   6    
HELIX  138 AP3 ASN a  247  ILE a  259  1                                  13    
HELIX  139 AP4 PHE a  260  SER a  264  5                                   5    
HELIX  140 AP5 ASN a  267  ALA a  294  1                                  28    
HELIX  141 AP6 THR a  316  HIS a  332  1                                  17    
HELIX  142 AP7 TYR b    6  ILE b   13  5                                   8    
HELIX  143 AP8 ASP b   15  PHE b   45  1                                  31    
HELIX  144 AP9 PRO b   54  GLN b   58  5                                   5    
HELIX  145 AQ1 VAL b   62  LEU b   69  1                                   8    
HELIX  146 AQ2 SER b   92  TYR b  117  1                                  26    
HELIX  147 AQ3 LEU b  120  ARG b  124  5                                   5    
HELIX  148 AQ4 ASP b  134  PHE b  156  1                                  23    
HELIX  149 AQ5 GLY b  186  ASN b  191  5                                   6    
HELIX  150 AQ6 ASN b  194  VAL b  219  1                                  26    
HELIX  151 AQ7 PRO b  222  LEU b  229  1                                   8    
HELIX  152 AQ8 ASN b  233  GLY b  259  1                                  27    
HELIX  153 AQ9 PRO b  264  GLY b  269  1                                   6    
HELIX  154 AR1 THR b  271  SER b  277  1                                   7    
HELIX  155 AR2 SER b  278  SER b  294  1                                  17    
HELIX  156 AR3 THR b  297  ALA b  304  1                                   8    
HELIX  157 AR4 PRO b  306  ASP b  313  1                                   8    
HELIX  158 AR5 TYR b  314  GLY b  322  5                                   9    
HELIX  159 AR6 PRO b  329  GLY b  333  5                                   5    
HELIX  160 AR7 ASP b  413  ILE b  425  1                                  13    
HELIX  161 AR8 SER b  446  PHE b  475  1                                  30    
HELIX  162 AR9 ARG b  476  PHE b  479  5                                   4    
HELIX  163 AS1 SER b  487  GLU b  492  1                                   6    
HELIX  164 AS2 ASP b  501  ARG b  505  5                                   5    
HELIX  165 AS3 ASP c   27  GLY c   32  1                                   6    
HELIX  166 AS4 ALA c   34  ILE c   43  5                                  10    
HELIX  167 AS5 LEU c   45  PHE c   75  1                                  31    
HELIX  168 AS6 PRO c   80  GLN c   84  5                                   5    
HELIX  169 AS7 ILE c   87  LEU c   95  1                                   9    
HELIX  170 AS8 GLY c  100  GLU c  104  5                                   5    
HELIX  171 AS9 THR c  108  ARG c  135  1                                  28    
HELIX  172 AT1 ASP c  153  PHE c  182  1                                  30    
HELIX  173 AT2 ASP c  205  LEU c  214  1                                  10    
HELIX  174 AT3 GLY c  222  VAL c  227  5                                   6    
HELIX  175 AT4 ASN c  229  THR c  254  1                                  26    
HELIX  176 AT5 PHE c  257  PHE c  264  1                                   8    
HELIX  177 AT6 SER c  267  ASN c  293  1                                  27    
HELIX  178 AT7 PRO c  298  GLY c  303  1                                   6    
HELIX  179 AT8 THR c  305  GLY c  325  1                                  21    
HELIX  180 AT9 GLY c  353  TRP c  359  5                                   7    
HELIX  181 AU1 LEU c  366  PRO c  368  5                                   3    
HELIX  182 AU2 ASP c  376  ASP c  383  1                                   8    
HELIX  183 AU3 GLN c  385  THR c  397  1                                  13    
HELIX  184 AU4 SER c  421  GLY c  454  1                                  34    
HELIX  185 AU5 ASP c  460  MET c  469  5                                  10    
HELIX  186 AU6 GLY d   13  LYS d   23  1                                  11    
HELIX  187 AU7 VAL d   30  VAL d   55  1                                  26    
HELIX  188 AU8 SER d   57  GLY d   62  1                                   6    
HELIX  189 AU9 SER d   66  GLY d   70  5                                   5    
HELIX  190 AV1 ALA d   82  GLY d   86  5                                   5    
HELIX  191 AV2 ASP d  100  LEU d  107  1                                   8    
HELIX  192 AV3 GLY d  108  GLY d  137  1                                  30    
HELIX  193 AV4 PRO d  140  LEU d  158  1                                  19    
HELIX  194 AV5 LEU d  158  GLN d  164  1                                   7    
HELIX  195 AV6 SER d  166  ALA d  170  5                                   5    
HELIX  196 AV7 VAL d  175  ASN d  190  1                                  16    
HELIX  197 AV8 TRP d  191  LEU d  193  5                                   3    
HELIX  198 AV9 ASN d  194  ASN d  220  1                                  27    
HELIX  199 AW1 THR d  231  PHE d  235  5                                   5    
HELIX  200 AW2 SER d  245  PHE d  257  1                                  13    
HELIX  201 AW3 ASN d  263  ALA d  290  1                                  28    
HELIX  202 AW4 PHE d  298  ASP d  308  1                                  11    
HELIX  203 AW5 THR d  313  GLN d  334  1                                  22    
HELIX  204 AW6 PRO d  335  ASN d  338  5                                   4    
HELIX  205 AW7 PRO d  342  LEU d  346  5                                   5    
HELIX  206 AW8 PRO e    9  THR e   15  1                                   7    
HELIX  207 AW9 SER e   16  THR e   40  1                                  25    
HELIX  208 AX1 GLY e   41  GLY e   48  1                                   8    
HELIX  209 AX2 GLU e   71  GLN e   82  1                                  12    
HELIX  210 AX3 THR f   17  GLN f   41  1                                  25    
HELIX  211 AX4 THR h    5  ARG h   12  1                                   8    
HELIX  212 AX5 PRO h   13  SER h   16  5                                   4    
HELIX  213 AX6 THR h   27  ASN h   50  1                                  24    
HELIX  214 AX7 GLU i    2  SER i   25  1                                  24    
HELIX  215 AX8 PRO j    9  ALA j   32  1                                  24    
HELIX  216 AX9 PRO k   12  ILE k   17  5                                   6    
HELIX  217 AY1 PHE k   18  LEU k   25  1                                   8    
HELIX  218 AY2 VAL k   27  VAL k   43  1                                  17    
HELIX  219 AY3 ASN l   13  ASN l   37  1                                  25    
HELIX  220 AY4 LEU m    6  SER m   31  1                                  26    
HELIX  221 AY5 THR o    6  VAL o   11  1                                   6    
HELIX  222 AY6 GLY o   14  LYS o   18  5                                   5    
HELIX  223 AY7 LEU o  182  VAL o  187  1                                   6    
HELIX  224 AY8 GLU t    2  PHE t   23  1                                  22    
HELIX  225 AY9 ASN u   11  GLY u   18  1                                   8    
HELIX  226 AZ1 THR u   19  GLU u   23  5                                   5    
HELIX  227 AZ2 ASN u   31  TYR u   38  5                                   8    
HELIX  228 AZ3 PRO u   43  ALA u   53  1                                  11    
HELIX  229 AZ4 SER u   57  ILE u   64  5                                   8    
HELIX  230 AZ5 THR u   68  LEU u   79  1                                  12    
HELIX  231 AZ6 GLU u   88  GLU u   93  1                                   6    
HELIX  232 AZ7 GLY u   94  ASP u   96  5                                   3    
HELIX  233 AZ8 THR v   22  CYS v   37  1                                  16    
HELIX  234 AZ9 CYS v   37  VAL v   42  1                                   6    
HELIX  235 BA1 GLY v   43  ILE v   45  5                                   3    
HELIX  236 BA2 ARG v   55  ALA v   62  1                                   8    
HELIX  237 BA3 ASN v   68  ASN v   78  1                                  11    
HELIX  238 BA4 PHE v  101  ARG v  105  5                                   5    
HELIX  239 BA5 THR v  108  GLY v  127  1                                  20    
HELIX  240 BA6 ASP v  128  TRP v  130  5                                   3    
HELIX  241 BA7 GLY v  132  TYR v  137  5                                   6    
HELIX  242 BA8 ILE y   19  ARG y   42  1                                  24    
HELIX  243 BA9 THR x    4  ASP x   35  1                                  32    
HELIX  244 BB1 THR z    2  SER z   29  1                                  28    
HELIX  245 BB2 ASP z   32  PHE z   59  1                                  28    
SHEET    1 AA1 2 ALA A  81  VAL A  82  0                                        
SHEET    2 AA1 2 LEU A 174  GLY A 175 -1  O  LEU A 174   N  VAL A  82           
SHEET    1 AA2 2 LEU A 297  ASN A 298  0                                        
SHEET    2 AA2 2 GLY C 402  SER C 403  1  O  GLY C 402   N  ASN A 298           
SHEET    1 AA3 2 LEU B   3  PRO B   4  0                                        
SHEET    2 AA3 2 VAL L  10  GLU L  11  1  O  GLU L  11   N  LEU B   3           
SHEET    1 AA4 2 MET B 166  VAL B 168  0                                        
