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Database: PDB
Entry: 4PBU
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HEADER    PHOTOSYNTHESIS                          13-APR-14   4PBU              
TITLE     SERIAL TIME-RESOLVED CRYSTALLOGRAPHY OF PHOTOSYSTEM II USING A        
TITLE    2 FEMTOSECOND X-RAY LASER THE S1 STATE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;                                
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN 1, PHOTOSYSTEM II PROTEIN 
COMPND   5 D-1, PHOTOSYSTEM II D-1 PROTEIN;                                     
COMPND   6 EC: 1.10.3.9;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PHOTOSYSTEM II CORE LIGHT HARVESTING PROTEIN;              
COMPND   9 CHAIN: B, b;                                                         
COMPND  10 SYNONYM: PHOTOSYSTEM II CP47 PROTEIN;                                
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;                               
COMPND  13 CHAIN: C, c;                                                         
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  16 CHAIN: D, d;                                                         
COMPND  17 SYNONYM: PSII D2 PROTEIN, PHOTOSYSTEM Q(A) PROTEIN, PHOTOSYSTEM II D2
COMPND  18 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, PSII 5 KDA PROTEIN;                                 
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 
COMPND  68 C;                                                                   
COMPND  69 MOL_ID: 17;                                                          
COMPND  70 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  71 CHAIN: Y, y;                                                         
COMPND  72 MOL_ID: 18;                                                          
COMPND  73 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  74 CHAIN: X, x;                                                         
COMPND  75 MOL_ID: 19;                                                          
COMPND  76 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  77 CHAIN: Z, z;                                                         
COMPND  78 SYNONYM: PSII-Z                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 STRAIN: BP-1;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   7 ORGANISM_TAXID: 197221;                                              
SOURCE   8 STRAIN: BP-1;                                                        
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  11 ORGANISM_TAXID: 197221;                                              
SOURCE  12 STRAIN: BP-1;                                                        
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  15 ORGANISM_TAXID: 197221;                                              
SOURCE  16 STRAIN: BP-1;                                                        
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  19 ORGANISM_TAXID: 197221;                                              
SOURCE  20 STRAIN: BP-1;                                                        
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  23 ORGANISM_TAXID: 197221;                                              
SOURCE  24 STRAIN: BP-1;                                                        
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  27 ORGANISM_TAXID: 197221;                                              
SOURCE  28 STRAIN: BP-1;                                                        
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  31 ORGANISM_TAXID: 197221;                                              
SOURCE  32 STRAIN: BP-1;                                                        
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  35 ORGANISM_TAXID: 197221;                                              
SOURCE  36 STRAIN: BP-1;                                                        
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  39 ORGANISM_TAXID: 197221;                                              
SOURCE  40 STRAIN: BP-1;                                                        
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  43 ORGANISM_TAXID: 197221;                                              
SOURCE  44 STRAIN: BP-1;                                                        
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  47 ORGANISM_TAXID: 197221;                                              
SOURCE  48 STRAIN: BP-1;                                                        
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  51 ORGANISM_TAXID: 197221;                                              
SOURCE  52 STRAIN: BP-1;                                                        
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  55 ORGANISM_TAXID: 197221;                                              
SOURCE  56 STRAIN: BP-1;                                                        
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  59 ORGANISM_TAXID: 197221;                                              
SOURCE  60 STRAIN: BP-1;                                                        
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  63 ORGANISM_TAXID: 197221;                                              
SOURCE  64 STRAIN: BP-1;                                                        
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  67 ORGANISM_TAXID: 197221;                                              
SOURCE  68 STRAIN: BP-1;                                                        
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  71 ORGANISM_TAXID: 197221;                                              
SOURCE  72 STRAIN: BP-1;                                                        
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  75 ORGANISM_TAXID: 197221;                                              
SOURCE  76 STRAIN: BP-1                                                         
KEYWDS    PHOTOSYSTEM II, TIME RESOLVED, FREE ELECTRON LASER, PHOTOSYNTHESIS    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.KUPITZ,S.BASU,I.GROTJOHANN,R.FROMME,N.ZATSEPIN,K.N.RENDEK,M.HUNTER, 
AUTHOR   2 R.L.SHOEMAN,T.A.WHITE,D.WANG,D.JAMES,J.H.YANG,D.E.COBB,B.REEDER,     
AUTHOR   3 R.G.SIERRA,H.LIU,A.BARTY,A.AQUILA,D.DEPONTE,R.A.KIRIAN,S.BARI,       
AUTHOR   4 J.J.BERGKAMP,K.BEYERLEIN,M.J.BOGAN,C.CALEMAN,T.-C.CHAO,C.E.CONRAD,   
AUTHOR   5 K.M.DAVIS,H.FLECKENSTEIN,L.GALLI,S.P.HAU-RIEGE,S.KASSEMEYER,         
AUTHOR   6 H.LAKSMONO,M.LIANG,L.LOMB,S.MARCHESINI,A.V.MARTIN,M.MESSERSCHMIDT,   
AUTHOR   7 D.MILATHIANAKI,K.NASS,A.ROS,S.ROY-CHOWDHURY,K.SCHMIDT,M.SEIBERT,     
AUTHOR   8 J.STEINBRENER,F.STELLATO,L.YAN,C.YOON,T.A.MOORE,A.L.MOORE,Y.PUSHKAR, 
AUTHOR   9 G.J.WILLIAMS,S.BOUTET,R.B.DOAK,U.WEIERSTALL,M.FRANK,H.N.CHAPMAN,     
AUTHOR  10 J.C.H.SPENCE,P.FROMME                                                
REVDAT   9   27-NOV-19 4PBU    1       REMARK                                   
REVDAT   8   19-SEP-18 4PBU    1       REMARK                                   
REVDAT   7   22-NOV-17 4PBU    1       REMARK                                   
REVDAT   6   06-SEP-17 4PBU    1       REMARK                                   
REVDAT   5   23-SEP-15 4PBU    1       REMARK                                   
REVDAT   4   01-OCT-14 4PBU    1       JRNL                                     
REVDAT   3   06-AUG-14 4PBU    1       AUTHOR                                   
REVDAT   2   30-JUL-14 4PBU    1       JRNL                                     
REVDAT   1   16-JUL-14 4PBU    0                                                
JRNL        AUTH   C.KUPITZ,S.BASU,I.GROTJOHANN,R.FROMME,N.A.ZATSEPIN,          
JRNL        AUTH 2 K.N.RENDEK,M.S.HUNTER,R.L.SHOEMAN,T.A.WHITE,D.WANG,D.JAMES,  
JRNL        AUTH 3 J.H.YANG,D.E.COBB,B.REEDER,R.G.SIERRA,H.LIU,A.BARTY,         
JRNL        AUTH 4 A.L.AQUILA,D.DEPONTE,R.A.KIRIAN,S.BARI,J.J.BERGKAMP,         
JRNL        AUTH 5 K.R.BEYERLEIN,M.J.BOGAN,C.CALEMAN,T.C.CHAO,C.E.CONRAD,       
JRNL        AUTH 6 K.M.DAVIS,H.FLECKENSTEIN,L.GALLI,S.P.HAU-RIEGE,S.KASSEMEYER, 
JRNL        AUTH 7 H.LAKSMONO,M.LIANG,L.LOMB,S.MARCHESINI,A.V.MARTIN,           
JRNL        AUTH 8 M.MESSERSCHMIDT,D.MILATHIANAKI,K.NASS,A.ROS,S.ROY-CHOWDHURY, 
JRNL        AUTH 9 K.SCHMIDT,M.SEIBERT,J.STEINBRENER,F.STELLATO,L.YAN,C.YOON,   
JRNL        AUTH10 T.A.MOORE,A.L.MOORE,Y.PUSHKAR,G.J.WILLIAMS,S.BOUTET,         
JRNL        AUTH11 R.B.DOAK,U.WEIERSTALL,M.FRANK,H.N.CHAPMAN,J.C.SPENCE,        
JRNL        AUTH12 P.FROMME                                                     
JRNL        TITL   SERIAL TIME-RESOLVED CRYSTALLOGRAPHY OF PHOTOSYSTEM II USING 
JRNL        TITL 2 A FEMTOSECOND X-RAY LASER.                                   
JRNL        REF    NATURE                        V. 513   261 2014              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   25043005                                                     
JRNL        DOI    10.1038/NATURE13453                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
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) : 5.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.64                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 40946                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.261                           
REMARK   3   R VALUE            (WORKING SET) : 0.261                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2056                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1100.6583 - 12.3240    1.00     2781   141  0.3308 0.3492        
REMARK   3     2 12.3240 -  9.7846    1.00     2649   146  0.2021 0.2183        
REMARK   3     3  9.7846 -  8.5485    1.00     2617   152  0.1916 0.1719        
REMARK   3     4  8.5485 -  7.7672    1.00     2588   135  0.2071 0.2055        
REMARK   3     5  7.7672 -  7.2107    1.00     2634   118  0.2360 0.2221        
REMARK   3     6  7.2107 -  6.7856    1.00     2617   116  0.2407 0.2425        
REMARK   3     7  6.7856 -  6.4459    1.00     2533   160  0.2454 0.2503        
REMARK   3     8  6.4459 -  6.1653    1.00     2579   136  0.2601 0.2509        
REMARK   3     9  6.1653 -  5.9280    1.00     2569   144  0.2766 0.2731        
REMARK   3    10  5.9280 -  5.7235    1.00     2567   135  0.2859 0.2517        
REMARK   3    11  5.7235 -  5.5445    1.00     2531   128  0.2959 0.2806        
REMARK   3    12  5.5445 -  5.3860    1.00     2559   138  0.3080 0.2834        
REMARK   3    13  5.3860 -  5.2442    1.00     2564   133  0.3120 0.2985        
REMARK   3    14  5.2442 -  5.1163    1.00     2532   134  0.3246 0.3632        
REMARK   3    15  5.1163 -  5.0000    1.00     2570   140  0.3502 0.3434        
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)     : 0.600            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.720           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 285.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.75                          
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      :  0.039          51301                                  
REMARK   3   ANGLE     :  3.029          70757                                  
REMARK   3   CHIRALITY :  0.491           7125                                  
REMARK   3   PLANARITY :  0.020           8628                                  
REMARK   3   DIHEDRAL  : 21.659          18204                                  
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 : 19                                          
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN A                                     
REMARK   3     ATOM PAIRS NUMBER  : 3021                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 4445                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 4054                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 3154                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN E                                     
REMARK   3     SELECTION          : CHAIN E                                     
REMARK   3     ATOM PAIRS NUMBER  : 735                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 6                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN F                                     
REMARK   3     SELECTION          : CHAIN F                                     
REMARK   3     ATOM PAIRS NUMBER  : 290                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 7                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN H                                     
REMARK   3     SELECTION          : CHAIN H                                     
REMARK   3     ATOM PAIRS NUMBER  : 568                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 8                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN I                                     
REMARK   3     SELECTION          : CHAIN I                                     
REMARK   3     ATOM PAIRS NUMBER  : 342                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 9                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN J                                     
REMARK   3     SELECTION          : CHAIN J                                     
REMARK   3     ATOM PAIRS NUMBER  : 312                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 10                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN K                                     
REMARK   3     SELECTION          : CHAIN K                                     
REMARK   3     ATOM PAIRS NUMBER  : 336                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 11                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN L                                     
REMARK   3     SELECTION          : CHAIN L                                     
REMARK   3     ATOM PAIRS NUMBER  : 348                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 12                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN M                                     
REMARK   3     SELECTION          : CHAIN M                                     
REMARK   3     ATOM PAIRS NUMBER  : 302                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 13                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN O                                     
REMARK   3     SELECTION          : CHAIN O                                     