SHEET    2 AA4 2 SER B 177  GLN B 179 -1  O  GLN B 179   N  MET B 166           
SHEET    1 AA5 6 VAL B 377  ASP B 380  0                                        
SHEET    2 AA5 6 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA5 6 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA5 6 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA5 6 THR B 398  TYR B 402 -1  O  THR B 398   N  ARG B 347           
SHEET    6 AA5 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1 AA6 5 VAL B 377  ASP B 380  0                                        
SHEET    2 AA6 5 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA6 5 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA6 5 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA6 5 ILE B 429  ASP B 433 -1  O  GLU B 431   N  GLN B 338           
SHEET    1 AA7 2 LEU C 185  ASP C 187  0                                        
SHEET    2 AA7 2 ASP C 195  ARG C 197 -1  O  ARG C 197   N  LEU C 185           
SHEET    1 AA8 2 LEU C 341  ARG C 343  0                                        
SHEET    2 AA8 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1 AA9 2 ARG C 370  GLY C 371  0                                        
SHEET    2 AA9 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1 AB1 2 ALA D  77  VAL D  78  0                                        
SHEET    2 AB1 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1 AB2 2 TYR O  30  PRO O  31  0                                        
SHEET    2 AB2 2 SER O 135  ILE O 136 -1  O  ILE O 136   N  TYR O  30           
SHEET    1 AB310 PHE O  65  PRO O  67  0                                        
SHEET    2 AB310 TYR O  38  LYS O  53 -1  N  VAL O  52   O  VAL O  66           
SHEET    3 AB310 GLU O 232  PRO O 245 -1  O  GLN O 236   N  THR O  48           
SHEET    4 AB310 GLU O 210  LEU O 220 -1  N  ILE O 211   O  ALA O 241           
SHEET    5 AB310 LEU O 192  ASP O 205 -1  N  ASN O 200   O  THR O 214           
SHEET    6 AB310 ASP O 141  PRO O 149 -1  N  PHE O 142   O  LEU O 199           
SHEET    7 AB310 VAL O 126  SER O 128 -1  N  SER O 128   O  LYS O 143           
SHEET    8 AB310 LEU O  93  ILE O 101 -1  N  PHE O  95   O  ALA O 127           
SHEET    9 AB310 LEU O  78  VAL O  87 -1  N  GLN O  82   O  ASP O  99           
SHEET   10 AB310 TYR O  38  LYS O  53 -1  N  LEU O  45   O  LEU O  78           
SHEET    1 AB4 3 LYS O  69  LEU O  70  0                                        
SHEET    2 AB4 3 PHE O 103  GLN O 109 -1  O  GLN O 109   N  LYS O  69           
SHEET    3 AB4 3 ARG O 115  THR O 121 -1  O  ILE O 116   N  VAL O 108           
SHEET    1 AB5 2 ILE U  25  ASP U  26  0                                        
SHEET    2 AB5 2 PHE U  82  THR U  83  1  O  THR U  83   N  ILE U  25           
SHEET    1 AB6 2 THR V   9  PRO V  11  0                                        
SHEET    2 AB6 2 THR V  18  THR V  20 -1  O  ILE V  19   N  VAL V  10           
SHEET    1 AB7 2 ALA a  81  VAL a  82  0                                        
SHEET    2 AB7 2 LEU a 174  GLY a 175 -1  O  LEU a 174   N  VAL a  82           
SHEET    1 AB8 2 LEU a 297  ASN a 298  0                                        
SHEET    2 AB8 2 GLY c 402  SER c 403  1  O  GLY c 402   N  ASN a 298           
SHEET    1 AB9 2 LEU b   3  PRO b   4  0                                        
SHEET    2 AB9 2 VAL l  10  GLU l  11  1  O  GLU l  11   N  LEU b   3           
SHEET    1 AC1 2 MET b 166  VAL b 168  0                                        
SHEET    2 AC1 2 SER b 177  GLN b 179 -1  O  GLN b 179   N  MET b 166           
SHEET    1 AC2 6 VAL b 377  ASP b 380  0                                        
SHEET    2 AC2 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC2 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC2 6 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC2 6 THR b 398  TYR b 402 -1  O  THR b 398   N  ARG b 347           
SHEET    6 AC2 6 THR b 410  PHE b 411 -1  O  PHE b 411   N  VAL b 399           
SHEET    1 AC3 5 VAL b 377  ASP b 380  0                                        
SHEET    2 AC3 5 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC3 5 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC3 5 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC3 5 ILE b 429  ASP b 433 -1  O  GLU b 431   N  GLN b 338           
SHEET    1 AC4 2 LEU c 185  ASP c 187  0                                        
SHEET    2 AC4 2 ASP c 195  ARG c 197 -1  O  ARG c 197   N  LEU c 185           
SHEET    1 AC5 2 LEU c 341  ARG c 343  0                                        
SHEET    2 AC5 2 ILE c 349  PHE c 351 -1  O  ILE c 350   N  MET c 342           
SHEET    1 AC6 2 ARG c 370  GLY c 371  0                                        
SHEET    2 AC6 2 GLY c 374  LEU c 375 -1  O  GLY c 374   N  GLY c 371           
SHEET    1 AC7 2 ALA d  77  VAL d  78  0                                        
SHEET    2 AC7 2 PHE d 173  GLY d 174 -1  O  PHE d 173   N  VAL d  78           
SHEET    1 AC8 2 TYR o  30  PRO o  31  0                                        
SHEET    2 AC8 2 SER o 135  ILE o 136 -1  O  ILE o 136   N  TYR o  30           
SHEET    1 AC910 PHE o  65  PRO o  67  0                                        
SHEET    2 AC910 TYR o  38  LYS o  53 -1  N  VAL o  52   O  VAL o  66           
SHEET    3 AC910 GLU o 232  PRO o 245 -1  O  GLN o 236   N  THR o  48           
SHEET    4 AC910 GLU o 210  LEU o 220 -1  N  ILE o 211   O  ALA o 241           
SHEET    5 AC910 LEU o 192  ASP o 205 -1  N  GLN o 196   O  GLU o 218           
SHEET    6 AC910 ASP o 141  PRO o 149 -1  N  PHE o 142   O  LEU o 199           
SHEET    7 AC910 VAL o 126  SER o 128 -1  N  SER o 128   O  LYS o 143           
SHEET    8 AC910 LEU o  93  ILE o 101 -1  N  PHE o  95   O  ALA o 127           
SHEET    9 AC910 LEU o  78  VAL o  87 -1  N  GLN o  82   O  ASP o  99           
SHEET   10 AC910 TYR o  38  LYS o  53 -1  N  LEU o  45   O  LEU o  78           
SHEET    1 AD1 3 LYS o  69  LEU o  70  0                                        
SHEET    2 AD1 3 PHE o 103  GLN o 109 -1  O  GLN o 109   N  LYS o  69           
SHEET    3 AD1 3 ARG o 115  THR o 121 -1  O  ILE o 116   N  VAL o 108           
SHEET    1 AD2 2 ILE u  25  ASP u  26  0                                        
SHEET    2 AD2 2 PHE u  82  THR u  83  1  O  THR u  83   N  ILE u  25           
SHEET    1 AD3 2 THR v   9  PRO v  11  0                                        
SHEET    2 AD3 2 THR v  18  THR v  20 -1  O  ILE v  19   N  VAL v  10           
SSBOND   1 CYS O   19    CYS O   44                          1555   1555  2.03  
SSBOND   2 CYS o   19    CYS o   44                          1555   1555  2.03  
LINK         OD1 ASP A 170                CA1  OEX A 601     1555   1555  2.92  
LINK         OD2 ASP A 170                MN4  OEX A 601     1555   1555  2.46  
LINK         OD2 ASP A 170                CA1  OEX A 601     1555   1555  3.19  
LINK         OE2 GLU A 189                MN1  OEX A 601     1555   1555  2.24  
LINK         NE2 HIS A 215                FE   FE2 A 613     1555   1555  2.42  
LINK         NE2 HIS A 272                FE   FE2 A 613     1555   1555  2.42  
LINK         NE2 HIS A 332                MN1  OEX A 601     1555   1555  2.41  
LINK         OE1 GLU A 333                MN3  OEX A 601     1555   1555  2.33  
LINK         OE2 GLU A 333                MN4  OEX A 601     1555   1555  2.43  
LINK         OD1 ASP A 342                MN2  OEX A 601     1555   1555  2.32  
LINK         OD2 ASP A 342                MN1  OEX A 601     1555   1555  2.36  
LINK         O   ALA A 344                CA1  OEX A 601     1555   1555  2.95  
LINK         OXT ALA A 344                MN2  OEX A 601     1555   1555  2.34  
LINK         OD1 ASN C  39                MG   CLA C 511     1555   1555  2.78  
LINK         OE1 GLU C 354                MN2  OEX A 601     1555   1555  2.38  
LINK         OE2 GLU C 354                MN3  OEX A 601     1555   1555  2.40  
LINK         NE2 HIS D 214                FE   FE2 A 613     1555   1555  2.52  
LINK         NE2 HIS D 268                FE   FE2 A 613     1555   1555  2.42  
LINK         NE2 HIS E  23                FE   HEM E 102     1555   1555  2.37  
LINK         NE2 HIS F  24                FE   HEM E 102     1555   1555  2.37  
LINK         O   GLY J  31                MG    MG J 102     1555   1555  2.97  
LINK         O   ALA J  34                MG    MG J 102     1555   1555  2.17  
LINK         O   LEU J  36                MG    MG J 102     1555   1555  2.38  
LINK         O   THR O 138                CA    CA O 301     1555   1555  2.52  
LINK         OD1 ASN O 200                CA    CA O 301     1555   1555  3.19  
LINK         NE2 HIS V  41                FE   HEM V 202     1555   1555  2.32  
LINK         NE2 HIS V  92                FE   HEM V 202     1555   1555  2.38  
LINK         OD1 ASP a 170                CA1  OEX a 601     1555   1555  2.95  
LINK         OD2 ASP a 170                CA1  OEX a 601     1555   1555  3.12  
LINK         OD2 ASP a 170                MN4  OEX a 601     1555   1555  2.50  
LINK         OE2 GLU a 189                MN1  OEX a 601     1555   1555  2.22  
LINK         NE2 HIS a 215                FE   FE2 a 615     1555   1555  2.46  