REMARK   3     ATOM PAIRS NUMBER  : 2194                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 14                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN T                                     
REMARK   3     SELECTION          : CHAIN T                                     
REMARK   3     ATOM PAIRS NUMBER  : 273                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 15                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN U                                     
REMARK   3     SELECTION          : CHAIN U                                     
REMARK   3     ATOM PAIRS NUMBER  : 930                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 16                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN V                                     
REMARK   3     SELECTION          : CHAIN V                                     
REMARK   3     ATOM PAIRS NUMBER  : 1264                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 17                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN X                                     
REMARK   3     SELECTION          : CHAIN X                                     
REMARK   3     ATOM PAIRS NUMBER  : 313                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 18                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN Y                                     
REMARK   3     SELECTION          : CHAIN Y                                     
REMARK   3     ATOM PAIRS NUMBER  : 251                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 19                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN Z                                     
REMARK   3     SELECTION          : CHAIN Z                                     
REMARK   3     ATOM PAIRS NUMBER  : 531                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4PBU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201052.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 7.0                                
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) : 2.04                               
REMARK 200  MONOCHROMATOR                  : NONE                               
REMARK 200  OPTICS                         : SEVERAL DAYS                       
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          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40964                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 5.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.638                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 684.0                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 5.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 617.0                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: 3ARC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.96                     
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 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     ILE C    21                                                      
REMARK 465     PHE C    22                                                      
REMARK 465     MET J     1                                                      
REMARK 465     MET J     2                                                      
REMARK 465     GLU d    11                                                      
REMARK 465     SER f    12                                                      
REMARK 465     TYR f    13                                                      
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   SG   CYS V    37     CAB  HEM V   202              2.03            
REMARK 500   SG   CYS V    40     CAC  HEM V   202              2.03            
REMARK 500   NZ   LYS c   457     O    GLU d   227              2.08            
REMARK 500   SG   CYS v    40     CAC  HEM v   202              2.12            
REMARK 500   SG   CYS v    37     CAB  HEM v   202              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    THR O    37     CG   ASN c    19     2455     0.56            
REMARK 500   O    THR O    37     ND2  ASN c    19     2455     0.91            
REMARK 500   NE2  GLN O    36     CA   ASN c    19     2455     0.99            
REMARK 500   N    THR O    37     OD1  ASN c    19     2455     1.04            
REMARK 500   NE2  GLN O    36     C    ASN c    19     2455     1.05            
REMARK 500   O    SER O    35     OG   SER c    20     2455     1.43            
REMARK 500   NE2  GLN O    36     N    ASN c    19     2455     1.56            
REMARK 500   C    THR O    37     OD1  ASN c    19     2455     1.59            
REMARK 500   O    THR O    37     CB   ASN c    19     2455     1.60            
REMARK 500   O    THR O    37     OD1  ASN c    19     2455     1.73            
REMARK 500   OE1  GLN O    36     N    SER c    20     2455     1.77            
REMARK 500   CA   GLN O    36     CB   SER c    20     2455     1.77            
REMARK 500   CD   GLN O    36     N    ASN c    19     2455     1.89            
REMARK 500   C    GLN O    36     OD1  ASN c    19     2455     1.94            
REMARK 500   CD   GLN O    36     C    ASN c    19     2455     1.97            
REMARK 500   OE1  GLN O    36     O    SER c    20     2455     2.03            
REMARK 500   C    SER O    35     OG   SER c    20     2455     2.06            
REMARK 500   CA   THR O    37     CG   ASN c    19     2455     2.09            
REMARK 500   N    TYR O    38     ND2  ASN c    19     2455     2.12            
REMARK 500   OD2  ASP O    33     CA   ALA c    23     2455     2.14            
REMARK 500   OXT  ALA O   246     CB   ASN c    19     2455     2.14            
REMARK 500   NE2  GLN O    36     CB   ASN c    19     2455     2.17            
REMARK 500   O    SER O    35     CB   SER c    20     2455     2.18            
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      -82.90    -93.24                                   
REMARK 500    LEU A 159      -54.97   -124.71                                   
REMARK 500    ILE A 259      -93.51   -101.21                                   
REMARK 500    TYR B 117       55.86    -92.30                                   
REMARK 500    ASP B 313       45.52    -93.51                                   
REMARK 500    PHE B 383      -77.83    -86.85                                   
REMARK 500    ASP C 107      114.00   -160.69                                   
REMARK 500    GLU C 221      -65.05   -125.05                                   
REMARK 500    TRP C 223     -137.61     46.74                                   
REMARK 500    THR C 295      -60.12   -100.82                                   
REMARK 500    SER C 416      -49.33    175.15                                   
REMARK 500    ARG D  12       42.42   -156.08                                   
REMARK 500    VAL D  30      -70.48   -107.17                                   
REMARK 500    SER D  65       14.90   -148.63                                   
REMARK 500    PRO D 140       44.95    -91.64                                   
REMARK 500    ALA D 234       32.70    -77.87                                   
REMARK 500    PRO D 309        1.78    -66.02                                   
REMARK 500    ALA D 351      -52.26     71.42                                   
REMARK 500    LYS H  63       31.95    -82.84                                   
REMARK 500    LEU H  65      -88.06   -150.65                                   
REMARK 500    LYS I  33     -119.87   -110.34                                   
REMARK 500    SER J  39       -4.07     73.51                                   
REMARK 500    ASN O  58       -3.58    149.42                                   
REMARK 500    ARG O  73     -163.40     70.15                                   
REMARK 500    THR O 138        8.18    -69.31                                   
REMARK 500    ASN U  29      -37.10   -138.98                                   
REMARK 500    TYR U 103     -144.13   -112.85                                   
REMARK 500    ASN V  49       81.88   -158.76                                   
REMARK 500    ASP V  67       36.37    -89.53                                   
REMARK 500    PHE V 101       79.42   -116.65                                   
REMARK 500    ASP X  35       68.47   -116.95                                   
REMARK 500    VAL a  30      -82.54    -93.21                                   
REMARK 500    LEU a 159      -51.87   -129.14                                   
REMARK 500    ILE a 259      -93.41   -100.44                                   
REMARK 500    TYR b 117       53.82    -97.25                                   
REMARK 500    PHE b 162       81.66   -155.10                                   
REMARK 500    ASP b 313       47.84    -92.88                                   
REMARK 500    PHE b 383      -79.05    -85.83                                   
REMARK 500    GLU b 485       50.74   -104.45                                   
REMARK 500    LEU c  45       79.59   -118.73                                   
REMARK 500    ASP c 107      115.56   -165.52                                   
REMARK 500    GLU c 221      -69.01   -122.97                                   
REMARK 500    TRP c 223     -140.99     51.01                                   
REMARK 500    SER c 416      -48.89    169.61                                   
REMARK 500    SER c 463       54.69   -143.92                                   
REMARK 500    VAL d  30      -67.35   -105.41                                   
REMARK 500    SER d  65       11.52   -141.44                                   
REMARK 500    PRO d 140       44.42    -90.50                                   
REMARK 500    ALA d 234       31.78    -78.14                                   
REMARK 500    PRO d 309        2.78    -69.27                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 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     LHG A  615                                                       
REMARK 610     DGD C  516                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     DGD C  518                                                       
REMARK 610     DGD D  406                                                       
REMARK 610     SQD F  101                                                       
REMARK 610     DGD H  102                                                       
REMARK 610     LHG a  413                                                       
REMARK 610     DGD c  916                                                       
REMARK 610     DGD c  917                                                       
REMARK 610     DGD d  406                                                       
REMARK 610     SQD d  407                                                       
REMARK 610     DGD h  102                                                       
REMARK 610     DGD j  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  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD1                                                    
REMARK 620 2 OEX A 601   O5   99.7                                              
REMARK 620 3 OEX A 601   O4   90.4  92.5                                        
REMARK 620 4 GLU A 333   OE2 171.6  84.4  96.9                                  
REMARK 620 N                    1     2     3                                   
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   OD2                                                    
REMARK 620 2 OEX A 601   O1  155.9                                              
REMARK 620 3 OEX A 601   O2   84.6  75.2                                        
REMARK 620 4 OEX A 601   O5  111.5  76.8  76.7                                  
REMARK 620 5 ALA A 344   O    84.3  78.3  76.2 147.0                            
REMARK 620 N                    1     2     3     4                             
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   93.2                                              
REMARK 620 3 OEX A 601   O5   96.4  82.4                                        
REMARK 620 4 OEX A 601   O3  174.1  92.0  81.7                                  
REMARK 620 5 HIS A 332   NE2  86.4 178.3  99.3  88.4                            
REMARK 620 6 ASP A 342   OD2  94.2  91.9 168.2  88.3  86.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2  93.0                                              
REMARK 620 3 HIS D 214   NE2 110.9  91.0                                        
REMARK 620 4 HIS D 268   NE2  89.0 177.3  89.9                                  
REMARK 620 5 BCT A 605   O3  155.9  92.3  92.4  85.1                            
REMARK 620 6 BCT A 605   O2   99.4  84.4 149.5  93.6  57.8                      
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  176.3                                              
REMARK 620 3 OEX A 601   O3   88.7  93.2                                        
REMARK 620 4 OEX A 601   O4   95.0  83.2 175.9                                  
REMARK 620 5 OEX A 601   O5   91.1  92.3  81.5  96.6                            
REMARK 620 6 GLU C 354   OE2  87.7  89.2  86.1  95.9 167.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 OEX A 601   O1   90.2                                              
REMARK 620 3 OEX A 601   O2  179.2  89.0                                        
REMARK 620 4 OEX A 601   O3   93.3  78.9  86.8                                  
REMARK 620 5 ALA A 344   OXT  90.1  94.4  89.7 172.5                            
REMARK 620 6 GLU C 354   OE1  93.7 168.2  87.1  89.8  96.7                      
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  100.0                                              
REMARK 620 3 CLA C 511   NB  102.4  87.7                                        
REMARK 620 4 CLA C 511   NC   97.8 160.9  95.1                                  
REMARK 620 5 CLA C 511   ND   98.8  90.5 158.7  80.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM E 101   NA   96.8                                              
REMARK 620 3 HEM E 101   NB  100.1  88.7                                        
REMARK 620 4 HEM E 101   NC   88.5 174.6  90.6                                  
REMARK 620 5 HEM E 101   ND   79.6  93.0 178.3  87.7                            
REMARK 620 6 HIS F  24   NE2 174.0  83.4  85.8  91.3  94.4                      
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  43.9                                              
REMARK 620 N                    1                                               
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 149.7                                              