LINK         NE2 HIS a 272                FE   FE2 a 615     1555   1555  2.40  
LINK         NE2 HIS a 332                MN1  OEX a 601     1555   1555  2.43  
LINK         OE1 GLU a 333                MN3  OEX a 601     1555   1555  2.29  
LINK         OE2 GLU a 333                MN4  OEX a 601     1555   1555  2.52  
LINK         OD1 ASP a 342                MN2  OEX a 601     1555   1555  2.38  
LINK         OD2 ASP a 342                MN1  OEX a 601     1555   1555  2.34  
LINK         O   ALA a 344                CA1  OEX a 601     1555   1555  2.98  
LINK         OXT ALA a 344                MN2  OEX a 601     1555   1555  2.34  
LINK         OD1 ASN c  39                MG   CLA c 512     1555   1555  2.75  
LINK         OE1 GLU c 354                MN2  OEX a 601     1555   1555  2.32  
LINK         OE2 GLU c 354                MN3  OEX a 601     1555   1555  2.36  
LINK         NE2 HIS d 214                FE   FE2 a 615     1555   1555  2.47  
LINK         NE2 HIS d 268                FE   FE2 a 615     1555   1555  2.40  
LINK         NE2 HIS e  23                FE   HEM e 102     1555   1555  2.42  
LINK         NE2 HIS f  24                FE   HEM e 102     1555   1555  2.40  
LINK         O   ARG f  45                CA    CA f 102     1555   1555  3.02  
LINK         OXT ARG f  45                CA    CA f 102     1555   1555  2.75  
LINK         O   GLY j  31                MG    MG j 102     1555   1555  2.31  
LINK         O   ALA j  34                MG    MG j 102     1555   1555  1.98  
LINK         O   LEU j  36                MG    MG j 102     1555   1555  2.59  
LINK         O   THR o 138                CA    CA o 301     1555   1555  2.41  
LINK         OD1 ASN o 200                CA    CA o 301     1555   1555  2.57  
LINK         O   VAL o 201                CA    CA o 301     1555   1555  2.48  
LINK         OE1 GLU v  23                CA    CA f 102     1555   1555  3.10  
LINK         NE2 HIS v  41                FE   HEM v 201     1555   1555  2.34  
LINK         NE2 HIS v  92                FE   HEM v 201     1555   1555  2.39  
LINK         O1  BCT A 604                FE   FE2 A 613     1555   1555  2.52  
LINK         O2  BCT A 604                FE   FE2 A 613     1555   1555  2.52  
LINK         O4  LMG J 101                MG    MG J 102     1555   1555  2.71  
LINK         O1  BCT a 603                FE   FE2 a 615     1555   1555  2.57  
LINK         O2  BCT a 603                FE   FE2 a 615     1555   1555  2.54  
LINK         O4  LMG j 101                MG    MG j 102     1555   1555  2.37  
CISPEP   1 TYR U   42    PRO U   43          0         3.67                     
CISPEP   2 ALA U   53    PRO U   54          0        -2.14                     
CISPEP   3 THR V   63    PRO V   64          0       -10.81                     
CISPEP   4 TYR u   42    PRO u   43          0         4.33                     
CISPEP   5 ALA u   53    PRO u   54          0         5.30                     
CISPEP   6 THR v   63    PRO v   64          0        -8.08                     
SITE     1 AC1  9 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 AC1  9 HIS A 337  ASP A 342  ALA A 344  GLU C 354                    
SITE     3 AC1  9 ARG C 357                                                     
SITE     1 AC2  4 ASN A 181  HIS A 332  GLU A 333  LYS D 317                    
SITE     1 AC3  3 ASN A 338  PHE A 339  GLU C 354                               
SITE     1 AC4  7 GLU A 244  TYR A 246  HIS A 272  FE2 A 613                    
SITE     2 AC4  7 HIS D 214  TYR D 244  HIS D 268                               
SITE     1 AC5 22 PHE A 119  TYR A 147  PRO A 150  SER A 153                    
SITE     2 AC5 22 VAL A 157  MET A 183  PHE A 186  GLN A 187                    
SITE     3 AC5 22 ILE A 192  LEU A 193  HIS A 198  PHE A 206                    
SITE     4 AC5 22 ALA A 286  ALA A 287  ILE A 290  CLA A 606                    
SITE     5 AC5 22 PHO A 607  LEU D 182  LEU D 205  CLA D 402                    
SITE     6 AC5 22 CLA D 403  PHE T  17                                          
SITE     1 AC6 18 GLN A 199  VAL A 202  ALA A 203  PHE A 206                    
SITE     2 AC6 18 GLY A 207  LEU A 210  TRP A 278  CLA A 605                    
SITE     3 AC6 18 PL9 A 610  DGD C 518  PHE D 157  VAL D 175                    
SITE     4 AC6 18 ILE D 178  PHE D 179  LEU D 182  PHO D 401                    
SITE     5 AC6 18 CLA D 403  LMG J 101                                          
SITE     1 AC7 20 LEU A  41  ALA A  44  THR A  45  ILE A 115                    
SITE     2 AC7 20 PHE A 119  TYR A 126  GLN A 130  ALA A 146                    
SITE     3 AC7 20 TYR A 147  ALA A 149  PRO A 150  GLY A 175                    
SITE     4 AC7 20 PRO A 279  VAL A 283  CLA A 605  LEU D 205                    
SITE     5 AC7 20 LEU D 209  ILE D 213  TRP D 253  CLA D 402                    
SITE     1 AC8 18 ILE A  36  PRO A  39  THR A  40  PHE A  93                    
SITE     2 AC8 18 PRO A  95  ILE A  96  TRP A  97  LEU A 114                    
SITE     3 AC8 18 HIS A 118  LEU A 121  BCR A 609  LMG A 612                    
SITE     4 AC8 18 VAL I   8  TYR I   9  VAL I  11  VAL I  12                    
SITE     5 AC8 18 PHE I  15  VAL I  20                                          
SITE     1 AC9 12 VAL A  35  PRO A  39  LEU A  42  ALA A  43                    
SITE     2 AC9 12 CYS A  47  ILE A  50  ILE A  96  TRP A 105                    
SITE     3 AC9 12 LEU A 106  CLA A 608  PHE I  15  LEU I  18                    
SITE     1 AD1 20 PHE A 211  MET A 214  HIS A 215  LEU A 218                    
SITE     2 AD1 20 HIS A 252  PHE A 255  SER A 264  PHE A 265                    
SITE     3 AD1 20 LEU A 271  PHE A 274  CLA A 606  VAL D  30                    
SITE     4 AD1 20 PRO D  39  ALA D  41  TYR D  42  PHO D 401                    
SITE     5 AD1 20 ALA F  22  THR F  25  THR X  24  LEU X  28                    
SITE     1 AD2 13 GLY A 204  ASN A 267  SER A 270  PHE A 273                    
SITE     2 AD2 13 TRP A 278  GLY A 282  GLN C  28  ALA C  34                    
SITE     3 AD2 13 TRP C  36  CLA C 508  ARG D 233  LHG D 408                    
SITE     4 AD2 13 PHE K  37                                                     
SITE     1 AD3 13 PHE A  93  TRP A  97  GLU A  98  LEU A 121                    
SITE     2 AD3 13 SER A 124  PHE A 155  CLA A 608  LEU C 214                    
SITE     3 AD3 13 GLU C 221  TRP C 223  CLA C 505  LYS I   5                    
SITE     4 AD3 13 TYR I   9                                                     
SITE     1 AD4  5 HIS A 215  HIS A 272  BCT A 604  HIS D 214                    
SITE     2 AD4  5 HIS D 268                                                     
SITE     1 AD5  2 ASN B 438  GLU O 181                                          
SITE     1 AD6  5 PRO B 187  PHE B 190  CLA B 603  PHE H  41                    
SITE     2 AD6  5 BCR H 101                                                     
SITE     1 AD7 22 GLU B 184  TRP B 185  GLY B 189  PHE B 190                    
SITE     2 AD7 22 PRO B 192  GLY B 197  ALA B 200  HIS B 201                    
SITE     3 AD7 22 ALA B 204  ALA B 205  VAL B 208  PHE B 247                    
SITE     4 AD7 22 PHE B 250  CLA B 602  CLA B 604  CLA B 606                    
SITE     5 AD7 22 PHE H  41  ILE H  45  LEU H  46  TYR H  49                    
SITE     6 AD7 22 BCR H 101  DGD H 102                                          
SITE     1 AD8 18 LEU B  69  ALA B 146  LEU B 149  CYS B 150                    
SITE     2 AD8 18 PHE B 153  LEU B 158  VAL B 198  HIS B 201                    
SITE     3 AD8 18 HIS B 202  VAL B 252  THR B 262  CLA B 603                    
SITE     4 AD8 18 CLA B 605  CLA B 606  CLA B 607  MET H  35                    
SITE     5 AD8 18 PHE H  38  LEU H  39                                          
SITE     1 AD9 17 TRP B  33  PHE B  65  ARG B  68  LEU B 149                    
SITE     2 AD9 17 VAL B 245  ALA B 248  ALA B 249  VAL B 252                    
SITE     3 AD9 17 PHE B 451  HIS B 455  PHE B 458  ALA B 459                    
SITE     4 AD9 17 CLA B 604  CLA B 606  CLA B 608  CLA B 613                    
SITE     5 AD9 17 CLA B 616                                                     
SITE     1 AE1 20 THR B  27  ALA B  34  VAL B  62  MET B  66                    
SITE     2 AE1 20 LEU B  69  HIS B 100  LEU B 103  ALA B 146                    
SITE     3 AE1 20 GLY B 147  CYS B 150  ALA B 205  GLY B 209                    
SITE     4 AE1 20 CLA B 603  CLA B 604  CLA B 605  CLA B 607                    
SITE     5 AE1 20 CLA B 610  CLA B 611  CLA B 616  BCR B 620                    
SITE     1 AE2 16 VAL B  71  PHE B  90  TRP B  91  VAL B  96                    
SITE     2 AE2 16 VAL B 102  GLY B 152  PHE B 153  PHE B 156                    
SITE     3 AE2 16 HIS B 157  PHE B 162  GLY B 163  PRO B 164                    
SITE     4 AE2 16 CLA B 604  CLA B 606  BCR B 620  SQD a 612                    
SITE     1 AE3 18 TRP B  33  TYR B  40  GLN B  58  GLY B  59                    
SITE     2 AE3 18 MET B  60  PHE B  61  LEU B 324  THR B 327                    
SITE     3 AE3 18 GLY B 328  PRO B 329  TRP B 450  PHE B 451                    
SITE     4 AE3 18 CLA B 605  BCR B 619  LMG B 621  LHG B 622                    
SITE     5 AE3 18 PHE M  14  BCR t 101                                          
SITE     1 AE4 14 THR B 236  SER B 239  SER B 240  ALA B 243                    
SITE     2 AE4 14 PHE B 246  PHE B 463  HIS B 466  ILE B 467                    
SITE     3 AE4 14 CLA B 611  PHE D 120  LEU D 127  ILE D 150                    
SITE     4 AE4 14 LEU H  39  LEU H  43                                          
SITE     1 AE5 17 PHE B 139  LEU B 143  VAL B 208  ALA B 212                    
SITE     2 AE5 17 PHE B 215  HIS B 216  VAL B 219  PRO B 221                    
SITE     3 AE5 17 PRO B 222  LEU B 229  CLA B 606  CLA B 611                    
SITE     4 AE5 17 THR H  27  MET H  31  PHE H  34  LEU H  43                    
SITE     5 AE5 17 BCR H 101                                                     
SITE     1 AE6 14 LEU B 135  MET B 138  PHE B 139  HIS B 142                    
SITE     2 AE6 14 LEU B 143  LEU B 145  ALA B 146  VAL B 237                    
SITE     3 AE6 14 SER B 241  CLA B 606  CLA B 609  CLA B 610                    
SITE     4 AE6 14 CLA B 613  CLA B 616                                          
SITE     1 AE7 18 TYR B   6  ARG B   7  VAL B   8  HIS B   9                    
SITE     2 AE7 18 THR B  10  LEU B 238  LEU B 461  PHE B 462                    
SITE     3 AE7 18 PHE B 464  GLY B 465  TRP B 468  HIS B 469                    
SITE     4 AE7 18 ARG B 472  CLA B 613  CLA B 614  CLA B 615                    
SITE     5 AE7 18 BCR B 619  LHG B 622                                          
SITE     1 AE8 14 HIS B   9  LEU B  19  HIS B  23  HIS B  26                    
SITE     2 AE8 14 THR B  27  LEU B 238  SER B 241  VAL B 245                    
SITE     3 AE8 14 CLA B 605  CLA B 611  CLA B 612  CLA B 614                    
SITE     4 AE8 14 CLA B 615  CLA B 616                                          
SITE     1 AE9 12 HIS B   9  HIS B  26  VAL B  30  TRP B  33                    
SITE     2 AE9 12 PHE B 462  CLA B 612  CLA B 613  CLA B 615                    
SITE     3 AE9 12 BCR B 618  BCR B 619  LMG B 621  LHG B 622                    
SITE     1 AF1 16 VAL B   8  HIS B   9  VAL B  11  ALA B  22                    
SITE     2 AF1 16 LEU B  29  TRP B 115  CLA B 612  CLA B 613                    
SITE     3 AF1 16 CLA B 614  BCR B 618  LMG B 621  SQD B 623                    
SITE     4 AF1 16 GLN L   8  VAL L  10  PHE M  21  PHE t   8                    
SITE     1 AF2 12 HIS B  23  LEU B  24  MET B 138  HIS B 142                    
SITE     2 AF2 12 LEU B 145  CLA B 605  CLA B 606  CLA B 611                    
SITE     3 AF2 12 CLA B 613  CLA B 617  BCR B 620  LEU H  14                    
SITE     1 AF3 10 LEU B  24  ALA B 110  TRP B 113  HIS B 114                    
SITE     2 AF3 10 LEU B 120  CLA B 616  BCR B 620  THR H   5                    
SITE     3 AF3 10 LEU H   7  GLY H   8                                          
SITE     1 AF4 10 MET B  25  LEU B  29  TRP B 115  CLA B 614                    
SITE     2 AF4 10 CLA B 615  BCR B 619  LMG B 621  SQD B 623                    
SITE     3 AF4 10 PHE t  19  BCR t 101                                          
SITE     1 AF5 14 LEU B  29  GLY B  32  TRP B  33  SER B  36                    
SITE     2 AF5 14 ILE B 101  VAL B 102  SER B 104  GLY B 105                    
SITE     3 AF5 14 CLA B 608  CLA B 612  CLA B 614  BCR B 618                    
SITE     4 AF5 14 LMG B 621  BCR t 101                                          
SITE     1 AF6  9 LEU B 106  LEU B 109  TRP B 113  CLA B 606                    
SITE     2 AF6  9 CLA B 607  CLA B 616  CLA B 617  SQD a 612                    
SITE     3 AF6  9 PHE t  23                                                     
SITE     1 AF7 14 TYR B  40  THR B 327  GLY B 328  PRO B 329                    
SITE     2 AF7 14 ALA B 454  CLA B 608  CLA B 614  CLA B 615                    
SITE     3 AF7 14 BCR B 618  BCR B 619  LHG B 622  LHG L 101                    
SITE     4 AF7 14 ASN M   4  ALA M  10                                          
SITE     1 AF8 18 SER A 232  ASN A 234  TRP B   5  TYR B   6                    
SITE     2 AF8 18 ARG B   7  LEU B 461  PHE B 464  TRP B 468                    
SITE     3 AF8 18 CLA B 608  CLA B 612  CLA B 614  LMG B 621                    
SITE     4 AF8 18 TYR D 141  ILE D 144  TRP D 266  PHE D 269                    
SITE     5 AF8 18 THR D 277  LHG L 101                                          
SITE     1 AF9 14 ARG B  18  ALA B  28  LEU B  29  SER B 104                    
SITE     2 AF9 14 PHE B 108  TRP B 115  CLA B 615  BCR B 618                    
SITE     3 AF9 14 ARG L   7  ARG l  14  TYR l  18  LEU m  16                    
SITE     4 AF9 14 PHE t  19  PHE t  23                                          
SITE     1 AG1 16 LEU C  95  LEU C 168  GLY C 171  ALA C 172                    
SITE     2 AG1 16 LEU C 175  VAL C 233  HIS C 237  ILE C 240                    
SITE     3 AG1 16 MET C 282  VAL C 296  TYR C 297  CLA C 502                    
SITE     4 AG1 16 CLA C 503  CLA C 506  CLA C 507  BCR C 515                    
SITE     1 AG2 16 HIS C  91  GLY C 171  LYS C 178  PHE C 182                    
SITE     2 AG2 16 LEU C 279  MET C 282  ALA C 286  VAL C 290                    
SITE     3 AG2 16 TYR C 297  HIS C 430  LEU C 433  PHE C 437                    
SITE     4 AG2 16 CLA C 501  CLA C 503  CLA C 504  CLA C 510                    
SITE     1 AG3 13 ILE C  60  VAL C  61  THR C  68  LEU C  88                    
SITE     2 AG3 13 HIS C  91  LEU C  95  VAL C 114  HIS C 118                    
SITE     3 AG3 13 CLA C 501  CLA C 502  CLA C 510  CLA C 512                    
SITE     4 AG3 13 LMG C 520                                                     
SITE     1 AG4 18 TRP C  63  MET C  67  PHE C  70  GLN C  84                    
SITE     2 AG4 18 GLY C  85  ILE C  87  TRP C 425  SER C 429                    
SITE     3 AG4 18 PHE C 436  CLA C 502  CLA C 508  CLA C 510                    
SITE     4 AG4 18 DGD C 517  DGD C 518  LMG C 519  LHG D 408                    
SITE     5 AG4 18 PRO K  26  VAL K  30                                          
SITE     1 AG5 16 PHE A  33  MET A 127  TRP A 131  LMG A 612                    
SITE     2 AG5 16 PHE C 264  SER C 273  TYR C 274  HIS C 441                    
SITE     3 AG5 16 LEU C 442  ALA C 445  ARG C 449  CLA C 507                    
SITE     4 AG5 16 BCR C 515  VAL I  12  VAL I  16  PHE I  23                    
SITE     1 AG6 14 LEU C 161  LEU C 165  LEU C 213  ILE C 243                    
SITE     2 AG6 14 GLY C 247  TRP C 250  HIS C 251  THR C 254                    
SITE     3 AG6 14 THR C 255  PHE C 257  TRP C 259  PHE C 264                    
SITE     4 AG6 14 CLA C 501  CLA C 507                                          
SITE     1 AG7 16 MET C 157  THR C 158  LEU C 161  HIS C 164                    
SITE     2 AG7 16 LEU C 168  CYS C 244  PHE C 264  TRP C 266                    
SITE     3 AG7 16 TYR C 271  TYR C 274  SER C 275  CLA C 501                    
SITE     4 AG7 16 CLA C 505  CLA C 506  CLA C 509  BCR C 515                    
SITE     1 AG8 23 SQD A 611  TRP C  36  ALA C  37  GLY C  38                    
SITE     2 AG8 23 ASN C  39  ALA C  40  GLU C 269  LEU C 272                    
SITE     3 AG8 23 LEU C 276  PHE C 436  PHE C 437  GLY C 440                    
SITE     4 AG8 23 TRP C 443  HIS C 444  ARG C 447  CLA C 504                    
SITE     5 AG8 23 CLA C 509  CLA C 510  CLA C 511  DGD C 518                    
SITE     6 AG8 23 LMG C 519  LHG D 408  VAL K  30                               
SITE     1 AG9 20 ASN C  39  LEU C  49  ALA C  52  HIS C  53                    
SITE     2 AG9 20 HIS C  56  TYR C 149  MET C 157  ILE C 160                    
SITE     3 AG9 20 HIS C 164  GLY C 268  GLU C 269  TYR C 271                    
SITE     4 AG9 20 LEU C 272  SER C 275  LEU C 279  CLA C 507                    
SITE     5 AG9 20 CLA C 508  CLA C 510  CLA C 511  CLA C 512                    
SITE     1 AH1 16 ASN C  39  HIS C  56  LEU C  59  ILE C  60                    
SITE     2 AH1 16 TRP C  63  LEU C 279  PHE C 436  PHE C 437                    
SITE     3 AH1 16 CLA C 502  CLA C 503  CLA C 504  CLA C 508                    
SITE     4 AH1 16 CLA C 509  LHG D 408  PRO K  29  LEU K  33                    
SITE     1 AH2 28 THR C  24  ARG C  26  TRP C  35  GLY C  38                    
SITE     2 AH2 28 ASN C  39  ARG C  41  LEU C  42  LEU C  45                    
SITE     3 AH2 28 LYS C  48  ALA C  52  ALA C 123  PHE C 127                    
SITE     4 AH2 28 ILE C 134  CLA C 508  CLA C 509  BCR C 521                    
SITE     5 AH2 28 LEU K  33  ALA K  36  TRP K  39  GLN K  40                    
SITE     6 AH2 28 LEU Y  39  ASN Y  45  LEU Y  46  MET Z  19                    
SITE     7 AH2 28 VAL Z  20  VAL Z  23  PRO Z  24  ALA Z  28                    
SITE     1 AH3 11 HIS C  53  PHE C 146  PHE C 147  PHE C 163                    
SITE     2 AH3 11 HIS C 164  VAL C 167  ILE C 170  GLY C 171                    
SITE     3 AH3 11 CLA C 503  CLA C 509  CLA C 513                               
SITE     1 AH4  9 LEU C  50  GLY C 128  TYR C 131  HIS C 132                    