REMARK 620 3 VAL O 201   O    78.6  75.3                                        
REMARK 620 N                    1     2                                         
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   88.7                                              
REMARK 620 3 HEM V 202   NB   87.3  91.4                                        
REMARK 620 4 HEM V 202   NC   91.8 179.4  88.4                                  
REMARK 620 5 HEM V 202   ND   91.2  88.5 178.5  91.8                            
REMARK 620 6 HIS V  92   NE2 177.7  93.3  91.5  86.2  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 401  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD1                                                    
REMARK 620 2 OEX a 401   O5  108.8                                              
REMARK 620 3 OEX a 401   O4   91.1  96.4                                        
REMARK 620 4 GLU a 333   OE2 168.6  78.6  96.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 401  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD2                                                    
REMARK 620 2 OEX a 401   O1  158.7                                              
REMARK 620 3 OEX a 401   O2   85.2  75.8                                        
REMARK 620 4 OEX a 401   O5  108.4  76.8  77.1                                  
REMARK 620 5 ALA a 344   O    88.9  76.9  73.9 144.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 401  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 OEX a 401   O1   94.3                                              
REMARK 620 3 OEX a 401   O5   97.6  92.9                                        
REMARK 620 4 OEX a 401   O3  168.9  95.4  76.6                                  
REMARK 620 5 HIS a 332   NE2  83.5 177.4  88.6  86.9                            
REMARK 620 6 ASP a 342   OD2  90.8  90.1 170.8  94.5  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a 403  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS a 272   NE2  92.5                                              
REMARK 620 3 HIS d 214   NE2 109.1  87.4                                        
REMARK 620 4 HIS d 268   NE2  95.2 172.2  91.2                                  
REMARK 620 5 BCT a 414   O2  106.9  84.2 143.4  92.5                            
REMARK 620 6 BCT a 414   O3  166.5  86.9  84.4  85.4  59.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 401  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 OEX a 401   O2  175.6                                              
REMARK 620 3 OEX a 401   O3   90.8  90.9                                        
REMARK 620 4 OEX a 401   O4   91.7  86.7 176.4                                  
REMARK 620 5 OEX a 401   O5   86.5  97.8  78.7  98.8                            
REMARK 620 6 GLU c 354   OE2  89.1  87.0  86.6  96.1 164.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 401  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 342   OD1                                                    
REMARK 620 2 OEX a 401   O1   87.5                                              
REMARK 620 3 OEX a 401   O2  179.0  93.5                                        
REMARK 620 4 OEX a 401   O3   95.4  80.3  84.7                                  
REMARK 620 5 ALA a 344   OXT  88.1  95.8  91.8 174.6                            
REMARK 620 6 GLU c 354   OE1  91.0 167.8  88.0  87.8  96.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA c 901  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE c  22   O                                                      
REMARK 620 2 THR c  24   O    84.3                                              
REMARK 620 3 ASP c  27   OD1 130.4  96.1                                        
REMARK 620 4 ASP c  27   OD2  80.9  79.7  50.9                                  
REMARK 620 5 GLU c  29   OE1  96.2 175.5  87.0 104.8                            
REMARK 620 6 SER c  30   OG  151.8  89.8  77.6 125.1  87.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 912  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c  39   OD1                                                    
REMARK 620 2 CLA c 912   NA  108.1                                              
REMARK 620 3 CLA c 912   NB  107.0  91.6                                        
REMARK 620 4 CLA c 912   NC   94.5 154.9  91.8                                  
REMARK 620 5 CLA c 912   ND  100.4  89.4 150.7  75.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM e 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e  23   NE2                                                    
REMARK 620 2 HEM e 101   NA  100.7                                              
REMARK 620 3 HEM e 101   NB   99.2  88.4                                        
REMARK 620 4 HEM e 101   NC   84.8 174.5  91.0                                  
REMARK 620 5 HEM e 101   ND   80.2  92.5 179.0  88.1                            
REMARK 620 6 HIS f  24   NE2 168.3  81.1  92.4  93.4  88.2                      
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  43.6                                              
REMARK 620 N                    1                                               
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    75.9                                              
REMARK 620 3 LEU j  36   O   104.7 108.0                                        
REMARK 620 N                    1     2                                         
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 154.7                                              
REMARK 620 3 VAL o 201   O    83.9  72.7                                        
REMARK 620 N                    1     2                                         
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   94.3                                              
REMARK 620 3 HEM v 202   NB   88.5  86.8                                        
REMARK 620 4 HEM v 202   NC   86.6 179.1  93.5                                  
REMARK 620 5 HEM v 202   ND   89.6  92.9 178.1  86.7                            
REMARK 620 6 HIS v  92   NE2 171.4  93.6  95.4  85.5  86.5                      
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 FE2 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 CL A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT 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 CLA A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD F 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD L 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR Y 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA b 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA c 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 909                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 910                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 913                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 914                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 915                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 916                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 917                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 918                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA f 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD j 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG j 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD l 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA o 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM v 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand THR O 37 bound to ASN c    
REMARK 800  19                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand THR O 37 bound to ASN c    
REMARK 800  19                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand THR O 37 bound to ASN c    
REMARK 800  19                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand GLN O 36 bound to SER c    
REMARK 800  20                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand GLN O 36 bound to SER c    
REMARK 800  20                                                                  
DBREF  4PBU A   11   344  UNP    P0A444   PSBA1_THEEB     11    344             
DBREF  4PBU B    2   505  UNP    Q8DIQ1   Q8DIQ1_THEEB     2    505             
DBREF  4PBU C   19   473  UNP    Q8DIF8   Q8DIF8_THEEB     7    461             
DBREF  4PBU D   11   352  UNP    Q8CM25   PSBD_THEEB      11    352             
DBREF  4PBU E    4    84  UNP    Q8DIP0   PSBE_THEEB       4     84             
DBREF  4PBU F   12    45  UNP    Q8DIN9   PSBF_THEEB      12     45             
DBREF  4PBU H    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  4PBU I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4PBU J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4PBU K   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  4PBU L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4PBU M    1    34  UNP    Q8DHA7   PSBM_THEEB       1     34             
DBREF  4PBU O    4   246  UNP    P0A431   PSBO_THEEB      30    272             
DBREF  4PBU T    1    30  UNP    Q8DIQ0   PSBT_THEEB       1     30             
DBREF  4PBU U    8   104  UNP    Q9F1L5   PSBU_THEEB      38    134             
DBREF  4PBU V    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  4PBU Y   18    46  UNP    Q8DJI1   YCF12_THEEB     18     46             
DBREF  4PBU X    2    40  UNP    Q9F1R6   PSBX_THEEB       2     40             
DBREF  4PBU Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  4PBU a   11   344  UNP    P0A444   PSBA1_THEEB     11    344             
DBREF  4PBU b    2   505  UNP    Q8DIQ1   Q8DIQ1_THEEB     2    505             
DBREF  4PBU c   19   473  UNP    Q8DIF8   Q8DIF8_THEEB     7    461             
DBREF  4PBU d   11   352  UNP    Q8CM25   PSBD_THEEB      11    352             
DBREF  4PBU e    4    84  UNP    Q8DIP0   PSBE_THEEB       4     84             
DBREF  4PBU f   12    45  UNP    Q8DIN9   PSBF_THEEB      12     45             
DBREF  4PBU h    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  4PBU i    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4PBU j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4PBU k   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  4PBU l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4PBU m    1    34  UNP    Q8DHA7   PSBM_THEEB       1     34             
DBREF  4PBU o    4   246  UNP    P0A431   PSBO_THEEB      30    272             
DBREF  4PBU t    1    30  UNP    Q8DIQ0   PSBT_THEEB       1     30             
DBREF  4PBU u    8   104  UNP    Q9F1L5   PSBU_THEEB      38    134             
DBREF  4PBU v    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  4PBU y   18    46  UNP    Q8DJI1   YCF12_THEEB     18     46             
DBREF  4PBU x    2    40  UNP    Q9F1R6   PSBX_THEEB       2     40             
DBREF  4PBU z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
SEQADV 4PBU ALA A  286  UNP  P0A444    THR   286 CONFLICT                       
SEQADV 4PBU 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  455  ASN SER ILE PHE ALA THR ASN ARG ASP GLN GLU SER SER          
SEQRES   2 C  455  GLY PHE ALA TRP TRP ALA GLY ASN ALA ARG LEU ILE ASN          
SEQRES   3 C  455  LEU SER GLY LYS LEU LEU GLY ALA HIS VAL ALA HIS ALA          
SEQRES   4 C  455  GLY LEU ILE VAL PHE TRP ALA GLY ALA MET THR LEU PHE          
SEQRES   5 C  455  GLU LEU ALA HIS PHE ILE PRO GLU LYS PRO MET TYR GLU          
SEQRES   6 C  455  GLN GLY LEU ILE LEU ILE PRO HIS ILE ALA THR LEU GLY          
SEQRES   7 C  455  TRP GLY VAL GLY PRO GLY GLY GLU VAL VAL ASP THR PHE          
SEQRES   8 C  455  PRO PHE PHE VAL VAL GLY VAL VAL HIS LEU ILE SER SER          
SEQRES   9 C  455  ALA VAL LEU GLY PHE GLY GLY VAL TYR HIS ALA ILE ARG          
SEQRES  10 C  455  GLY PRO GLU THR LEU GLU GLU TYR SER SER PHE PHE GLY          
SEQRES  11 C  455  TYR ASP TRP LYS ASP LYS ASN LYS MET THR THR ILE LEU          
SEQRES  12 C  455  GLY PHE HIS LEU ILE VAL LEU GLY ILE GLY ALA LEU LEU          
SEQRES  13 C  455  LEU VAL ALA LYS ALA MET PHE PHE GLY GLY LEU TYR ASP          
SEQRES  14 C  455  THR TRP ALA PRO GLY GLY GLY ASP VAL ARG VAL ILE THR          
SEQRES  15 C  455  ASN PRO THR LEU ASP PRO ARG VAL ILE PHE GLY TYR LEU          
SEQRES  16 C  455  LEU LYS SER PRO PHE GLY GLY GLU GLY TRP ILE VAL SER          
SEQRES  17 C  455  VAL ASN ASN LEU GLU ASP VAL VAL GLY GLY HIS ILE TRP          
SEQRES  18 C  455  ILE GLY LEU ILE CYS ILE ALA GLY GLY ILE TRP HIS ILE          
SEQRES  19 C  455  LEU THR THR PRO PHE GLY TRP ALA ARG ARG ALA PHE ILE          
SEQRES  20 C  455  TRP SER GLY GLU ALA TYR LEU SER TYR SER LEU GLY ALA          
SEQRES  21 C  455  LEU SER MET MET GLY PHE ILE ALA THR CYS PHE VAL TRP          
SEQRES  22 C  455  PHE ASN ASN THR VAL TYR PRO SER GLU PHE TYR GLY PRO          
SEQRES  23 C  455  THR GLY PRO GLU ALA SER GLN ALA GLN ALA MET THR PHE          
SEQRES  24 C  455  LEU ILE ARG ASP GLN LYS LEU GLY ALA ASN VAL GLY SER          
SEQRES  25 C  455  ALA GLN GLY PRO THR GLY LEU GLY LYS TYR LEU MET ARG          
SEQRES  26 C  455  SER PRO THR GLY GLU ILE ILE PHE GLY GLY GLU THR MET          
SEQRES  27 C  455  ARG PHE TRP ASP PHE ARG GLY PRO TRP LEU GLU PRO LEU          
SEQRES  28 C  455  ARG GLY PRO ASN GLY LEU ASP LEU ASN LYS ILE LYS ASN          
SEQRES  29 C  455  ASP ILE GLN PRO TRP GLN GLU ARG ARG ALA ALA GLU TYR          
SEQRES  30 C  455  MET THR HIS ALA PRO LEU GLY SER LEU ASN SER VAL GLY          
SEQRES  31 C  455  GLY VAL ALA THR GLU ILE ASN SER VAL ASN PHE VAL SER          
SEQRES  32 C  455  PRO ARG SER TRP LEU ALA THR SER HIS PHE VAL LEU ALA          
SEQRES  33 C  455  PHE PHE PHE LEU VAL GLY HIS LEU TRP HIS ALA GLY ARG          
SEQRES  34 C  455  ALA ARG ALA ALA ALA ALA GLY PHE GLU LYS GLY ILE ASP          
SEQRES  35 C  455  ARG GLU SER GLU 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   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 J   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 J   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 J   40  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  455  ASN SER ILE PHE ALA THR ASN ARG ASP GLN GLU SER SER          
SEQRES   2 c  455  GLY PHE ALA TRP TRP ALA GLY ASN ALA ARG LEU ILE ASN          
SEQRES   3 c  455  LEU SER GLY LYS LEU LEU GLY ALA HIS VAL ALA HIS ALA          
SEQRES   4 c  455  GLY LEU ILE VAL PHE TRP ALA GLY ALA MET THR LEU PHE          
SEQRES   5 c  455  GLU LEU ALA HIS PHE ILE PRO GLU LYS PRO MET TYR GLU          
SEQRES   6 c  455  GLN GLY LEU ILE LEU ILE PRO HIS ILE ALA THR LEU GLY          
SEQRES   7 c  455  TRP GLY VAL GLY PRO GLY GLY GLU VAL VAL ASP THR PHE          
SEQRES   8 c  455  PRO PHE PHE VAL VAL GLY VAL VAL HIS LEU ILE SER SER          
SEQRES   9 c  455  ALA VAL LEU GLY PHE GLY GLY VAL TYR HIS ALA ILE ARG          
SEQRES  10 c  455  GLY PRO GLU THR LEU GLU GLU TYR SER SER PHE PHE GLY          
SEQRES  11 c  455  TYR ASP TRP LYS ASP LYS ASN LYS MET THR THR ILE LEU          
SEQRES  12 c  455  GLY PHE HIS LEU ILE VAL LEU GLY ILE GLY ALA LEU LEU          
SEQRES  13 c  455  LEU VAL ALA LYS ALA MET PHE PHE GLY GLY LEU TYR ASP          
SEQRES  14 c  455  THR TRP ALA PRO GLY GLY GLY ASP VAL ARG VAL ILE THR          
SEQRES  15 c  455  ASN PRO THR LEU ASP PRO ARG VAL ILE PHE GLY TYR LEU          
SEQRES  16 c  455  LEU LYS SER PRO PHE GLY GLY GLU GLY TRP ILE VAL SER          
SEQRES  17 c  455  VAL ASN ASN LEU GLU ASP VAL VAL GLY GLY HIS ILE TRP          
SEQRES  18 c  455  ILE GLY LEU ILE CYS ILE ALA GLY GLY ILE TRP HIS ILE          
SEQRES  19 c  455  LEU THR THR PRO PHE GLY TRP ALA ARG ARG ALA PHE ILE          
SEQRES  20 c  455  TRP SER GLY GLU ALA TYR LEU SER TYR SER LEU GLY ALA          
SEQRES  21 c  455  LEU SER MET MET GLY PHE ILE ALA THR CYS PHE VAL TRP          
SEQRES  22 c  455  PHE ASN ASN THR VAL TYR PRO SER GLU PHE TYR GLY PRO          
SEQRES  23 c  455  THR GLY PRO GLU ALA SER GLN ALA GLN ALA MET THR PHE          
SEQRES  24 c  455  LEU ILE ARG ASP GLN LYS LEU GLY ALA ASN VAL GLY SER          
SEQRES  25 c  455  ALA GLN GLY PRO THR GLY LEU GLY LYS TYR LEU MET ARG          
SEQRES  26 c  455  SER PRO THR GLY GLU ILE ILE PHE GLY GLY GLU THR MET          
SEQRES  27 c  455  ARG PHE TRP ASP PHE ARG GLY PRO TRP LEU GLU PRO LEU          
SEQRES  28 c  455  ARG GLY PRO ASN GLY LEU ASP LEU ASN LYS ILE LYS ASN          
SEQRES  29 c  455  ASP ILE GLN PRO TRP GLN GLU ARG ARG ALA ALA GLU TYR          
SEQRES  30 c  455  MET THR HIS ALA PRO LEU GLY SER LEU ASN SER VAL GLY          
SEQRES  31 c  455  GLY VAL ALA THR GLU ILE ASN SER VAL ASN PHE VAL SER          
SEQRES  32 c  455  PRO ARG SER TRP LEU ALA THR SER HIS PHE VAL LEU ALA          
SEQRES  33 c  455  PHE PHE PHE LEU VAL GLY HIS LEU TRP HIS ALA GLY ARG          
SEQRES  34 c  455  ALA ARG ALA ALA ALA ALA GLY PHE GLU LYS GLY ILE ASP          
SEQRES  35 c  455  ARG GLU SER GLU 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   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 j   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 j   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 j   40  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    FE2  A 602       1                                                       
HET     CL  A 603       1                                                       
HET     CL  A 604       1                                                       
HET    BCT  A 605       4                                                       
HET    CLA  A 606      65                                                       
HET    CLA  A 607      65                                                       
HET    PHO  A 608      64                                                       
HET    CLA  A 609      65                                                       
HET    BCR  A 610      40                                                       
HET    PL9  A 611      55                                                       
HET    SQD  A 612      54                                                       
HET    SQD  A 613      54                                                       
HET    CLA  A 614      65                                                       
HET    LHG  A 615      42                                                       
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      65                                                       
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    LHG  B 621      49                                                       
HET    BCR  B 622      40                                                       
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    PHO  D 401      64                                                       
HET    CLA  D 402      65                                                       
HET    CLA  D 403      65                                                       
HET    BCR  D 404      40                                                       
HET    PL9  D 405      55                                                       
HET    DGD  D 406      62                                                       
HET    LHG  D 407      49                                                       
HET    LHG  D 408      49                                                       
HET    LHG  D 409      49                                                       
HET    HEM  E 101      43                                                       
HET    SQD  F 101      43                                                       
HET     CA  F 102       1                                                       
HET    BCR  H 101      40                                                       
HET    DGD  H 102      62                                                       
HET    BCR  K 101      40                                                       
HET    SQD  L 101      54                                                       
HET     CA  O 301       1                                                       
HET    BCR  T 101      40                                                       
HET    BCR  T 102      40                                                       
HET     CL  V 201       1                                                       
HET    HEM  V 202      43                                                       
HET    BCR  Y 101      40                                                       
HET    OEX  a 401      10                                                       
HET    SQD  a 402      54                                                       
HET    FE2  a 403       1                                                       
HET     CL  a 404       1                                                       
HET     CL  a 405       1                                                       
HET    CLA  a 406      65                                                       
HET    CLA  a 407      65                                                       
HET    CLA  a 408      65                                                       
HET    BCR  a 409      40                                                       
HET    PL9  a 410      55                                                       
HET    SQD  a 411      54                                                       
HET    PHO  a 412      64                                                       
HET    LHG  a 413      42                                                       
HET    BCT  a 414       4                                                       
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      65                                                       
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    LHG  b 620      49                                                       
HET     CA  c 901       1                                                       
HET    CLA  c 902      65                                                       
HET    CLA  c 903      65                                                       
HET    CLA  c 904      65                                                       
HET    CLA  c 905      65                                                       
HET    CLA  c 906      65                                                       
HET    CLA  c 907      65                                                       
HET    CLA  c 908      65                                                       
HET    CLA  c 909      65                                                       
HET    CLA  c 910      65                                                       
HET    CLA  c 911      65                                                       
HET    CLA  c 912      65                                                       
HET    CLA  c 913      65                                                       
HET    CLA  c 914      65                                                       
HET    BCR  c 915      40                                                       
HET    DGD  c 916      62                                                       
HET    DGD  c 917      62                                                       
HET    BCR  c 918      40                                                       
HET    CLA  d 401      65                                                       
HET    PHO  d 402      64                                                       
HET    CLA  d 403      65                                                       
HET    CLA  d 404      65                                                       
HET    PL9  d 405      55                                                       
HET    DGD  d 406      62                                                       
HET    SQD  d 407      43                                                       
HET    LHG  d 408      49                                                       
HET    LHG  d 409      49                                                       
HET    LHG  d 410      49                                                       
HET    HEM  e 101      43                                                       
HET    BCR  f 101      40                                                       
HET     CA  f 102       1                                                       
HET    BCR  h 101      40                                                       
HET    DGD  h 102      62                                                       
HET    DGD  j 101      62                                                       
HET     MG  j 102       1                                                       
HET    BCR  k 101      40                                                       
HET    BCR  k 102      40                                                       
HET    SQD  l 101      54                                                       
HET     CA  o 301       1                                                       
HET     CL  v 201       1                                                       
HET    HEM  v 202      43                                                       
HETNAM     OEX CA-MN4-O5 CLUSTER                                                
HETNAM     FE2 FE (II) ION                                                      
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     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM      CA CALCIUM ION                                                      
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  FE2    2(FE 2+)                                                     
FORMUL  41   CL    6(CL 1-)                                                     
FORMUL  43  BCT    2(C H O3 1-)                                                 
FORMUL  44  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  46  PHO    4(C55 H74 N4 O5)                                             
FORMUL  48  BCR    22(C40 H56)                                                  
FORMUL  49  PL9    4(C53 H80 O2)                                                
FORMUL  50  SQD    8(C41 H78 O12 S)                                             
FORMUL  53  LHG    10(C38 H75 O10 P)                                            
FORMUL  54   CA    7(CA 2+)                                                     
FORMUL  91  DGD    10(C51 H96 O15)                                              
FORMUL  03  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  84   MG    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 PRO B    4  ILE B   13  5                                  10    
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 GLU C  464  MET C  469  5                                   6    
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  ILE E   14  1                                   6    
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 GLU I    2  SER I   25  1                                  24    
HELIX   91 AK1 GLY I   26  ARG I   30  5                                   5    
HELIX   92 AK2 PRO J    9  TYR J   33  1                                  25    
HELIX   93 AK3 PRO K   12  ILE K   17  5                                   6    
HELIX   94 AK4 PHE K   18  LEU K   25  1                                   8    
HELIX   95 AK5 VAL K   27  VAL K   43  1                                  17    
HELIX   96 AK6 ASN L   13  ASN L   37  1                                  25    
HELIX   97 AK7 LEU M    6  SER M   31  1                                  26    
HELIX   98 AK8 THR O    6  VAL O   11  1                                   6    
HELIX   99 AK9 GLY O   14  LYS O   18  5                                   5    
HELIX  100 AL1 GLU O  179  GLU O  181  5                                   3    
HELIX  101 AL2 LEU O  182  VAL O  187  1                                   6    
HELIX  102 AL3 GLU T    2  PHE T   23  1                                  22    
HELIX  103 AL4 ASN U   11  LEU U   17  1                                   7    
HELIX  104 AL5 GLY U   18  GLU U   23  5                                   6    
HELIX  105 AL6 ASN U   31  TYR U   38  5                                   8    
HELIX  106 AL7 PRO U   43  ALA U   53  1                                  11    
HELIX  107 AL8 SER U   57  ILE U   64  5                                   8    
HELIX  108 AL9 THR U   68  ASN U   78  1                                  11    
HELIX  109 AM1 GLU U   88  GLU U   93  1                                   6    
HELIX  110 AM2 GLY U   94  ASP U   96  5                                   3    
HELIX  111 AM3 THR V   22  CYS V   37  1                                  16    
HELIX  112 AM4 CYS V   37  VAL V   42  1                                   6    
HELIX  113 AM5 GLY V   43  ILE V   45  5                                   3    
HELIX  114 AM6 ARG V   55  ALA V   62  1                                   8    
HELIX  115 AM7 ASN V   68  ASN V   78  1                                  11    
HELIX  116 AM8 PHE V  101  ARG V  105  5                                   5    
HELIX  117 AM9 THR V  108  GLY V  127  1                                  20    
HELIX  118 AN1 ASP V  128  TRP V  130  5                                   3    