SITE     2 AH4  9 TYR C 143  PHE C 147  CLA C 512  BCR C 514                    
SITE     3 AH4  9 LMG Z 101                                                     
SITE     1 AH5 11 PHE C 112  VAL C 116  SER C 121  VAL C 124                    
SITE     2 AH5 11 LEU C 125  CLA C 513  LMG C 520  TYR K  15                    
SITE     3 AH5 11 VAL Z  51  GLY Z  55  ASN Z  58                               
SITE     1 AH6 13 ILE C 209  PHE C 210  LEU C 213  VAL C 227                    
SITE     2 AH6 13 GLY C 236  HIS C 237  ILE C 240  CLA C 501                    
SITE     3 AH6 13 CLA C 505  CLA C 507  VAL I  20  PHE I  23                    
SITE     4 AH6 13 LEU I  24                                                     
SITE     1 AH7 22 LEU A  91  SER A 148  PRO C 217  PHE C 218                    
SITE     2 AH7 22 GLY C 219  GLY C 220  GLU C 221  GLY C 222                    
SITE     3 AH7 22 TRP C 223  VAL C 225  SER C 226  VAL C 227                    
SITE     4 AH7 22 ASN C 228  CYS C 288  PHE C 292  ASN C 293                    
SITE     5 AH7 22 ASN C 294  THR C 295  ASP C 360  PHE C 361                    
SITE     6 AH7 22 ARG C 362  LEU C 438                                          
SITE     1 AH8 17 HIS A 195  PHE A 197  LEU A 297  GLU C  83                    
SITE     2 AH8 17 GLN C  84  GLY C  85  SER C 406  ASN C 418                    
SITE     3 AH8 17 PHE C 419  VAL C 420  TRP C 425  SER C 429                    
SITE     4 AH8 17 CLA C 504  DGD C 518  LMG C 519  PHE J  29                    
SITE     5 AH8 17 TYR J  33                                                     
SITE     1 AH9 25 GLN A 199  LEU A 200  ALA A 203  ASN A 301                    
SITE     2 AH9 25 PHE A 302  SER A 305  CLA A 606  ASN C 405                    
SITE     3 AH9 25 VAL C 407  ASN C 415  SER C 416  VAL C 417                    
SITE     4 AH9 25 ASN C 418  CLA C 504  CLA C 508  DGD C 517                    
SITE     5 AH9 25 ASN D  72  PHE J  29  ALA J  32  TYR J  33                    
SITE     6 AH9 25 GLY J  37  SER J  38  SER J  39  LEU J  40                    
SITE     7 AH9 25 LMG J 101                                                     
SITE     1 AI1  9 PHE C  70  HIS C  74  GLN C  84  CLA C 504                    
SITE     2 AI1  9 CLA C 508  DGD C 517  ASP K  23  VAL K  27                    
SITE     3 AI1  9 ILE Y  25                                                     
SITE     1 AI2  8 TRP C  97  ASP C 107  VAL C 117  SER C 121                    
SITE     2 AI2  8 CLA C 503  BCR C 514  PHE Z  59  VAL Z  62                    
SITE     1 AI3 17 ALA C  55  GLY C  58  LEU C  59  PHE C  62                    
SITE     2 AI3 17 ILE C 120  SER C 122  ALA C 123  GLY C 126                    
SITE     3 AI3 17 CLA C 511  TYR K  15  PHE K  32  ALA K  36                    
SITE     4 AI3 17 TRP K  39  BCR K 101  LEU Z   9  SER Z  16                    
SITE     5 AI3 17 TRP Z  47                                                     
SITE     1 AI4 21 PHE A 206  ALA A 209  LEU A 210  MET A 214                    
SITE     2 AI4 21 PHE A 255  CLA A 606  PL9 A 610  ALA D  41                    
SITE     3 AI4 21 TRP D  48  ILE D 114  GLY D 118  GLY D 121                    
SITE     4 AI4 21 LEU D 122  PHE D 125  GLN D 129  ASN D 142                    
SITE     5 AI4 21 PHE D 146  PRO D 149  PHE D 153  LEU D 279                    
SITE     6 AI4 21 CLA D 403                                                     
SITE     1 AI5 16 VAL A 157  MET A 172  ILE A 176  THR A 179                    
SITE     2 AI5 16 MET A 183  CLA A 605  PHO A 607  MET D 198                    
SITE     3 AI5 16 VAL D 201  ALA D 202  LEU D 205  GLY D 206                    
SITE     4 AI5 16 CLA D 403  PL9 D 405  LHG L 101  SQD b 601                    
SITE     1 AI6 21 MET A 183  PHE A 206  CLA A 605  CLA A 606                    
SITE     2 AI6 21 LEU D  45  LEU D 122  PRO D 149  VAL D 152                    
SITE     3 AI6 21 VAL D 156  LEU D 182  PHE D 185  GLN D 186                    
SITE     4 AI6 21 TRP D 191  HIS D 197  VAL D 201  VAL D 204                    
SITE     5 AI6 21 SER D 282  ALA D 283  VAL D 286  PHO D 401                    
SITE     6 AI6 21 CLA D 402                                                     
SITE     1 AI7 18 ILE D  35  PRO D  39  CYS D  40  LEU D  43                    
SITE     2 AI7 18 LEU D  89  LEU D  90  LEU D  91  LEU D  92                    
SITE     3 AI7 18 TRP D  93  TRP D 104  THR D 112  PHE D 113                    
SITE     4 AI7 18 HIS D 117  BCR F 101  LEU H  39  GLY X  13                    
SITE     5 AI7 18 LEU X  14  LEU X  21                                          
SITE     1 AI8 22 PHE A  52  ILE A  53  MET D 198  MET D 199                    
SITE     2 AI8 22 ALA D 202  LEU D 209  HIS D 214  THR D 217                    
SITE     3 AI8 22 TRP D 253  ALA D 260  PHE D 261  LEU D 267                    
SITE     4 AI8 22 VAL D 274  GLY D 278  CLA D 402  LHG D 407                    
SITE     5 AI8 22 LEU L  23  LEU L  27  LEU L  29  LEU L  30                    
SITE     6 AI8 22 LHG L 101  PHE T  10                                          
SITE     1 AI9  6 GLY D  99  ASP D 100  THR D 102  PHE E  37                    
SITE     2 AI9  6 ASP E  45  BCR F 101                                          
SITE     1 AJ1 21 MET A  37  ARG A 129  ILE D 256  PHE D 257                    
SITE     2 AJ1 21 ILE D 259  ALA D 260  PHE D 261  SER D 262                    
SITE     3 AJ1 21 ASN D 263  TRP D 266  PHE D 270  PL9 D 405                    
SITE     4 AJ1 21 ASN L  13  THR L  15  SER L  16  TYR L  18                    
SITE     5 AJ1 21 LEU L  19  LHG L 101  PHE T  10  PHE T  17                    
SITE     6 AJ1 21 ALA T  20                                                     
SITE     1 AJ2 17 ARG A 140  TRP A 142  PHE A 273  SQD A 611                    
SITE     2 AJ2 17 PHE C  33  TRP C  36  TRP C 443  ARG C 447                    
SITE     3 AJ2 17 CLA C 504  CLA C 508  CLA C 510  GLU D 219                    
SITE     4 AJ2 17 ASN D 220  ALA D 229  SER D 230  THR D 231                    
SITE     5 AJ2 17 PHE D 232                                                     
SITE     1 AJ3 12 LEU A 258  PHE A 260  TYR A 262  PHE D  27                    
SITE     2 AJ3 12 ARG D 128  THR E   4  THR E   5  GLU E   7                    
SITE     3 AJ3 12 PRO E   9  PHE E  10  SER E  11  ARG F  19                    
SITE     1 AJ4 15 PHE E  10  ARG E  18  TYR E  19  ILE E  22                    
SITE     2 AJ4 15 HIS E  23  THR E  26  ILE E  27  LEU E  30                    
SITE     3 AJ4 15 ILE F  15  ARG F  19  TRP F  20  VAL F  23                    
SITE     4 AJ4 15 HIS F  24  ALA F  27  ILE F  31                               
SITE     1 AJ5 14 LEU D  43  GLY D  46  GLY D  47  LEU D  49                    
SITE     2 AJ5 14 PHE D 101  PHE D 113  CLA D 404  DGD D 406                    
SITE     3 AJ5 14 PRO F  29  THR F  30  PHE F  33  LEU F  34                    
SITE     4 AJ5 14 VAL J  21  LMG J 101                                          
SITE     1 AJ6  2 ARG F  45  GLU V  23                                          
SITE     1 AJ7 10 CLA B 602  CLA B 603  CLA B 610  MET H  31                    
SITE     2 AJ7 10 MET H  35  LEU H  37  PHE H  38  VAL H  40                    
SITE     3 AJ7 10 PHE H  41  ILE H  44                                          
SITE     1 AJ8 19 TYR B 193  PHE B 250  GLY B 254  TYR B 258                    
SITE     2 AJ8 19 GLN B 274  SER B 277  TYR B 279  ALA B 456                    
SITE     3 AJ8 19 PHE B 463  CLA B 603  HIS D  87  ILE D 159                    
SITE     4 AJ8 19 LEU D 162  LEU H  46  TYR H  49  ASN H  50                    
SITE     5 AJ8 19 VAL H  60  SER H  61  TRP H  62                               
SITE     1 AJ9 17 CLA A 606  DGD C 518  TYR D  67  GLY D  70                    
SITE     2 AJ9 17 CYS D  71  ASN D  72  PHE D  73  THR F  30                    
SITE     3 AJ9 17 ILE F  37  MET F  40  GLN F  41  BCR F 101                    
SITE     4 AJ9 17 PHE J  28  GLY J  31  ALA J  32  LEU J  36                    
SITE     5 AJ9 17  MG J 102                                                     
SITE     1 AK1  5 GLY J  31  ALA J  34  GLY J  35  LEU J  36                    
SITE     2 AK1  5 LMG J 101                                                     
SITE     1 AK2 14 PHE C  62  BCR C 521  ALA J  14  THR J  15                    
SITE     2 AK2 14 GLY J  18  MET J  19  LEU K  31  PHE K  32                    
SITE     3 AK2 14 ALA K  34  PRO Y  33  VAL Z  13  SER Z  16                    
SITE     4 AK2 14 PHE Z  17  VAL Z  20                                          
SITE     1 AK3 21 SER A 232  ASN A 234  PRO B   4  TRP B   5                    
SITE     2 AK3 21 TYR B   6  LMG B 621  LHG B 622  TRP D 266                    
SITE     3 AK3 21 PHE D 273  CLA D 402  PL9 D 405  LHG D 407                    
SITE     4 AK3 21 GLU L  11  LEU L  12  ASN L  13  SER L  16                    
SITE     5 AK3 21 LEU L  19  GLY L  20  LEU L  22  LEU L  23                    
SITE     6 AK3 21 PHE M  21                                                     
SITE     1 AK4  3 THR O 138  ASN O 200  VAL O 201                               