HELIX  119 AN2 GLY V  133  TYR V  137  5                                   5    
HELIX  120 AN3 ILE Y   19  ARG Y   42  1                                  24    
HELIX  121 AN4 THR X    4  ASP X   35  1                                  32    
HELIX  122 AN5 THR Z    2  SER Z   29  1                                  28    
HELIX  123 AN6 ASP Z   32  ASN Z   58  1                                  27    
HELIX  124 AN7 PHE Z   59  VAL Z   61  5                                   3    
HELIX  125 AN8 ASN a   12  THR a   22  1                                  11    
HELIX  126 AN9 VAL a   30  ALA a   55  1                                  26    
HELIX  127 AO1 PRO a   95  ALA a   99  5                                   5    
HELIX  128 AO2 SER a  101  ASN a  108  1                                   8    
HELIX  129 AO3 GLY a  109  LEU a  137  1                                  29    
HELIX  130 AO4 TRP a  142  LEU a  159  1                                  18    
HELIX  131 AO5 LEU a  159  GLY a  166  1                                   8    
HELIX  132 AO6 SER a  167  GLY a  171  5                                   5    
HELIX  133 AO7 ILE a  176  ASN a  191  1                                  16    
HELIX  134 AO8 ILE a  192  MET a  194  5                                   3    
HELIX  135 AO9 HIS a  195  SER a  222  1                                  28    
HELIX  136 AP1 SER a  232  TYR a  237  5                                   6    
HELIX  137 AP2 ASN a  247  ILE a  259  1                                  13    
HELIX  138 AP3 PHE a  260  SER a  264  5                                   5    
HELIX  139 AP4 ASN a  267  ALA a  294  1                                  28    
HELIX  140 AP5 THR a  316  HIS a  332  1                                  17    
HELIX  141 AP6 PRO b    4  ILE b   13  5                                  10    
HELIX  142 AP7 ASP b   15  PHE b   45  1                                  31    
HELIX  143 AP8 PRO b   54  GLN b   58  5                                   5    
HELIX  144 AP9 VAL b   62  LEU b   69  1                                   8    
HELIX  145 AQ1 SER b   92  TYR b  117  1                                  26    
HELIX  146 AQ2 LEU b  120  ARG b  124  5                                   5    
HELIX  147 AQ3 ASP b  134  PHE b  156  1                                  23    
HELIX  148 AQ4 GLY b  186  ASN b  191  5                                   6    
HELIX  149 AQ5 ASN b  194  VAL b  219  1                                  26    
HELIX  150 AQ6 PRO b  222  LEU b  229  1                                   8    
HELIX  151 AQ7 ASN b  233  GLY b  259  1                                  27    
HELIX  152 AQ8 PRO b  264  GLY b  269  1                                   6    
HELIX  153 AQ9 THR b  271  SER b  277  1                                   7    
HELIX  154 AR1 SER b  278  SER b  294  1                                  17    
HELIX  155 AR2 THR b  297  ALA b  304  1                                   8    
HELIX  156 AR3 PRO b  306  ASP b  313  1                                   8    
HELIX  157 AR4 TYR b  314  GLY b  322  5                                   9    
HELIX  158 AR5 PRO b  329  GLY b  333  5                                   5    
HELIX  159 AR6 SER b  391  GLY b  396  1                                   6    
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 ASP b  501  ARG b  505  5                                   5    
HELIX  164 AS2 ASP c   27  GLY c   32  1                                   6    
HELIX  165 AS3 ALA c   34  ILE c   43  5                                  10    
HELIX  166 AS4 LEU c   45  PHE c   75  1                                  31    
HELIX  167 AS5 PRO c   80  GLN c   84  5                                   5    
HELIX  168 AS6 ILE c   87  LEU c   95  1                                   9    
HELIX  169 AS7 GLY c  100  GLU c  104  5                                   5    
HELIX  170 AS8 THR c  108  ARG c  135  1                                  28    
HELIX  171 AS9 ASP c  153  PHE c  182  1                                  30    
HELIX  172 AT1 ASP c  205  LEU c  214  1                                  10    
HELIX  173 AT2 GLY c  222  VAL c  227  5                                   6    
HELIX  174 AT3 ASN c  229  THR c  254  1                                  26    
HELIX  175 AT4 PHE c  257  PHE c  264  1                                   8    
HELIX  176 AT5 SER c  267  ASN c  293  1                                  27    
HELIX  177 AT6 PRO c  298  GLY c  303  1                                   6    
HELIX  178 AT7 THR c  305  GLY c  325  1                                  21    
HELIX  179 AT8 GLY c  353  TRP c  359  5                                   7    
HELIX  180 AT9 LEU c  366  PRO c  368  5                                   3    
HELIX  181 AU1 ASP c  376  ASP c  383  1                                   8    
HELIX  182 AU2 GLN c  385  THR c  397  1                                  13    
HELIX  183 AU3 SER c  421  GLY c  454  1                                  34    
HELIX  184 AU4 ASP c  460  MET c  469  5                                  10    
HELIX  185 AU5 GLY d   13  LYS d   23  1                                  11    
HELIX  186 AU6 VAL d   30  VAL d   55  1                                  26    
HELIX  187 AU7 SER d   57  GLY d   62  1                                   6    
HELIX  188 AU8 SER d   66  GLY d   70  5                                   5    
HELIX  189 AU9 ALA d   82  GLY d   86  5                                   5    
HELIX  190 AV1 ASP d  100  LEU d  107  1                                   8    
HELIX  191 AV2 GLY d  108  GLY d  137  1                                  30    
HELIX  192 AV3 PRO d  140  LEU d  158  1                                  19    
HELIX  193 AV4 LEU d  158  GLN d  164  1                                   7    
HELIX  194 AV5 SER d  166  ALA d  170  5                                   5    
HELIX  195 AV6 VAL d  175  ASN d  190  1                                  16    
HELIX  196 AV7 TRP d  191  LEU d  193  5                                   3    
HELIX  197 AV8 ASN d  194  ASN d  220  1                                  27    
HELIX  198 AV9 THR d  231  PHE d  235  5                                   5    
HELIX  199 AW1 SER d  245  PHE d  257  1                                  13    
HELIX  200 AW2 ASN d  263  ALA d  290  1                                  28    
HELIX  201 AW3 PHE d  298  ASP d  308  1                                  11    
HELIX  202 AW4 THR d  313  GLN d  334  1                                  22    
HELIX  203 AW5 PRO d  335  ASN d  338  5                                   4    
HELIX  204 AW6 PRO d  342  LEU d  346  5                                   5    
HELIX  205 AW7 PRO e    9  ILE e   14  1                                   6    
HELIX  206 AW8 SER e   16  THR e   40  1                                  25    
HELIX  207 AW9 GLY e   41  GLY e   48  1                                   8    
HELIX  208 AX1 GLU e   71  GLN e   82  1                                  12    
HELIX  209 AX2 THR f   17  GLN f   41  1                                  25    
HELIX  210 AX3 THR h    5  ARG h   12  1                                   8    
HELIX  211 AX4 PRO h   13  SER h   16  5                                   4    
HELIX  212 AX5 THR h   27  ASN h   50  1                                  24    
HELIX  213 AX6 SER h   61  LEU h   65  5                                   5    
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 GLU o  179  GLU o  181  5                                   3    
HELIX  224 AY8 LEU o  182  VAL o  187  1                                   6    
HELIX  225 AY9 GLU t    2  PHE t   23  1                                  22    
HELIX  226 AZ1 ASN u   11  LEU u   17  1                                   7    
HELIX  227 AZ2 GLY u   18  GLU u   23  5                                   6    
HELIX  228 AZ3 ASN u   31  TYR u   38  5                                   8    
HELIX  229 AZ4 PRO u   43  ALA u   53  1                                  11    
HELIX  230 AZ5 SER u   57  ILE u   64  5                                   8    
HELIX  231 AZ6 THR u   68  LEU u   79  1                                  12    
HELIX  232 AZ7 GLU u   88  GLU u   93  1                                   6    
HELIX  233 AZ8 GLY u   94  ASP u   96  5                                   3    
HELIX  234 AZ9 THR v   22  CYS v   37  1                                  16    
HELIX  235 BA1 CYS v   37  VAL v   42  1                                   6    
HELIX  236 BA2 GLY v   43  ILE v   45  5                                   3    
HELIX  237 BA3 ARG v   55  ALA v   62  1                                   8    
HELIX  238 BA4 ASN v   68  ASN v   78  1                                  11    
HELIX  239 BA5 PHE v  101  ARG v  105  5                                   5    
HELIX  240 BA6 THR v  108  GLY v  127  1                                  20    
HELIX  241 BA7 ASP v  128  TRP v  130  5                                   3    
HELIX  242 BA8 GLY v  133  TYR v  137  5                                   5    
HELIX  243 BA9 ILE y   19  ARG y   42  1                                  24    
HELIX  244 BB1 THR x    4  ASP x   35  1                                  32    
HELIX  245 BB2 THR z    2  SER z   29  1                                  28    
HELIX  246 BB3 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 MET B 166  VAL B 168  0                                        
SHEET    2 AA3 2 SER B 177  GLN B 179 -1  O  GLN B 179   N  MET B 166           
SHEET    1 AA4 6 VAL B 377  ASP B 380  0                                        
SHEET    2 AA4 6 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA4 6 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA4 6 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA4 6 THR B 398  TYR B 402 -1  O  TYR B 402   N  HIS B 343           
SHEET    6 AA4 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1 AA5 5 VAL B 377  ASP B 380  0                                        
SHEET    2 AA5 5 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA5 5 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA5 5 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA5 5 ILE B 429  ASP B 433 -1  O  GLU B 431   N  GLN B 338           
SHEET    1 AA6 2 LEU C 185  ASP C 187  0                                        
SHEET    2 AA6 2 ASP C 195  ARG C 197 -1  O  ASP C 195   N  ASP C 187           
SHEET    1 AA7 2 LEU C 341  ARG C 343  0                                        
SHEET    2 AA7 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1 AA8 2 ARG C 370  GLY C 371  0                                        
SHEET    2 AA8 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1 AA9 2 ALA D  77  VAL D  78  0                                        
SHEET    2 AA9 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1 AB1 2 TYR O  30  PRO O  31  0                                        
SHEET    2 AB1 2 SER O 135  ILE O 136 -1  O  ILE O 136   N  TYR O  30           
SHEET    1 AB210 PHE O  65  PRO O  67  0                                        
SHEET    2 AB210 TYR O  38  LYS O  53 -1  N  VAL O  52   O  VAL O  66           
SHEET    3 AB210 GLU O 232  PRO O 245 -1  O  GLN O 236   N  THR O  48           
SHEET    4 AB210 GLU O 210  LEU O 220 -1  N  ILE O 211   O  ALA O 241           
SHEET    5 AB210 LEU O 192  ASP O 205 -1  N  ASN O 200   O  THR O 214           
SHEET    6 AB210 ASP O 141  PRO O 149 -1  N  PHE O 142   O  LEU O 199           
SHEET    7 AB210 VAL O 126  SER O 128 -1  N  SER O 128   O  LYS O 143           
SHEET    8 AB210 LEU O  93  ILE O 101 -1  N  PHE O  95   O  ALA O 127           
SHEET    9 AB210 LEU O  78  VAL O  87 -1  N  LYS O  86   O  THR O  94           
SHEET   10 AB210 TYR O  38  LYS O  53 -1  N  LEU O  45   O  LEU O  78           
SHEET    1 AB3 3 LYS O  69  LEU O  70  0                                        
SHEET    2 AB3 3 PHE O 103  GLN O 109 -1  O  GLN O 109   N  LYS O  69           
SHEET    3 AB3 3 ARG O 115  THR O 121 -1  O  ILE O 116   N  VAL O 108           
SHEET    1 AB4 2 ILE U  25  ASP U  26  0                                        
SHEET    2 AB4 2 PHE U  82  THR U  83  1  O  THR U  83   N  ILE U  25           
SHEET    1 AB5 2 THR V   9  PRO V  11  0                                        
SHEET    2 AB5 2 THR V  18  THR V  20 -1  O  ILE V  19   N  VAL V  10           
SHEET    1 AB6 2 ALA a  81  VAL a  82  0                                        
SHEET    2 AB6 2 LEU a 174  GLY a 175 -1  O  LEU a 174   N  VAL a  82           
SHEET    1 AB7 2 LEU a 297  ASN a 298  0                                        
SHEET    2 AB7 2 GLY c 402  SER c 403  1  O  GLY c 402   N  ASN a 298           
SHEET    1 AB8 2 MET b 166  VAL b 168  0                                        
SHEET    2 AB8 2 SER b 177  GLN b 179 -1  O  GLN b 179   N  MET b 166           
SHEET    1 AB9 6 VAL b 377  ASP b 380  0                                        
SHEET    2 AB9 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AB9 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AB9 6 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AB9 6 THR b 398  TYR b 402 -1  O  TYR b 402   N  HIS b 343           
SHEET    6 AB9 6 THR b 410  PHE b 411 -1  O  PHE b 411   N  VAL b 399           
SHEET    1 AC1 5 VAL b 377  ASP b 380  0                                        
SHEET    2 AC1 5 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC1 5 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC1 5 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC1 5 ILE b 429  ASP b 433 -1  O  GLU b 431   N  GLN b 338           
SHEET    1 AC2 2 LEU c 185  ASP c 187  0                                        
SHEET    2 AC2 2 ASP c 195  ARG c 197 -1  O  ASP c 195   N  ASP c 187           
SHEET    1 AC3 2 LEU c 341  ARG c 343  0                                        
SHEET    2 AC3 2 ILE c 349  PHE c 351 -1  O  ILE c 350   N  MET c 342           
SHEET    1 AC4 2 ARG c 370  GLY c 371  0                                        
SHEET    2 AC4 2 GLY c 374  LEU c 375 -1  O  GLY c 374   N  GLY c 371           
SHEET    1 AC5 2 ALA d  77  VAL d  78  0                                        
SHEET    2 AC5 2 PHE d 173  GLY d 174 -1  O  PHE d 173   N  VAL d  78           
SHEET    1 AC6 2 TYR o  30  PRO o  31  0                                        
SHEET    2 AC6 2 SER o 135  ILE o 136 -1  O  ILE o 136   N  TYR o  30           
SHEET    1 AC710 PHE o  65  PRO o  67  0                                        
SHEET    2 AC710 TYR o  38  LYS o  53 -1  N  VAL o  52   O  VAL o  66           
SHEET    3 AC710 GLU o 232  PRO o 245 -1  O  GLN o 236   N  THR o  48           
SHEET    4 AC710 GLU o 210  LEU o 220 -1  N  ILE o 211   O  ALA o 241           
SHEET    5 AC710 LEU o 192  ASP o 205 -1  N  ASN o 200   O  THR o 214           
SHEET    6 AC710 ASP o 141  PRO o 149 -1  N  PHE o 142   O  LEU o 199           
SHEET    7 AC710 VAL o 126  SER o 128 -1  N  SER o 128   O  LYS o 143           
SHEET    8 AC710 LEU o  93  ILE o 101 -1  N  PHE o  95   O  ALA o 127           
SHEET    9 AC710 LEU o  78  VAL o  87 -1  N  LYS o  86   O  THR o  94           
SHEET   10 AC710 TYR o  38  LYS o  53 -1  N  LEU o  45   O  LEU o  78           
SHEET    1 AC8 3 LYS o  69  LEU o  70  0                                        
SHEET    2 AC8 3 PHE o 103  GLN o 109 -1  O  GLN o 109   N  LYS o  69           
SHEET    3 AC8 3 ARG o 115  THR o 121 -1  O  ILE o 116   N  VAL o 108           
SHEET    1 AC9 2 ILE u  25  ASP u  26  0                                        
SHEET    2 AC9 2 PHE u  82  THR u  83  1  O  THR u  83   N  ILE u  25           
SHEET    1 AD1 2 THR v   9  PRO v  11  0                                        
SHEET    2 AD1 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  2.05  
SSBOND   2 CYS o   19    CYS o   44                          1555   1555  2.03  
LINK         OD1 ASP A 170                MN4  OEX A 601     1555   1555  2.08  
LINK         OD2 ASP A 170                CA1  OEX A 601     1555   1555  2.44  
LINK         OE2 GLU A 189                MN1  OEX A 601     1555   1555  1.90  
LINK         NE2 HIS A 215                FE   FE2 A 602     1555   1555  2.16  
LINK         NE2 HIS A 272                FE   FE2 A 602     1555   1555  2.25  
LINK         NE2 HIS A 332                MN1  OEX A 601     1555   1555  2.14  
LINK         OE1 GLU A 333                MN3  OEX A 601     1555   1555  2.07  
LINK         OE2 GLU A 333                MN4  OEX A 601     1555   1555  2.17  
LINK         OD1 ASP A 342                MN2  OEX A 601     1555   1555  2.15  
LINK         OD2 ASP A 342                MN1  OEX A 601     1555   1555  2.26  
LINK         O   ALA A 344                CA1  OEX A 601     1555   1555  2.54  
LINK         OXT ALA A 344                MN2  OEX A 601     1555   1555  1.99  
LINK         OD1 ASN B 438                CA    CA B 601     1555   1555  2.65  
LINK         OD1 ASN C  39                MG   CLA C 511     1555   1555  2.11  
LINK         OE1 GLU C 354                MN2  OEX A 601     1555   1555  1.85  
LINK         OE2 GLU C 354                MN3  OEX A 601     1555   1555  1.99  
LINK         NE2 HIS D 214                FE   FE2 A 602     1555   1555  2.26  
LINK         NE2 HIS D 268                FE   FE2 A 602     1555   1555  2.29  
LINK         NE2 HIS E  23                FE   HEM E 101     1555   1555  2.10  
LINK         NE2 HIS F  24                FE   HEM E 101     1555   1555  2.10  
LINK         O   ARG F  45                CA    CA F 102     1555   1555  2.97  
LINK         OXT ARG F  45                CA    CA F 102     1555   1555  2.58  
LINK         O   THR O 138                CA    CA O 301     1555   1555  2.48  
LINK         OD1 ASN O 200                CA    CA O 301     1555   1555  2.52  
LINK         O   VAL O 201                CA    CA O 301     1555   1555  2.51  
LINK         NE2 HIS V  41                FE   HEM V 202     1555   1555  2.05  
LINK         NE2 HIS V  92                FE   HEM V 202     1555   1555  2.13  
LINK         OD1 ASP a 170                MN4  OEX a 401     1555   1555  2.03  
LINK         OD2 ASP a 170                CA1  OEX a 401     1555   1555  2.37  
LINK         OE2 GLU a 189                MN1  OEX a 401     1555   1555  1.79  
LINK         NE2 HIS a 215                FE   FE2 a 403     1555   1555  2.11  
LINK         NE2 HIS a 272                FE   FE2 a 403     1555   1555  2.32  
LINK         NE2 HIS a 332                MN1  OEX a 401     1555   1555  2.19  
LINK         OE1 GLU a 333                MN3  OEX a 401     1555   1555  1.98  
LINK         OE2 GLU a 333                MN4  OEX a 401     1555   1555  2.13  
LINK         OD1 ASP a 342                MN2  OEX a 401     1555   1555  2.13  
LINK         OD2 ASP a 342                MN1  OEX a 401     1555   1555  2.26  
LINK         O   ALA a 344                CA1  OEX a 401     1555   1555  2.46  
LINK         OXT ALA a 344                MN2  OEX a 401     1555   1555  1.89  
LINK         OD1 ASN b 438                CA    CA b 601     1555   1555  2.58  
LINK         O   PHE c  22                CA    CA c 901     1555   1555  2.42  
LINK         O   THR c  24                CA    CA c 901     1555   1555  2.39  
LINK         OD1 ASP c  27                CA    CA c 901     1555   1555  2.64  
LINK         OD2 ASP c  27                CA    CA c 901     1555   1555  2.46  
LINK         OE1 GLU c  29                CA    CA c 901     1555   1555  2.41  
LINK         OG  SER c  30                CA    CA c 901     1555   1555  2.41  
LINK         OD1 ASN c  39                MG   CLA c 912     1555   1555  1.96  
LINK         OE1 GLU c 354                MN2  OEX a 401     1555   1555  1.85  
LINK         OE2 GLU c 354                MN3  OEX a 401     1555   1555  1.89  
LINK         NE2 HIS d 214                FE   FE2 a 403     1555   1555  2.41  
LINK         NE2 HIS d 268                FE   FE2 a 403     1555   1555  2.22  
LINK         NE2 HIS e  23                FE   HEM e 101     1555   1555  2.13  
LINK         NE2 HIS f  24                FE   HEM e 101     1555   1555  2.15  
LINK         O   ARG f  45                CA    CA f 102     1555   1555  3.01  
LINK         OXT ARG f  45                CA    CA f 102     1555   1555  2.51  
LINK         O   GLY j  31                MG    MG j 102     1555   1555  2.25  
LINK         O   ALA j  34                MG    MG j 102     1555   1555  2.33  
LINK         O   LEU j  36                MG    MG j 102     1555   1555  2.28  
LINK         O   THR o 138                CA    CA o 301     1555   1555  2.28  
LINK         OD1 ASN o 200                CA    CA o 301     1555   1555  2.59  
LINK         O   VAL o 201                CA    CA o 301     1555   1555  2.51  
LINK         NE2 HIS v  41                FE   HEM v 202     1555   1555  2.05  
LINK         NE2 HIS v  92                FE   HEM v 202     1555   1555  2.09  
LINK        FE   FE2 A 602                 O3  BCT A 605     1555   1555  2.26  
LINK        FE   FE2 A 602                 O2  BCT A 605     1555   1555  2.29  
LINK        FE   FE2 a 403                 O2  BCT a 414     1555   1555  2.18  
LINK        FE   FE2 a 403                 O3  BCT a 414     1555   1555  2.24  
LINK         CD  GLN O  36                 N   SER c  20     1555   2455  1.33  
LINK         NE2 GLN O  36                 N   SER c  20     1555   2455  1.51  
LINK         CA  THR O  37                 OD1 ASN c  19     1555   2455  1.33  
LINK         C   THR O  37                 CG  ASN c  19     1555   2455  1.29  
LINK         C   THR O  37                 ND2 ASN c  19     1555   2455  1.55  
CISPEP   1 TYR U   42    PRO U   43          0         3.60                     
CISPEP   2 ALA U   53    PRO U   54          0         1.90                     
CISPEP   3 THR V   63    PRO V   64          0       -10.57                     
CISPEP   4 TYR u   42    PRO u   43          0         4.53                     
CISPEP   5 ALA u   53    PRO u   54          0         4.30                     
CISPEP   6 THR v   63    PRO v   64          0        -7.09                     
SITE     1 AC1 10 ASP A 170  VAL A 185  GLU A 189  HIS A 332                    
SITE     2 AC1 10 GLU A 333  HIS A 337  ASP A 342  ALA A 344                    
SITE     3 AC1 10 GLU C 354  ARG C 357                                          
SITE     1 AC2  5 HIS A 215  HIS A 272  BCT A 605  HIS D 214                    
SITE     2 AC2  5 HIS D 268                                                     
SITE     1 AC3  4 ASN A 181  HIS A 332  GLU A 333  LYS D 317                    
SITE     1 AC4  4 ASN A 338  PHE A 339  GLY C 353  GLU C 354                    
SITE     1 AC5  8 HIS A 215  GLU A 244  TYR A 246  HIS A 272                    
SITE     2 AC5  8 FE2 A 602  HIS D 214  TYR D 244  HIS D 268                    
SITE     1 AC6 20 TYR A 147  PRO A 150  SER A 153  VAL A 157                    
SITE     2 AC6 20 MET A 183  PHE A 186  GLN A 187  ILE A 192                    
SITE     3 AC6 20 HIS A 198  GLY A 201  PHE A 206  ALA A 286                    
SITE     4 AC6 20 ALA A 287  ILE A 290  PHO A 608  CLA A 614                    
SITE     5 AC6 20 LEU D 182  LEU D 205  CLA D 402  PHE T  17                    
SITE     1 AC7 14 GLN A 199  VAL A 202  ALA A 203  PHE A 206                    
SITE     2 AC7 14 GLY A 207  LEU A 210  TRP A 278  PHE D 157                    
SITE     3 AC7 14 VAL D 175  ILE D 178  PHE D 179  LEU D 182                    
SITE     4 AC7 14 PHO D 401  CLA D 402                                          
SITE     1 AC8 20 LEU A  41  ALA A  44  THR A  45  PHE A  48                    
SITE     2 AC8 20 TYR A 126  GLN A 130  ALA A 146  TYR A 147                    
SITE     3 AC8 20 PRO A 150  GLY A 175  PRO A 279  CLA A 606                    
SITE     4 AC8 20 CLA A 614  LEU D 205  ALA D 208  LEU D 209                    
SITE     5 AC8 20 ILE D 213  TRP D 253  PHE D 257  LHG D 408                    
SITE     1 AC9 15 ILE A  36  THR A  40  PHE A  93  PRO A  95                    
SITE     2 AC9 15 ILE A  96  TRP A  97  LEU A 114  HIS A 118                    
SITE     3 AC9 15 BCR A 610  CLA C 506  VAL I   8  TYR I   9                    
SITE     4 AC9 15 VAL I  11  VAL I  12  PHE I  15                               
SITE     1 AD1  4 ALA A  43  ILE A  96  CLA A 609  PHE I  15                    
SITE     1 AD2 18 PHE A 211  MET A 214  HIS A 215  LEU A 218                    
SITE     2 AD2 18 HIS A 252  PHE A 255  SER A 264  PHE A 265                    
SITE     3 AD2 18 LEU A 271  PHE A 274  LHG A 615  PHO D 401                    
SITE     4 AD2 18 VAL F  18  ALA F  22  THR F  25  LEU F  26                    
SITE     5 AD2 18 THR X  24  LEU X  28                                          
SITE     1 AD3 16 LEU A 200  GLY A 204  ASN A 267  SER A 270                    
SITE     2 AD3 16 PHE A 273  PHE A 274  TRP A 278  GLN C  28                    
SITE     3 AD3 16 ALA C  34  TRP C  36  CLA C 508  PHE D 232                    
SITE     4 AD3 16 ARG D 233  LHG D 409  ILE J  22  PHE K  37                    
SITE     1 AD4 12 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 AD4 12 ILE A  38  THR A  45  CLA A 614  PHE T  22                    
SITE     3 AD4 12 BCR T 101  TRP b 113  TYR b 117  BCR b 619                    
SITE     1 AD5 18 VAL A 157  MET A 172  ILE A 176  THR A 179                    
SITE     2 AD5 18 PHE A 180  PHE A 182  MET A 183  CLA A 606                    
SITE     3 AD5 18 PHO A 608  SQD A 613  LHG B 621  MET D 198                    
SITE     4 AD5 18 VAL D 201  ALA D 202  LEU D 205  GLY D 206                    
SITE     5 AD5 18 CLA D 402  PL9 D 405                                          
SITE     1 AD6 11 LEU A 258  PHE A 260  TYR A 262  PL9 A 611                    
SITE     2 AD6 11 PHE D  27  THR E   4  THR E   5  GLU E   7                    
SITE     3 AD6 11 PRO E   9  PHE E  10  SER E  11                               
SITE     1 AD7  1 ASN B 438                                                     
SITE     1 AD8  6 TRP B 185  GLY B 186  PHE B 190  CLA B 603                    
SITE     2 AD8  6 PHE H  41  BCR H 101                                          
SITE     1 AD9 19 GLY B 189  PHE B 190  GLY B 197  ALA B 200                    
SITE     2 AD9 19 HIS B 201  ALA B 204  VAL B 208  PHE B 250                    
SITE     3 AD9 19 CLA B 602  CLA B 604  CLA B 606  LEU D 158                    
SITE     4 AD9 19 PHE H  38  PHE H  41  ILE H  45  LEU H  46                    
SITE     5 AD9 19 TYR H  49  BCR H 101  DGD H 102                               
SITE     1 AE1 16 ARG B  68  LEU B  69  ALA B 146  LEU B 149                    
SITE     2 AE1 16 PHE B 153  HIS B 201  HIS B 202  PHE B 247                    
SITE     3 AE1 16 ALA B 248  VAL B 252  THR B 262  CLA B 603                    
SITE     4 AE1 16 CLA B 605  CLA B 606  CLA B 607  CLA B 611                    
SITE     1 AE2 18 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 AE2 18 LEU B 149  VAL B 245  ALA B 248  ALA B 249                    
SITE     3 AE2 18 VAL B 252  PHE B 451  HIS B 455  PHE B 458                    
SITE     4 AE2 18 PHE B 462  CLA B 604  CLA B 606  CLA B 608                    
SITE     5 AE2 18 CLA B 613  CLA B 614                                          
SITE     1 AE3 22 THR B  27  VAL B  30  TRP B  33  ALA B  34                    
SITE     2 AE3 22 VAL B  62  PHE B  65  MET B  66  ARG B  68                    
SITE     3 AE3 22 LEU B  69  VAL B  96  HIS B 100  LEU B 103                    
SITE     4 AE3 22 ALA B 205  CLA B 603  CLA B 604  CLA B 605                    
SITE     5 AE3 22 CLA B 607  CLA B 610  CLA B 611  CLA B 613                    
SITE     6 AE3 22 CLA B 616  BCR B 620                                          
SITE     1 AE4 15 LEU B  69  GLY B  70  TRP B  91  HIS B 100                    
SITE     2 AE4 15 VAL B 102  GLY B 152  PHE B 153  HIS B 157                    
SITE     3 AE4 15 PHE B 162  GLY B 163  PRO B 164  CLA B 604                    
SITE     4 AE4 15 CLA B 606  BCR B 620  SQD a 402                               
SITE     1 AE5 20 TRP B  33  TYR B  40  GLN B  58  GLY B  59                    
SITE     2 AE5 20 PHE B  61  LEU B 324  PHE B 325  THR B 327                    
SITE     3 AE5 20 GLY B 328  PRO B 329  TRP B 450  ALA B 454                    
SITE     4 AE5 20 CLA B 605  CLA B 614  BCR B 619  BCR B 622                    
SITE     5 AE5 20 PL9 D 405  PHE L  31  PHE L  35  PHE M  14                    
SITE     1 AE6 17 LEU B 229  THR B 236  SER B 239  SER B 240                    
SITE     2 AE6 17 ALA B 243  PHE B 463  HIS B 466  ILE B 467                    
SITE     3 AE6 17 THR B 473  CLA B 611  LEU D  36  PHE D 120                    
SITE     4 AE6 17 ILE D 123  MET D 126  LEU D 127  ILE D 150                    
SITE     5 AE6 17 CLA D 403                                                     
SITE     1 AE7 16 PHE B 139  VAL B 208  ALA B 212  PHE B 215                    
SITE     2 AE7 16 HIS B 216  VAL B 219  PRO B 221  PRO B 222                    
SITE     3 AE7 16 LEU B 229  CLA B 606  CLA B 611  THR H  27                    
SITE     4 AE7 16 THR H  28  MET H  31  PHE H  34  BCR H 101                    