SITE     1 AK5 17 LEU A  28  PHE T   8  ALA T  11  CYS T  12                    
SITE     2 AK5 17 ALA T  15  PHE T  18  ILE T  21  PHE T  22                    
SITE     3 AK5 17 TRP b  33  SER b  36  MET b  37  TYR b  40                    
SITE     4 AK5 17 LEU b 109  SQD b 601  CLA b 610  BCR b 620                    
SITE     5 AK5 17 BCR b 621                                                     
SITE     1 AK6 18 CYS V  37  CYS V  40  HIS V  41  THR V  46                    
SITE     2 AK6 18 THR V  48  LEU V  52  ASP V  53  LEU V  54                    
SITE     3 AK6 18 THR V  58  LEU V  59  ALA V  62  LEU V  72                    
SITE     4 AK6 18 TYR V  75  MET V  76  THR V  81  TYR V  82                    
SITE     5 AK6 18 HIS V  92  PRO V  93                                          
SITE     1 AK7 10 TRP D  21  ARG D  24  ARG D  26  PHE F  16                    
SITE     2 AK7 10 THR F  17  VAL F  18  LEU X  23  VAL X  27                    
SITE     3 AK7 10 ILE X  31  ASP X  35                                          
SITE     1 AK8  6 CLA C 513  TYR Z  27  TRP Z  33  LYS Z  37                    
SITE     2 AK8  6 PHE Z  41  TRP Z  47                                          
SITE     1 AK9 10 ASP a  61  ASP a 170  GLU a 189  HIS a 332                    
SITE     2 AK9 10 GLU a 333  HIS a 337  ASP a 342  ALA a 344                    
SITE     3 AK9 10 GLU c 354  ARG c 357                                          
SITE     1 AL1  5 ASN a 181  HIS a 332  GLU a 333  LYS d 317                    
SITE     2 AL1  5 LEU d 321                                                     
SITE     1 AL2  7 GLU a 244  TYR a 246  HIS a 272  FE2 a 615                    
SITE     2 AL2  7 HIS d 214  TYR d 244  HIS d 268                               
SITE     1 AL3 19 TYR a 147  PRO a 150  SER a 153  VAL a 157                    
SITE     2 AL3 19 MET a 183  PHE a 186  GLN a 187  ILE a 192                    
SITE     3 AL3 19 LEU a 193  HIS a 198  ALA a 286  ALA a 287                    
SITE     4 AL3 19 ILE a 290  CLA a 605  PHO a 606  CLA a 613                    
SITE     5 AL3 19 LEU d 205  CLA d 402  PHE t  17                               
SITE     1 AL4 17 GLN a 199  VAL a 202  ALA a 203  PHE a 206                    
SITE     2 AL4 17 GLY a 207  LEU a 210  TRP a 278  CLA a 604                    
SITE     3 AL4 17 PL9 a 609  PHE d 157  VAL d 175  ILE d 178                    
SITE     4 AL4 17 PHE d 179  LEU d 182  PHO d 401  CLA d 402                    
SITE     5 AL4 17 LMG j 101                                                     
SITE     1 AL5 18 LEU a  41  ALA a  44  THR a  45  PHE a  48                    
SITE     2 AL5 18 TYR a 126  GLN a 130  ALA a 146  TYR a 147                    
SITE     3 AL5 18 PRO a 150  VAL a 283  CLA a 604  CLA a 613                    
SITE     4 AL5 18 LEU d 205  ALA d 208  LEU d 209  ILE d 213                    
SITE     5 AL5 18 TRP d 253  PHE d 257                                          
SITE     1 AL6 17 ILE a  36  PRO a  39  THR a  40  PHE a  93                    
SITE     2 AL6 17 PRO a  95  ILE a  96  TRP a  97  LEU a 114                    
SITE     3 AL6 17 HIS a 118  LEU a 121  BCR a 608  LMG a 611                    
SITE     4 AL6 17 VAL i   8  TYR i   9  VAL i  11  VAL i  12                    
SITE     5 AL6 17 PHE i  15                                                     
SITE     1 AL7  9 PRO a  39  LEU a  42  ALA a  43  CYS a  47                    
SITE     2 AL7  9 ILE a  50  TRP a 105  LEU a 106  CLA a 607                    
SITE     3 AL7  9 PHE i  15                                                     
SITE     1 AL8 20 PHE a 211  MET a 214  HIS a 215  LEU a 218                    
SITE     2 AL8 20 PHE a 255  SER a 264  PHE a 265  LEU a 271                    
SITE     3 AL8 20 PHE a 274  CLA a 605  VAL d  30  PHE d  38                    
SITE     4 AL8 20 PRO d  39  ALA d  41  TYR d  42  PHO d 401                    
SITE     5 AL8 20 THR f  25  LEU f  26  THR x  24  LEU x  28                    
SITE     1 AL9 16 GLY a 204  ASN a 267  SER a 270  PHE a 273                    
SITE     2 AL9 16 PHE a 274  TRP a 278  VAL a 281  GLY a 282                    
SITE     3 AL9 16 LHG a 614  GLN c  28  ALA c  34  TRP c  36                    
SITE     4 AL9 16 CLA c 509  PHE d 232  ARG d 233  PHE k  37                    
SITE     1 AM1 15 PHE a  93  TRP a  97  GLU a  98  PHE a 117                    
SITE     2 AM1 15 LEU a 121  SER a 124  PHE a 155  CLA a 607                    
SITE     3 AM1 15 LEU c 214  GLU c 221  TRP c 223  PHE c 284                    
SITE     4 AM1 15 DGD c 517  LYS i   5  TYR i   9                               
SITE     1 AM2 12 VAL B 102  TRP B 113  TYR B 117  CLA B 607                    
SITE     2 AM2 12 BCR B 620  TRP a  20  ASN a  26  ARG a  27                    
SITE     3 AM2 12 LEU a  28  ILE a  38  CLA a 613  BCR t 101                    
SITE     1 AM3 17 VAL a 157  MET a 172  ILE a 176  THR a 179                    
SITE     2 AM3 17 PHE a 180  MET a 183  CLA a 604  PHO a 606                    
SITE     3 AM3 17 SQD a 612  MET d 198  VAL d 201  ALA d 202                    
SITE     4 AM3 17 LEU d 205  GLY d 206  CLA d 402  PL9 d 404                    
SITE     5 AM3 17 LHG l 101                                                     
SITE     1 AM4 17 ARG a 140  TRP a 142  PHE a 273  SQD a 610                    
SITE     2 AM4 17 TRP c  36  TRP c 443  ARG c 447  CLA c 505                    
SITE     3 AM4 17 CLA c 509  CLA c 511  DGD c 519  GLU d 219                    
SITE     4 AM4 17 ASN d 220  ALA d 229  SER d 230  THR d 231                    
SITE     5 AM4 17 PHE d 232                                                     
SITE     1 AM5  5 HIS a 215  HIS a 272  BCT a 603  HIS d 214                    
SITE     2 AM5  5 HIS d 268                                                     
SITE     1 AM6 10 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 AM6 10 CLA D 402  BCR T 101  TRP b 113  TYR b 117                    
SITE     3 AM6 10 CLA b 609  BCR b 622                                          
SITE     1 AM7 14 ARG L  14  TYR L  18  LEU M  16  PHE T  19                    
SITE     2 AM7 14 PHE T  23  ARG b  18  ALA b  28  LEU b  29                    
SITE     3 AM7 14 SER b 104  PHE b 108  TRP b 115  CLA b 617                    
SITE     4 AM7 14 BCR b 620  ARG l   7                                          
SITE     1 AM8  1 ASN b 438                                                     
SITE     1 AM9  5 TRP b 185  PRO b 187  PHE b 190  CLA b 605                    
SITE     2 AM9  5 BCR h 101                                                     
SITE     1 AN1 18 TRP b 185  GLY b 189  PHE b 190  GLY b 197                    
SITE     2 AN1 18 ALA b 200  HIS b 201  ALA b 204  ALA b 205                    
SITE     3 AN1 18 VAL b 208  PHE b 247  PHE b 250  CLA b 604                    
SITE     4 AN1 18 CLA b 606  CLA b 608  PHE h  38  PHE h  41                    
SITE     5 AN1 18 ILE h  45  BCR h 101                                          
SITE     1 AN2 16 ARG b  68  LEU b  69  ALA b 146  LEU b 149                    
SITE     2 AN2 16 CYS b 150  PHE b 153  HIS b 201  HIS b 202                    
SITE     3 AN2 16 VAL b 252  THR b 262  CLA b 605  CLA b 607                    
SITE     4 AN2 16 CLA b 608  CLA b 609  MET h  35  PHE h  38                    
SITE     1 AN3 17 TRP b  33  PHE b  65  ARG b  68  LEU b 149                    
SITE     2 AN3 17 VAL b 245  ALA b 248  ALA b 249  VAL b 252                    
SITE     3 AN3 17 PHE b 451  HIS b 455  PHE b 458  CLA b 606                    
SITE     4 AN3 17 CLA b 608  CLA b 610  CLA b 615  CLA b 616                    
SITE     5 AN3 17 CLA b 618                                                     
SITE     1 AN4 22 THR b  27  VAL b  30  ALA b  34  VAL b  62                    
SITE     2 AN4 22 PHE b  65  MET b  66  LEU b  69  HIS b 100                    
SITE     3 AN4 22 LEU b 103  ALA b 146  GLY b 147  CYS b 150                    
SITE     4 AN4 22 ALA b 205  GLY b 209  CLA b 605  CLA b 606                    
SITE     5 AN4 22 CLA b 607  CLA b 609  CLA b 612  CLA b 613                    
SITE     6 AN4 22 CLA b 618  BCR b 622                                          
SITE     1 AN5 16 PHE b  90  TRP b  91  VAL b  96  VAL b 102                    
SITE     2 AN5 16 LEU b 106  GLY b 152  PHE b 153  PHE b 156                    
SITE     3 AN5 16 HIS b 157  PHE b 162  GLY b 163  PRO b 164                    
SITE     4 AN5 16 SQD b 601  CLA b 606  CLA b 608  BCR b 622                    
SITE     1 AN6 18 BCR T 101  TRP b  33  TYR b  40  GLN b  58                    
SITE     2 AN6 18 GLY b  59  MET b  60  PHE b  61  LEU b 324                    
SITE     3 AN6 18 THR b 327  GLY b 328  PRO b 329  TRP b 450                    
SITE     4 AN6 18 CLA b 607  BCR b 620  BCR b 621  LMG b 623                    
SITE     5 AN6 18 LHG b 624  PHE m  14                                          
SITE     1 AN7 12 THR b 236  SER b 239  SER b 240  ALA b 243                    
SITE     2 AN7 12 PHE b 463  HIS b 466  ILE b 467  GLY b 470                    
SITE     3 AN7 12 CLA b 613  ILE d 150  LEU h  39  LEU h  43                    