SITE     1 AE8 15 LEU B 135  PHE B 139  HIS B 142  LEU B 143                    
SITE     2 AE8 15 ALA B 146  MET B 231  VAL B 237  SER B 240                    
SITE     3 AE8 15 SER B 241  CLA B 604  CLA B 606  CLA B 609                    
SITE     4 AE8 15 CLA B 610  CLA B 613  CLA B 616                               
SITE     1 AE9 18 TRP B   5  TYR B   6  ARG B   7  VAL B   8                    
SITE     2 AE9 18 HIS B   9  THR B  10  ILE B 242  LEU B 461                    
SITE     3 AE9 18 PHE B 462  GLY B 465  TRP B 468  HIS B 469                    
SITE     4 AE9 18 ARG B 472  CLA B 613  CLA B 614  CLA B 615                    
SITE     5 AE9 18 LHG B 621  LHG D 407                                          
SITE     1 AF1 16 HIS B   9  LEU B  19  HIS B  23  HIS B  26                    
SITE     2 AF1 16 THR B  27  ILE B 234  VAL B 237  LEU B 238                    
SITE     3 AF1 16 SER B 241  CLA B 605  CLA B 606  CLA B 611                    
SITE     4 AF1 16 CLA B 612  CLA B 614  CLA B 615  CLA B 616                    
SITE     1 AF2 13 HIS B   9  HIS B  26  VAL B  30  TRP B  33                    
SITE     2 AF2 13 PHE B 462  CLA B 605  CLA B 608  CLA B 612                    
SITE     3 AF2 13 CLA B 613  CLA B 615  BCR B 618  BCR B 619                    
SITE     4 AF2 13 LHG D 407                                                     
SITE     1 AF3 17 VAL B   8  HIS B   9  VAL B  11  ALA B  22                    
SITE     2 AF3 17 MET B  25  LEU B  29  TRP B 115  CLA B 612                    
SITE     3 AF3 17 CLA B 613  CLA B 614  BCR B 618  GLN L   8                    
SITE     4 AF3 17 VAL L  10  PHE M  21  LEU M  25  SQD l 101                    
SITE     5 AF3 17 PHE t   8                                                     
SITE     1 AF4 12 ILE B  20  HIS B  23  LEU B  24  MET B 138                    
SITE     2 AF4 12 HIS B 142  LEU B 145  CLA B 606  CLA B 611                    
SITE     3 AF4 12 CLA B 613  CLA B 617  LEU H  14  ASN H  15                    
SITE     1 AF5  8 LEU B  24  TRP B 113  HIS B 114  CLA B 616                    
SITE     2 AF5  8 BCR B 620  THR H   5  LEU H   7  GLY H   8                    
SITE     1 AF6  6 MET B  25  LEU B  29  CLA B 614  CLA B 615                    
SITE     2 AF6  6 BCR B 619  PHE t  19                                          
SITE     1 AF7 10 LEU B  29  GLY B  32  TRP B  33  SER B  36                    
SITE     2 AF7 10 VAL B 102  GLY B 105  CLA B 608  CLA B 614                    
SITE     3 AF7 10 BCR B 618  BCR B 622                                          
SITE     1 AF8  4 CLA B 606  CLA B 607  CLA B 617  PHE t  23                    
SITE     1 AF9 17 SER A 232  ASN A 234  CLA A 614  PRO B   4                    
SITE     2 AF9 17 TRP B   5  TYR B   6  CLA B 612  TRP D 266                    
SITE     3 AF9 17 PHE D 273  LHG D 407  LHG D 408  GLU L  11                    
SITE     4 AF9 17 LEU L  12  ASN L  13  SER L  16  GLY L  20                    
SITE     5 AF9 17 PHE M  21                                                     
SITE     1 AG1  9 TRP B  33  SER B  36  MET B  37  TYR B  40                    
SITE     2 AG1  9 CLA B 608  BCR B 619  SQD a 402  SQD l 101                    
SITE     3 AG1  9 PHE t  18                                                     
SITE     1 AG2 18 LEU C  95  LEU C 168  GLY C 171  ALA C 172                    
SITE     2 AG2 18 LEU C 175  ILE C 224  VAL C 233  HIS C 237                    
SITE     3 AG2 18 ILE C 240  ALA C 278  MET C 282  PHE C 289                    
SITE     4 AG2 18 TYR C 297  CLA C 502  CLA C 503  CLA C 506                    
SITE     5 AG2 18 CLA C 507  BCR C 515                                          
SITE     1 AG3 14 TRP C  63  HIS C  91  LEU C 279  MET C 282                    
SITE     2 AG3 14 ALA C 286  VAL C 290  TYR C 297  HIS C 430                    
SITE     3 AG3 14 LEU C 433  PHE C 437  CLA C 501  CLA C 503                    
SITE     4 AG3 14 CLA C 504  CLA C 510                                          
SITE     1 AG4 12 ILE C  60  VAL C  61  ALA C  64  THR C  68                    
SITE     2 AG4 12 LEU C  88  HIS C  91  VAL C 114  HIS C 118                    
SITE     3 AG4 12 CLA C 501  CLA C 502  CLA C 509  CLA C 512                    
SITE     1 AG5 17 TRP C  63  MET C  67  PHE C  70  GLN C  84                    
SITE     2 AG5 17 GLY C  85  ILE C  87  TRP C 425  SER C 429                    
SITE     3 AG5 17 PHE C 436  CLA C 502  CLA C 508  CLA C 510                    
SITE     4 AG5 17 DGD C 517  DGD C 518  LHG D 409  PRO K  26                    
SITE     5 AG5 17 VAL K  30                                                     
SITE     1 AG6 16 PHE A  33  MET A 127  GLY A 128  TRP A 131                    
SITE     2 AG6 16 PHE C 264  SER C 273  TYR C 274  GLY C 277                    
SITE     3 AG6 16 ALA C 278  HIS C 441  LEU C 442  ALA C 445                    
SITE     4 AG6 16 ARG C 449  CLA C 507  BCR C 515  PHE I  23                    
SITE     1 AG7 16 CLA A 609  LEU C 161  LEU C 165  ILE C 243                    
SITE     2 AG7 16 GLY C 247  TRP C 250  HIS C 251  THR C 254                    
SITE     3 AG7 16 THR C 255  PRO C 256  PHE C 257  TRP C 259                    
SITE     4 AG7 16 PHE C 264  CLA C 501  CLA C 507  BCR C 515                    
SITE     1 AG8 17 MET C 157  THR C 158  LEU C 161  HIS C 164                    
SITE     2 AG8 17 LEU C 168  TRP C 259  PHE C 264  TRP C 266                    
SITE     3 AG8 17 TYR C 271  TYR C 274  SER C 275  MET C 282                    
SITE     4 AG8 17 CLA C 501  CLA C 505  CLA C 506  CLA C 509                    
SITE     5 AG8 17 BCR C 515                                                     
SITE     1 AG9 20 SQD A 612  TRP C  36  ALA C  37  GLY C  38                    
SITE     2 AG9 20 ASN C  39  ALA C  40  GLU C 269  LEU C 272                    
SITE     3 AG9 20 LEU C 276  PHE C 436  PHE C 437  GLY C 440                    
SITE     4 AG9 20 TRP C 443  HIS C 444  ARG C 447  CLA C 504                    
SITE     5 AG9 20 CLA C 509  CLA C 510  CLA C 511  LHG D 409                    
SITE     1 AH1 16 ASN C  39  LEU C  49  ALA C  52  HIS C  53                    
SITE     2 AH1 16 HIS C  56  TYR C 149  GLY C 268  GLU C 269                    
SITE     3 AH1 16 TYR C 271  LEU C 272  SER C 275  CLA C 503                    
SITE     4 AH1 16 CLA C 507  CLA C 508  CLA C 510  CLA C 511                    
SITE     1 AH2 15 ASN C  39  HIS C  56  LEU C  59  TRP C  63                    
SITE     2 AH2 15 LEU C 279  PHE C 436  PHE C 437  CLA C 502                    
SITE     3 AH2 15 CLA C 504  CLA C 508  CLA C 509  CLA C 511                    
SITE     4 AH2 15 LHG D 409  PRO K  29  LEU K  33                               
SITE     1 AH3 27 THR C  24  ARG C  26  TRP C  35  GLY C  38                    
SITE     2 AH3 27 ASN C  39  ARG C  41  LEU C  42  LEU C  45                    
SITE     3 AH3 27 LYS C  48  ALA C  52  PHE C 127  ILE C 134                    
SITE     4 AH3 27 CLA C 508  CLA C 509  CLA C 510  PHE K  32                    
SITE     5 AH3 27 LEU K  33  ALA K  36  TRP K  39  GLN K  40                    
SITE     6 AH3 27 BCR K 101  LEU Y  39  ASN Y  45  LEU Y  46                    
SITE     7 AH3 27 VAL Z  20  VAL Z  23  ALA Z  28                               
SITE     1 AH4 12 HIS C  53  ALA C  57  LEU C 125  PHE C 146                    
SITE     2 AH4 12 PHE C 147  PHE C 163  HIS C 164  VAL C 167                    
SITE     3 AH4 12 GLY C 171  CLA C 503  CLA C 513  BCR C 514                    
SITE     1 AH5 10 LEU C  50  VAL C 124  GLY C 128  TYR C 131                    
SITE     2 AH5 10 HIS C 132  PRO C 137  TYR C 143  PHE C 147                    
SITE     3 AH5 10 CLA C 512  BCR C 514                                          
SITE     1 AH6 10 PHE C 112  VAL C 116  SER C 121  VAL C 124                    
SITE     2 AH6 10 PHE C 147  CLA C 512  CLA C 513  TYR K  15                    
SITE     3 AH6 10 VAL Z  51  GLY Z  55                                          
SITE     1 AH7 11 ILE C 209  LEU C 213  ILE C 224  GLY C 236                    
SITE     2 AH7 11 HIS C 237  PHE C 264  CLA C 501  CLA C 505                    
SITE     3 AH7 11 CLA C 506  CLA C 507  PHE I  23                               
SITE     1 AH8 19 LEU A  91  SER A 148  ILE A 163  PRO C 217                    
SITE     2 AH8 19 GLY C 219  GLY C 220  GLU C 221  GLY C 222                    
SITE     3 AH8 19 TRP C 223  VAL C 227  PHE C 284  CYS C 288                    
SITE     4 AH8 19 PHE C 292  ASN C 293  ASN C 294  THR C 295                    
SITE     5 AH8 19 ASP C 360  PHE C 361  ARG C 362                               
SITE     1 AH9 15 HIS A 195  PHE A 197  GLU C  83  GLN C  84                    
SITE     2 AH9 15 GLY C  85  LEU C 404  SER C 406  ASN C 418                    
SITE     3 AH9 15 PHE C 419  VAL C 420  TRP C 425  CLA C 504                    
SITE     4 AH9 15 DGD C 518  PHE J  29  TYR J  33                               
SITE     1 AI1 19 GLN A 199  PHE A 300  ASN A 301  PHE A 302                    
SITE     2 AI1 19 SER A 305  ASN C 405  VAL C 407  ASN C 415                    
SITE     3 AI1 19 SER C 416  ASN C 418  CLA C 504  DGD C 517                    
SITE     4 AI1 19 LHG D 409  PHE J  29  ALA J  32  TYR J  33                    
SITE     5 AI1 19 GLY J  37  SER J  38  SER J  39                               
SITE     1 AI2 21 PHE A 206  ALA A 209  LEU A 210  MET A 214                    
SITE     2 AI2 21 LEU A 258  CLA A 607  PL9 A 611  ALA D  41                    
SITE     3 AI2 21 LEU D  45  TRP D  48  ILE D 114  GLY D 121                    
SITE     4 AI2 21 LEU D 122  PHE D 125  GLN D 129  ASN D 142                    
SITE     5 AI2 21 PHE D 146  PRO D 149  GLY D 174  LEU D 279                    
SITE     6 AI2 21 CLA D 402                                                     
SITE     1 AI3 23 MET A 183  PHE A 206  CLA A 606  CLA A 607                    
SITE     2 AI3 23 CLA A 614  PRO D 149  VAL D 152  SER D 155                    
SITE     3 AI3 23 VAL D 156  PHE D 181  LEU D 182  PHE D 185                    
SITE     4 AI3 23 GLN D 186  TRP D 191  THR D 192  HIS D 197                    
SITE     5 AI3 23 GLY D 200  VAL D 204  LEU D 205  SER D 282                    
SITE     6 AI3 23 ALA D 283  VAL D 286  PHO D 401                               
SITE     1 AI4 18 CLA B 609  ILE D  35  LEU D  36  PRO D  39                    
SITE     2 AI4 18 CYS D  40  LEU D  43  LEU D  89  LEU D  90                    
SITE     3 AI4 18 LEU D  91  LEU D  92  TRP D  93  TRP D 104                    
SITE     4 AI4 18 THR D 112  PHE D 113  LEU D 116  HIS D 117                    
SITE     5 AI4 18 GLY X  13  ALA X  18                                          
SITE     1 AI5 10 TYR D  42  LEU D  43  GLY D  46  GLY D  47                    
SITE     2 AI5 10 LEU D  49  THR D  50  PRO F  29  THR F  30                    
SITE     3 AI5 10 VAL J  21  VAL J  25                                          
SITE     1 AI6 21 PHE A  52  ILE A  53  CLA A 614  CLA B 608                    
SITE     2 AI6 21 MET D 198  MET D 199  ALA D 202  HIS D 214                    
SITE     3 AI6 21 THR D 217  TRP D 253  ALA D 260  PHE D 261                    
SITE     4 AI6 21 LEU D 267  PHE D 270  PHE D 273  VAL D 274                    
SITE     5 AI6 21 LHG D 408  LEU L  23  VAL L  26  LEU L  29                    
SITE     6 AI6 21 PHE T  10                                                     
SITE     1 AI7  6 GLY D  99  ASP D 100  PHE D 101  THR D 102                    
SITE     2 AI7  6 PHE E  37  ASP E  45                                          
SITE     1 AI8 18 SER A 232  ASN A 234  TRP B   5  TYR B   6                    
SITE     2 AI8 18 ARG B   7  LEU B 461  PHE B 464  TRP B 468                    
SITE     3 AI8 18 CLA B 612  CLA B 614  LHG B 621  TYR D 141                    
SITE     4 AI8 18 ILE D 144  TRP D 266  PHE D 269  THR D 277                    
SITE     5 AI8 18 LEU L  23  ILE L  24                                          
SITE     1 AI9 20 MET A  37  PHO A 608  LHG B 621  ILE D 256                    
SITE     2 AI9 20 PHE D 257  ALA D 260  PHE D 261  SER D 262                    
SITE     3 AI9 20 ASN D 263  TRP D 266  PHE D 270  PL9 D 405                    
SITE     4 AI9 20 ASN L  13  THR L  15  SER L  16  TYR L  18                    
SITE     5 AI9 20 LEU L  19  PHE T  10  PHE T  17  ALA T  20                    
SITE     1 AJ1 18 ARG A 140  TRP A 142  PHE A 273  SQD A 612                    
SITE     2 AJ1 18 PHE C  33  TRP C  36  TRP C 443  ARG C 447                    
SITE     3 AJ1 18 CLA C 504  CLA C 508  CLA C 510  DGD C 518                    
SITE     4 AJ1 18 GLU D 219  ASN D 220  ALA D 229  SER D 230                    
SITE     5 AJ1 18 THR D 231  PHE D 232                                          
SITE     1 AJ2 13 PHE E  10  ARG E  18  TYR E  19  HIS E  23                    
SITE     2 AJ2 13 THR E  26  ILE E  27  LEU E  30  ARG F  19                    
SITE     3 AJ2 13 TRP F  20  VAL F  23  HIS F  24  ALA F  27                    
SITE     4 AJ2 13 ILE F  31                                                     
SITE     1 AJ3  7 ARG D  24  ARG D  26  PHE F  16  THR F  17                    
SITE     2 AJ3  7 VAL F  18  ILE X  31  ASP X  35                               
SITE     1 AJ4  1 ARG F  45                                                     
SITE     1 AJ5  6 CLA B 602  CLA B 603  CLA B 610  PHE H  34                    
SITE     2 AJ5  6 MET H  35  PHE H  38                                          
SITE     1 AJ6 18 TYR B 193  PHE B 250  TYR B 258  TYR B 273                    
SITE     2 AJ6 18 GLN B 274  SER B 277  TYR B 279  CLA B 603                    
SITE     3 AJ6 18 HIS D  87  LEU D 162  GLY D 163  LEU D 291                    
SITE     4 AJ6 18 LEU H  46  TYR H  49  ASN H  50  VAL H  60                    
SITE     5 AJ6 18 SER H  61  TRP H  62                                          
SITE     1 AJ7 10 ALA C  55  GLY C  58  LEU C  59  SER C 122                    
SITE     2 AJ7 10 GLY C 126  CLA C 511  TYR K  15  PHE K  32                    
SITE     3 AJ7 10 BCR Y 101  SER Z  16                                          
SITE     1 AJ8 12 ARG L  14  TYR L  18  LEU M  16  CYS T  12                    
SITE     2 AJ8 12 PHE T  19  PHE T  23  BCR T 102  ARG b  18                    
SITE     3 AJ8 12 SER b 104  PHE b 108  TRP b 115  ARG l   7                    
SITE     1 AJ9  3 THR O 138  ASN O 200  VAL O 201                               
SITE     1 AK1  6 SQD A 613  PHE T  18  TRP b  33  MET b  37                    