SITE     1 AN8 19 PHE b 139  LEU b 143  VAL b 208  ALA b 212                    
SITE     2 AN8 19 PHE b 215  HIS b 216  VAL b 219  ARG b 220                    
SITE     3 AN8 19 PRO b 221  PRO b 222  LEU b 229  CLA b 608                    
SITE     4 AN8 19 CLA b 613  THR h  27  MET h  31  PHE h  34                    
SITE     5 AN8 19 LEU h  42  LEU h  43  BCR h 101                               
SITE     1 AN9 15 LEU b 135  MET b 138  PHE b 139  HIS b 142                    
SITE     2 AN9 15 LEU b 143  ALA b 146  MET b 231  VAL b 237                    
SITE     3 AN9 15 SER b 240  SER b 241  CLA b 608  CLA b 611                    
SITE     4 AN9 15 CLA b 612  CLA b 615  CLA b 618                               
SITE     1 AO1 18 TYR b   6  ARG b   7  VAL b   8  HIS b   9                    
SITE     2 AO1 18 THR b  10  LEU b 238  ILE b 242  LEU b 461                    
SITE     3 AO1 18 PHE b 462  GLY b 465  TRP b 468  HIS b 469                    
SITE     4 AO1 18 ARG b 472  CLA b 615  CLA b 616  CLA b 617                    
SITE     5 AO1 18 LHG b 624  PHE m  21                                          
SITE     1 AO2 15 HIS b   9  LEU b  19  HIS b  23  HIS b  26                    
SITE     2 AO2 15 THR b  27  ILE b 234  VAL b 237  LEU b 238                    
SITE     3 AO2 15 SER b 241  CLA b 607  CLA b 613  CLA b 614                    
SITE     4 AO2 15 CLA b 616  CLA b 617  CLA b 618                               
SITE     1 AO3 11 HIS b   9  HIS b  26  VAL b  30  TRP b  33                    
SITE     2 AO3 11 PHE b 462  CLA b 607  CLA b 614  CLA b 615                    
SITE     3 AO3 11 CLA b 617  BCR b 621  LMG b 623                               
SITE     1 AO4 16 PHE T   8  VAL b   8  HIS b   9  VAL b  11                    
SITE     2 AO4 16 ALA b  22  LEU b  29  TRP b 115  SQD b 602                    
SITE     3 AO4 16 CLA b 614  CLA b 615  CLA b 616  BCR b 620                    
SITE     4 AO4 16 LMG b 623  GLN l   8  VAL l  10  PHE m  21                    
SITE     1 AO5 14 HIS b  23  MET b 138  HIS b 142  LEU b 145                    
SITE     2 AO5 14 CLA b 607  CLA b 608  CLA b 613  CLA b 615                    
SITE     3 AO5 14 CLA b 619  BCR b 622  LEU h   7  LEU h  11                    
SITE     4 AO5 14 LEU h  14  ASN h  15                                          
SITE     1 AO6 10 LEU b  24  ALA b 110  TRP b 113  HIS b 114                    
SITE     2 AO6 10 LEU b 120  CLA b 618  BCR b 622  THR h   5                    
SITE     3 AO6 10 LEU h   7  GLY h   8                                          
SITE     1 AO7 13 PHE T  19  BCR T 101  MET b  25  LEU b  29                    
SITE     2 AO7 13 ALA b 111  CYS b 112  TRP b 115  SQD b 602                    
SITE     3 AO7 13 CLA b 610  CLA b 617  BCR b 621  LMG b 623                    
SITE     4 AO7 13 ALA m  10                                                     
SITE     1 AO8 13 BCR T 101  LEU b  29  GLY b  32  TRP b  33                    
SITE     2 AO8 13 SER b  36  ILE b 101  VAL b 102  SER b 104                    
SITE     3 AO8 13 GLY b 105  CLA b 610  CLA b 616  BCR b 620                    
SITE     4 AO8 13 LMG b 623                                                     
SITE     1 AO9  7 LEU b 106  TRP b 113  SQD b 601  CLA b 608                    
SITE     2 AO9  7 CLA b 609  CLA b 618  CLA b 619                               
SITE     1 AP1 13 TYR b  40  THR b 327  GLY b 328  PRO b 329                    
SITE     2 AP1 13 LYS b 332  CLA b 610  CLA b 616  CLA b 617                    
SITE     3 AP1 13 BCR b 620  BCR b 621  ILE d 284  PHE l  35                    
SITE     4 AP1 13 ASN m   4                                                     
SITE     1 AP2 17 SER a 232  ASN a 234  TRP b   5  TYR b   6                    
SITE     2 AP2 17 ARG b   7  LEU b 461  PHE b 464  TRP b 468                    
SITE     3 AP2 17 CLA b 610  CLA b 614  TYR d 141  ILE d 144                    
SITE     4 AP2 17 TRP d 266  PHE d 269  THR d 277  LEU l  23                    
SITE     5 AP2 17 LHG l 101                                                     
SITE     1 AP3  4 ASN a 338  PHE a 339  GLY c 353  GLU c 354                    
SITE     1 AP4 17 LEU c  95  LEU c 168  GLY c 171  ALA c 172                    
SITE     2 AP4 17 LEU c 175  VAL c 233  HIS c 237  ILE c 240                    
SITE     3 AP4 17 MET c 282  ILE c 285  PHE c 289  VAL c 296                    
SITE     4 AP4 17 TYR c 297  CLA c 503  CLA c 504  CLA c 507                    
SITE     5 AP4 17 BCR c 516                                                     
SITE     1 AP5 16 TRP c  63  HIS c  91  LYS c 178  PHE c 182                    
SITE     2 AP5 16 LEU c 279  MET c 282  ALA c 286  TYR c 297                    
SITE     3 AP5 16 LEU c 426  HIS c 430  LEU c 433  PHE c 437                    
SITE     4 AP5 16 CLA c 502  CLA c 504  CLA c 505  CLA c 511                    
SITE     1 AP6 13 ILE c  60  VAL c  61  THR c  68  LEU c  88                    
SITE     2 AP6 13 HIS c  91  LEU c  95  VAL c 114  HIS c 118                    
SITE     3 AP6 13 CLA c 502  CLA c 503  CLA c 511  CLA c 513                    
SITE     4 AP6 13 LMG c 521                                                     
SITE     1 AP7 17 LHG a 614  TRP c  63  PHE c  70  GLN c  84                    
SITE     2 AP7 17 GLY c  85  ILE c  87  TRP c 425  SER c 429                    
SITE     3 AP7 17 PHE c 436  CLA c 503  CLA c 509  CLA c 511                    
SITE     4 AP7 17 DGD c 518  DGD c 519  LMG c 520  PRO k  26                    
SITE     5 AP7 17 VAL k  30                                                     
SITE     1 AP8 16 PHE a  33  MET a 127  TRP a 131  PHE c 264                    
SITE     2 AP8 16 SER c 273  TYR c 274  GLY c 277  ALA c 278                    
SITE     3 AP8 16 HIS c 441  LEU c 442  ALA c 445  ARG c 449                    
SITE     4 AP8 16 CLA c 508  BCR c 516  VAL i  16  PHE i  23                    
SITE     1 AP9 16 LEU c 161  LEU c 165  LEU c 213  ILE c 243                    
SITE     2 AP9 16 GLY c 247  TRP c 250  HIS c 251  THR c 254                    
SITE     3 AP9 16 THR c 255  PHE c 257  TRP c 259  PHE c 264                    
SITE     4 AP9 16 CLA c 502  CLA c 508  BCR c 516  DGD c 517                    
SITE     1 AQ1 15 MET c 157  THR c 158  LEU c 161  HIS c 164                    
SITE     2 AQ1 15 LEU c 168  TRP c 259  PHE c 264  TRP c 266                    
SITE     3 AQ1 15 TYR c 271  TYR c 274  SER c 275  CLA c 506                    
SITE     4 AQ1 15 CLA c 507  CLA c 510  BCR c 516                               
SITE     1 AQ2 21 SQD a 610  LHG a 614  TRP c  36  ALA c  37                    
SITE     2 AQ2 21 GLY c  38  ASN c  39  GLU c 269  LEU c 272                    
SITE     3 AQ2 21 LEU c 276  PHE c 436  PHE c 437  GLY c 440                    
SITE     4 AQ2 21 TRP c 443  HIS c 444  ARG c 447  CLA c 505                    
SITE     5 AQ2 21 CLA c 510  CLA c 511  CLA c 512  DGD c 519                    
SITE     6 AQ2 21 LMG c 520                                                     
SITE     1 AQ3 21 ASN c  39  LEU c  49  ALA c  52  HIS c  53                    
SITE     2 AQ3 21 HIS c  56  TYR c 149  MET c 157  ILE c 160                    
SITE     3 AQ3 21 HIS c 164  LEU c 168  GLY c 268  GLU c 269                    
SITE     4 AQ3 21 TYR c 271  LEU c 272  SER c 275  LEU c 279                    
SITE     5 AQ3 21 CLA c 508  CLA c 509  CLA c 511  CLA c 512                    
SITE     6 AQ3 21 CLA c 513                                                     
SITE     1 AQ4 17 LHG a 614  ASN c  39  HIS c  56  LEU c  59                    
SITE     2 AQ4 17 ILE c  60  TRP c  63  LEU c 279  PHE c 436                    
SITE     3 AQ4 17 PHE c 437  CLA c 503  CLA c 504  CLA c 505                    
SITE     4 AQ4 17 CLA c 509  CLA c 510  PRO k  29  VAL k  30                    
SITE     5 AQ4 17 LEU k  33                                                     
SITE     1 AQ5 28 ASN c  25  ARG c  26  TRP c  35  GLY c  38                    
SITE     2 AQ5 28 ASN c  39  ARG c  41  LEU c  42  LEU c  45                    
SITE     3 AQ5 28 LYS c  48  ALA c  52  ALA c 123  PHE c 127                    
SITE     4 AQ5 28 ILE c 134  CLA c 509  CLA c 510  BCR c 522                    
SITE     5 AQ5 28 PHE k  32  LEU k  33  ALA k  36  TRP k  39                    
SITE     6 AQ5 28 GLN k  40  ILE y  35  ILE y  36  LEU y  39                    
SITE     7 AQ5 28 ASN y  45  VAL z  20  VAL z  23  ALA z  28                    
SITE     1 AQ6 14 HIS c  53  LEU c 125  PHE c 146  PHE c 147                    
SITE     2 AQ6 14 PHE c 163  HIS c 164  VAL c 167  ILE c 170                    
SITE     3 AQ6 14 GLY c 171  LEU c 174  CLA c 504  CLA c 510                    
SITE     4 AQ6 14 CLA c 514  BCR c 515                                          
SITE     1 AQ7  9 VAL c 124  GLY c 128  TYR c 131  HIS c 132                    
SITE     2 AQ7  9 TYR c 143  PHE c 147  CLA c 513  BCR c 515                    
SITE     3 AQ7  9 LMG z 101                                                     
SITE     1 AQ8 13 PHE c 112  VAL c 116  ILE c 120  SER c 121                    
SITE     2 AQ8 13 VAL c 124  LEU c 125  CLA c 513  CLA c 514                    
SITE     3 AQ8 13 LMG c 521  TYR k  15  VAL z  51  GLY z  55                    
SITE     4 AQ8 13 ASN z  58                                                     
SITE     1 AQ9 15 ILE c 209  PHE c 210  TYR c 212  LEU c 213                    
SITE     2 AQ9 15 VAL c 227  ASP c 232  GLY c 236  HIS c 237                    
SITE     3 AQ9 15 CLA c 502  CLA c 506  CLA c 507  CLA c 508                    
SITE     4 AQ9 15 VAL i  20  PHE i  23  LEU i  24                               
SITE     1 AR1 23 LEU a  91  SER a 148  LMG a 611  PRO c 217                    
SITE     2 AR1 23 GLY c 219  GLY c 220  GLU c 221  GLY c 222                    
SITE     3 AR1 23 TRP c 223  VAL c 225  SER c 226  VAL c 227                    
SITE     4 AR1 23 ASN c 228  PHE c 284  CYS c 288  PHE c 292                    
SITE     5 AR1 23 ASN c 293  ASN c 294  THR c 295  ASP c 360                    
SITE     6 AR1 23 PHE c 361  ARG c 362  CLA c 507                               
SITE     1 AR2 17 HIS a 195  PHE a 197  LEU a 297  GLU c  83                    
SITE     2 AR2 17 GLN c  84  GLY c  85  SER c 406  ASN c 418                    
SITE     3 AR2 17 PHE c 419  VAL c 420  TRP c 425  SER c 429                    
SITE     4 AR2 17 CLA c 505  DGD c 519  LMG c 520  PHE j  29                    
SITE     5 AR2 17 TYR j  33                                                     
SITE     1 AR3 24 GLN a 199  LEU a 200  ASN a 301  PHE a 302                    
SITE     2 AR3 24 SER a 305  LHG a 614  ASN c 405  VAL c 407                    
SITE     3 AR3 24 ASN c 415  SER c 416  VAL c 417  ASN c 418                    
SITE     4 AR3 24 CLA c 505  CLA c 509  DGD c 518  LEU d  74                    
SITE     5 AR3 24 PHE j  29  ALA j  32  TYR j  33  GLY j  37                    
SITE     6 AR3 24 SER j  38  SER j  39  LMG j 101  GLN v  34                    
SITE     1 AR4  9 HIS c  74  GLN c  84  CLA c 505  CLA c 509                    
SITE     2 AR4  9 DGD c 518  ASP k  23  VAL k  30  GLN y  21                    
SITE     3 AR4  9 ILE y  25                                                     
SITE     1 AR5  7 TRP c  97  ASP c 107  SER c 121  CLA c 504                    
SITE     2 AR5  7 BCR c 515  PHE z  59  VAL z  62                               
SITE     1 AR6 16 ALA c  55  GLY c  58  LEU c  59  PHE c  62                    
SITE     2 AR6 16 LEU c 119  SER c 122  ALA c 123  GLY c 126                    
SITE     3 AR6 16 CLA c 512  TYR k  15  PHE k  32  TRP k  39                    
SITE     4 AR6 16 BCR k 101  LEU z   9  SER z  16  TRP z  47                    
SITE     1 AR7 23 PHE a 206  ALA a 209  LEU a 210  MET a 214                    
SITE     2 AR7 23 PHE a 255  CLA a 605  PL9 a 609  ALA d  41                    
SITE     3 AR7 23 TRP d  48  ILE d 114  GLY d 118  GLY d 121                    
SITE     4 AR7 23 LEU d 122  PHE d 125  GLN d 129  ASN d 142                    
SITE     5 AR7 23 ALA d 145  PHE d 146  PRO d 149  PHE d 153                    
SITE     6 AR7 23 PRO d 275  LEU d 279  CLA d 402                               
SITE     1 AR8 22 MET a 183  PHE a 206  CLA a 604  CLA a 605                    
SITE     2 AR8 22 CLA a 613  LEU d  45  LEU d 122  PRO d 149                    
SITE     3 AR8 22 VAL d 152  PHE d 153  VAL d 156  LEU d 182                    
SITE     4 AR8 22 PHE d 185  GLN d 186  TRP d 191  HIS d 197                    
SITE     5 AR8 22 GLY d 200  VAL d 201  SER d 282  ALA d 283                    
SITE     6 AR8 22 VAL d 286  PHO d 401                                          
SITE     1 AR9 16 PRO d  39  CYS d  40  LEU d  43  LEU d  89                    
SITE     2 AR9 16 LEU d  90  LEU d  91  LEU d  92  TRP d  93                    
SITE     3 AR9 16 THR d 112  PHE d 113  HIS d 117  LEU h  39                    
SITE     4 AR9 16 GLY x  13  LEU x  14  VAL x  20  LEU x  21                    
SITE     1 AS1 23 PHE a  52  ILE a  53  CLA a 613  MET d 198                    
SITE     2 AS1 23 MET d 199  ALA d 202  LEU d 209  HIS d 214                    
SITE     3 AS1 23 THR d 217  TRP d 253  ALA d 260  PHE d 261                    
SITE     4 AS1 23 LEU d 267  PHE d 273  VAL d 274  THR d 277                    
SITE     5 AS1 23 GLY d 278  LHG d 406  LEU l  23  VAL l  26                    
SITE     6 AS1 23 LEU l  29  LHG l 101  PHE t  10                               
SITE     1 AS2  5 GLY d  99  ASP d 100  THR d 102  ASP e  45                    
SITE     2 AS2  5 BCR f 101                                                     
SITE     1 AS3 20 MET a  37  PHE d 257  ILE d 259  ALA d 260                    
SITE     2 AS3 20 PHE d 261  SER d 262  ASN d 263  TRP d 266                    
SITE     3 AS3 20 PHE d 270  PL9 d 404  ASN l  13  THR l  15                    
SITE     4 AS3 20 SER l  16  TYR l  18  LEU l  19  LHG l 101                    
SITE     5 AS3 20 PHE t  10  PHE t  17  ALA t  20  ILE t  21                    
SITE     1 AS4 11 LEU a 258  PHE a 260  TYR a 262  PHE d  27                    
SITE     2 AS4 11 THR e   4  THR e   5  GLU e   7  PRO e   9                    
SITE     3 AS4 11 PHE e  10  SER e  11  ALA f  22                               
SITE     1 AS5 12 ARG e  18  TYR e  19  HIS e  23  ILE e  27                    
SITE     2 AS5 12 LEU e  30  ILE f  15  ARG f  19  TRP f  20                    
SITE     3 AS5 12 VAL f  23  HIS f  24  VAL f  28  ILE f  31                    
SITE     1 AS6 14 TYR d  42  LEU d  43  GLY d  46  LEU d  49                    
SITE     2 AS6 14 THR d  50  PHE d 101  DGD d 405  PRO f  29                    
SITE     3 AS6 14 THR f  30  PHE f  33  LEU f  34  VAL j  21                    
SITE     4 AS6 14 VAL j  25  LMG j 101                                          
SITE     1 AS7  2 ARG f  45  GLU v  23                                          
SITE     1 AS8  7 CLA b 604  CLA b 605  CLA b 612  MET h  31                    
SITE     2 AS8  7 LEU h  37  PHE h  38  PHE h  41                               
SITE     1 AS9 16 TYR b 193  PHE b 250  GLY b 254  TYR b 258                    
SITE     2 AS9 16 GLN b 274  ALA b 456  PHE b 463  HIS d  87                    
SITE     3 AS9 16 ILE d 123  LEU d 162  LEU h  46  TYR h  49                    
SITE     4 AS9 16 ASN h  50  VAL h  60  SER h  61  TRP h  62                    
SITE     1 AT1 18 CLA a 605  DGD c 519  TYR d  67  GLY d  70                    
SITE     2 AT1 18 CYS d  71  ASN d  72  PHE d  73  LEU f  26                    
SITE     3 AT1 18 THR f  30  ILE f  37  MET f  40  GLN f  41                    
SITE     4 AT1 18 BCR f 101  PHE j  28  GLY j  31  ALA j  32                    
SITE     5 AT1 18 LEU j  36   MG j 102                                          
SITE     1 AT2  6 GLN f  41  GLY j  31  ALA j  34  GLY j  35                    
SITE     2 AT2  6 LEU j  36  LMG j 101                                          
SITE     1 AT3 16 PHE c  62  BCR c 522  ALA j  14  THR j  15                    
SITE     2 AT3 16 GLY j  18  MET j  19  LEU k  21  LEU k  31                    
SITE     3 AT3 16 PHE k  32  ALA k  34  ALA k  41  ILE y  28                    
SITE     4 AT3 16 GLY y  29  PRO y  33  VAL z  13  PHE z  17                    
SITE     1 AT4 21 SER a 232  ASN a 234  CLA a 613  PRO b   4                    
SITE     2 AT4 21 TRP b   5  TYR b   6  LHG b 624  TRP d 266                    
SITE     3 AT4 21 PHE d 273  PL9 d 404  LHG d 406  GLU l  11                    
SITE     4 AT4 21 LEU l  12  ASN l  13  SER l  16  GLY l  20                    
SITE     5 AT4 21 LEU l  22  LEU l  23  VAL l  26  PHE m  21                    
SITE     6 AT4 21 LEU m  22                                                     
SITE     1 AT5  3 THR o 138  ASN o 200  VAL o 201                               
SITE     1 AT6 14 TRP B  33  SER B  36  MET B  37  PHE B 108                    
SITE     2 AT6 14 LEU B 109  CLA B 608  BCR B 618  BCR B 619                    
SITE     3 AT6 14 LEU a  28  SQD a 612  PHE t   8  ALA t  15                    
SITE     4 AT6 14 PHE t  18  PHE t  22                                          
SITE     1 AT7 18 ALA v  36  CYS v  37  CYS v  40  HIS v  41                    
SITE     2 AT7 18 THR v  48  LEU v  52  ASP v  53  LEU v  54                    
SITE     3 AT7 18 THR v  58  ALA v  62  LEU v  72  TYR v  75                    
SITE     4 AT7 18 MET v  76  THR v  81  TYR v  82  HIS v  92                    
SITE     5 AT7 18 PRO v  93  MET v 104                                          
SITE     1 AT8 12 TRP d  21  ARG d  24  ARG d  26  PHE f  16                    
SITE     2 AT8 12 THR f  17  VAL f  18  LEU x  23  THR x  24                    
SITE     3 AT8 12 VAL x  27  LEU x  28  ILE x  31  ASP x  35                    
SITE     1 AT9  9 PHE c 127  TYR c 131  ARG c 135  CLA c 514                    
SITE     2 AT9  9 TYR z  27  TRP z  33  LYS z  37  PHE z  41                    
SITE     3 AT9  9 TRP z  47                                                     
CRYST1  133.250  226.260  307.090  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      0.007505  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004420  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003256        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system