SITE     2 AK1  6 TYR b  40  BCR b 618                                          
SITE     1 AK2  8 SQD L 101  PHE T  19  MET b  25  TRP b 115                    
SITE     2 AK2  8 CLA b 608  CLA b 614  CLA b 615  BCR b 618                    
SITE     1 AK3 20 ALA V  36  CYS V  37  CYS V  40  HIS V  41                    
SITE     2 AK3 20 THR V  46  THR V  48  LEU V  52  ASP V  53                    
SITE     3 AK3 20 LEU V  54  THR V  58  LEU V  59  ALA V  62                    
SITE     4 AK3 20 LEU V  72  TYR V  75  MET V  76  TYR V  82                    
SITE     5 AK3 20 ILE V  88  HIS V  92  PRO V  93  ILE V 115                    
SITE     1 AK4 14 PHE C  62  THR J  15  GLY J  18  MET J  19                    
SITE     2 AK4 14 LEU K  31  ALA K  34  PHE K  37  VAL K  38                    
SITE     3 AK4 14 BCR K 101  ILE Y  28  GLY Y  29  GLY Y  32                    
SITE     4 AK4 14 PRO Y  33  PHE Z  17                                          
SITE     1 AK5 11 ASP a  61  ASP a 170  VAL a 185  GLU a 189                    
SITE     2 AK5 11 HIS a 332  GLU a 333  HIS a 337  ASP a 342                    
SITE     3 AK5 11 ALA a 344  GLU c 354  ARG c 357                               
SITE     1 AK6 11 TRP B 113  TYR B 117  CLA B 607  BCR B 622                    
SITE     2 AK6 11 TRP a  20  ASN a  26  ARG a  27  LEU a  28                    
SITE     3 AK6 11 LEU a  42  THR a  45  PHE t  22                               
SITE     1 AK7  5 HIS a 215  HIS a 272  BCT a 414  HIS d 214                    
SITE     2 AK7  5 HIS d 268                                                     
SITE     1 AK8  4 ASN a 181  HIS a 332  GLU a 333  LYS d 317                    
SITE     1 AK9  5 HIS a 337  ASN a 338  PHE a 339  GLY c 353                    
SITE     2 AK9  5 GLU c 354                                                     
SITE     1 AL1 19 TYR a 147  PRO a 150  SER a 153  VAL a 157                    
SITE     2 AL1 19 MET a 183  PHE a 186  GLN a 187  HIS a 198                    
SITE     3 AL1 19 GLY a 201  PHE a 206  ALA a 286  ALA a 287                    
SITE     4 AL1 19 ILE a 290  LEU d 182  LEU d 205  CLA d 401                    
SITE     5 AL1 19 PHO d 402  CLA d 403  PHE t  17                               
SITE     1 AL2 13 GLN a 199  VAL a 202  ALA a 203  PHE a 206                    
SITE     2 AL2 13 GLY a 207  LEU a 210  TRP a 278  PHO a 412                    
SITE     3 AL2 13 PHE d 157  VAL d 175  ILE d 178  PHE d 179                    
SITE     4 AL2 13 CLA d 403                                                     
SITE     1 AL3 20 ILE a  36  THR a  40  PHE a  93  PRO a  95                    
SITE     2 AL3 20 ILE a  96  TRP a  97  GLN a 113  LEU a 114                    
SITE     3 AL3 20 HIS a 118  LEU a 121  BCR a 409  CLA c 906                    
SITE     4 AL3 20 CLA c 907  VAL i   8  TYR i   9  VAL i  11                    
SITE     5 AL3 20 VAL i  12  THR i  13  PHE i  15  PHE i  19                    
SITE     1 AL4  4 ALA a  43  ILE a  50  ILE a  96  CLA a 408                    
SITE     1 AL5 19 PHE a 211  MET a 214  HIS a 215  LEU a 218                    
SITE     2 AL5 19 HIS a 252  PHE a 255  ALA a 263  SER a 264                    
SITE     3 AL5 19 PHE a 265  LEU a 271  PHE a 274  LHG a 413                    
SITE     4 AL5 19 TYR d  42  SQD d 407  VAL f  18  ALA f  22                    
SITE     5 AL5 19 THR f  25  THR x  24  LEU x  28                               
SITE     1 AL6 14 LEU a 200  GLY a 204  PHE a 265  ASN a 267                    
SITE     2 AL6 14 SER a 270  PHE a 273  TRP a 278  GLN c  28                    
SITE     3 AL6 14 ALA c  34  TRP c  36  CLA c 909  PHE d 232                    
SITE     4 AL6 14 ARG d 233  LHG d 410                                          
SITE     1 AL7 21 PHE a 206  ALA a 209  LEU a 210  MET a 214                    
SITE     2 AL7 21 CLA a 407  ALA d  41  TRP d  48  ILE d 114                    
SITE     3 AL7 21 GLY d 121  LEU d 122  PHE d 125  GLN d 129                    
SITE     4 AL7 21 ASN d 142  ALA d 145  PHE d 146  PRO d 149                    
SITE     5 AL7 21 PHE d 153  GLY d 174  PRO d 275  LEU d 279                    
SITE     6 AL7 21 CLA d 403                                                     
SITE     1 AL8 13 LEU a 258  ILE a 259  PHE a 260  TYR a 262                    
SITE     2 AL8 13 PL9 a 410  PHE d  27  THR e   4  THR e   5                    
SITE     3 AL8 13 GLU e   7  PRO e   9  PHE e  10  SER e  11                    
SITE     4 AL8 13 ARG f  19                                                     
SITE     1 AL9  7 HIS a 215  GLU a 244  HIS a 272  FE2 a 403                    
SITE     2 AL9  7 HIS d 214  TYR d 244  HIS d 268                               
SITE     1 AM1  1 ASN b 438                                                     
SITE     1 AM2  6 TRP b 185  GLY b 186  PHE b 190  CLA b 603                    
SITE     2 AM2  6 PHE h  41  BCR h 101                                          
SITE     1 AM3 19 GLY b 189  PHE b 190  PRO b 192  GLY b 197                    
SITE     2 AM3 19 HIS b 201  ALA b 204  VAL b 208  PHE b 246                    
SITE     3 AM3 19 PHE b 247  PHE b 250  VAL b 251  CLA b 602                    
SITE     4 AM3 19 CLA b 604  CLA b 606  PHE h  38  PHE h  41                    
SITE     5 AM3 19 ILE h  45  LEU h  46  TYR h  49                               
SITE     1 AM4 12 ARG b  68  LEU b  69  ALA b 146  PHE b 153                    
SITE     2 AM4 12 HIS b 201  HIS b 202  VAL b 252  THR b 262                    
SITE     3 AM4 12 CLA b 603  CLA b 605  CLA b 606  CLA b 607                    
SITE     1 AM5 21 TRP b  33  PHE b  61  PHE b  65  ARG b  68                    
SITE     2 AM5 21 LEU b 149  VAL b 245  ALA b 248  ALA b 249                    
SITE     3 AM5 21 VAL b 252  PHE b 451  HIS b 455  PHE b 458                    
SITE     4 AM5 21 PHE b 462  CLA b 604  CLA b 606  CLA b 607                    
SITE     5 AM5 21 CLA b 608  CLA b 612  CLA b 613  CLA b 614                    
SITE     6 AM5 21 CLA b 616                                                     
SITE     1 AM6 18 THR b  27  TRP b  33  ALA b  34  VAL b  62                    
SITE     2 AM6 18 PHE b  65  MET b  66  ARG b  68  LEU b  69                    
SITE     3 AM6 18 VAL b  96  HIS b 100  ALA b 205  CLA b 603                    
SITE     4 AM6 18 CLA b 604  CLA b 605  CLA b 607  CLA b 611                    
SITE     5 AM6 18 CLA b 616  BCR b 619                                          
SITE     1 AM7 13 LEU b  69  GLY b  70  TRP b  91  VAL b  96                    
SITE     2 AM7 13 VAL b 102  HIS b 157  PHE b 162  GLY b 163                    
SITE     3 AM7 13 PRO b 164  CLA b 604  CLA b 605  CLA b 606                    
SITE     4 AM7 13 BCR b 619                                                     
SITE     1 AM8 21 BCR T 102  TRP b  33  MET b  37  TYR b  40                    
SITE     2 AM8 21 GLN b  58  GLY b  59  PHE b  61  LEU b 324                    
SITE     3 AM8 21 PHE b 325  THR b 327  GLY b 328  PRO b 329                    
SITE     4 AM8 21 TRP b 450  PHE b 451  ALA b 454  CLA b 605                    
SITE     5 AM8 21 CLA b 614  BCR b 618  PL9 d 405  PHE l  31                    
SITE     6 AM8 21 PHE m  14                                                     
SITE     1 AM9 16 THR b 236  SER b 239  SER b 240  ALA b 243                    
SITE     2 AM9 16 PHE b 463  HIS b 466  ILE b 467  THR b 473                    
SITE     3 AM9 16 LEU b 474  CLA b 611  PHE d 120  ILE d 123                    
SITE     4 AM9 16 MET d 126  LEU d 127  ILE d 150  CLA d 404                    
SITE     1 AN1 14 PHE b 139  VAL b 208  ALA b 212  PHE b 215                    
SITE     2 AN1 14 HIS b 216  VAL b 219  PRO b 221  PRO b 222                    
SITE     3 AN1 14 LEU b 229  CLA b 611  THR h  27  MET h  31                    
SITE     4 AN1 14 PHE h  34  BCR h 101                                          
SITE     1 AN2 14 LEU b 135  MET b 138  PHE b 139  HIS b 142                    
SITE     2 AN2 14 LEU b 143  MET b 231  VAL b 237  SER b 240                    
SITE     3 AN2 14 SER b 241  CLA b 606  CLA b 609  CLA b 610                    
SITE     4 AN2 14 CLA b 613  CLA b 616                                          
SITE     1 AN3 21 TRP b   5  TYR b   6  ARG b   7  VAL b   8                    
SITE     2 AN3 21 HIS b   9  THR b  10  LEU b 238  ILE b 242                    
SITE     3 AN3 21 LEU b 461  PHE b 462  GLY b 465  TRP b 468                    
SITE     4 AN3 21 HIS b 469  ARG b 472  CLA b 605  CLA b 613                    
SITE     5 AN3 21 CLA b 614  CLA b 615  LHG b 620  LHG d 408                    
SITE     6 AN3 21 PHE m  21                                                     
SITE     1 AN4 16 HIS b   9  LEU b  19  HIS b  23  HIS b  26                    
SITE     2 AN4 16 THR b  27  ILE b 234  VAL b 237  LEU b 238                    
SITE     3 AN4 16 SER b 241  ILE b 242  CLA b 605  CLA b 611                    
SITE     4 AN4 16 CLA b 612  CLA b 614  CLA b 615  CLA b 616                    
SITE     1 AN5 12 BCR T 102  HIS b   9  HIS b  26  VAL b  30                    
SITE     2 AN5 12 TRP b  33  PHE b 462  CLA b 605  CLA b 608                    
SITE     3 AN5 12 CLA b 612  CLA b 613  CLA b 615  LHG d 408                    
SITE     1 AN6 14 BCR T 102  VAL b   8  HIS b   9  VAL b  11                    
SITE     2 AN6 14 MET b  25  LEU b  29  TRP b 115  CLA b 612                    
SITE     3 AN6 14 CLA b 613  CLA b 614  VAL l  10  LEU m  13                    
SITE     4 AN6 14 PHE m  21  LEU m  25                                          
SITE     1 AN7 13 ILE b  20  HIS b  23  MET b 138  HIS b 142                    
SITE     2 AN7 13 LEU b 145  CLA b 605  CLA b 606  CLA b 611                    
SITE     3 AN7 13 CLA b 613  CLA b 617  LEU h   7  LEU h  14                    
SITE     4 AN7 13 ASN h  15                                                     
SITE     1 AN8  9 LEU b  24  TRP b 113  HIS b 114  LEU b 120                    
SITE     2 AN8  9 CLA b 616  BCR b 619  THR h   5  LEU h   7                    
SITE     3 AN8  9 GLY h   8                                                     
SITE     1 AN9  9 BCR T 101  BCR T 102  LEU b  29  GLY b  32                    
SITE     2 AN9  9 TRP b  33  SER b  36  VAL b 102  GLY b 105                    
SITE     3 AN9  9 CLA b 608                                                     
SITE     1 AO1  6 SQD A 613  PHE T  18  PHE T  22  CLA b 606                    
SITE     2 AO1  6 CLA b 607  CLA b 617                                          
SITE     1 AO2 18 SER a 232  ASN a 234  PRO b   4  TRP b   5                    
SITE     2 AO2 18 TYR b   6  CLA b 612  TRP d 266  PHE d 273                    
SITE     3 AO2 18 CLA d 401  LHG d 408  LHG d 409  GLU l  11                    
SITE     4 AO2 18 LEU l  12  ASN l  13  SER l  16  GLY l  20                    
SITE     5 AO2 18 PRO m  18  PHE m  21                                          
SITE     1 AO3  5 PHE c  22  THR c  24  ASP c  27  GLU c  29                    
SITE     2 AO3  5 SER c  30                                                     
SITE     1 AO4 17 LEU c  95  LEU c 168  GLY c 171  ALA c 172                    
SITE     2 AO4 17 ILE c 224  VAL c 233  HIS c 237  ILE c 240                    
SITE     3 AO4 17 ALA c 278  MET c 282  PHE c 289  VAL c 296                    
SITE     4 AO4 17 TYR c 297  CLA c 903  CLA c 904  CLA c 907                    
SITE     5 AO4 17 BCR c 915                                                     
SITE     1 AO5 17 TRP c  63  ILE c  87  HIS c  91  LEU c 174                    
SITE     2 AO5 17 LEU c 279  MET c 282  ALA c 286  VAL c 290                    
SITE     3 AO5 17 TYR c 297  HIS c 430  LEU c 433  PHE c 437                    
SITE     4 AO5 17 CLA c 902  CLA c 904  CLA c 905  CLA c 911                    
SITE     5 AO5 17 CLA c 913                                                     
SITE     1 AO6 11 ILE c  60  VAL c  61  ALA c  64  THR c  68                    
SITE     2 AO6 11 LEU c  88  HIS c  91  VAL c 114  HIS c 118                    
SITE     3 AO6 11 CLA c 902  CLA c 903  CLA c 910                               
SITE     1 AO7 17 TRP c  63  MET c  67  PHE c  70  GLN c  84                    
SITE     2 AO7 17 GLY c  85  ILE c  87  TRP c 425  SER c 429                    
SITE     3 AO7 17 PHE c 436  CLA c 903  CLA c 909  CLA c 911                    
SITE     4 AO7 17 DGD c 917  LHG d 410  DGD j 101  PRO k  26                    
SITE     5 AO7 17 VAL k  30                                                     
SITE     1 AO8 21 PHE a  33  LEU a 121  SER a 124  CYS a 125                    
SITE     2 AO8 21 MET a 127  GLY a 128  TRP a 131  CLA a 408                    
SITE     3 AO8 21 PHE c 264  SER c 273  TYR c 274  GLY c 277                    
SITE     4 AO8 21 ALA c 278  MET c 281  HIS c 441  LEU c 442                    
SITE     5 AO8 21 ALA c 445  ARG c 449  CLA c 908  BCR c 915                    
SITE     6 AO8 21 PHE i  23                                                     
SITE     1 AO9 16 CLA a 408  LEU c 161  LEU c 165  ILE c 243                    
SITE     2 AO9 16 GLY c 247  TRP c 250  HIS c 251  THR c 254                    
SITE     3 AO9 16 THR c 255  PRO c 256  PHE c 257  TRP c 259                    
SITE     4 AO9 16 PHE c 264  CLA c 902  CLA c 908  BCR c 915                    
SITE     1 AP1 16 MET c 157  THR c 158  LEU c 161  HIS c 164                    
SITE     2 AP1 16 LEU c 168  PHE c 264  TRP c 266  TYR c 271                    
SITE     3 AP1 16 TYR c 274  SER c 275  LEU c 279  MET c 282                    
SITE     4 AP1 16 CLA c 906  CLA c 907  CLA c 910  BCR c 915                    
SITE     1 AP2 18 SQD a 411  TRP c  36  ALA c  37  GLY c  38                    
SITE     2 AP2 18 ASN c  39  ALA c  40  LEU c 276  PHE c 436                    
SITE     3 AP2 18 PHE c 437  GLY c 440  TRP c 443  HIS c 444                    
SITE     4 AP2 18 ARG c 447  CLA c 905  CLA c 910  CLA c 911                    
SITE     5 AP2 18 CLA c 912  LHG d 410                                          
SITE     1 AP3 19 ASN c  39  LEU c  49  ALA c  52  HIS c  53                    
SITE     2 AP3 19 HIS c  56  TYR c 149  TRP c 151  GLY c 268                    
SITE     3 AP3 19 GLU c 269  TYR c 271  LEU c 272  SER c 275                    
SITE     4 AP3 19 LEU c 276  CLA c 904  CLA c 908  CLA c 909                    
SITE     5 AP3 19 CLA c 911  CLA c 912  CLA c 913                               
SITE     1 AP4 16 ASN c  39  HIS c  56  LEU c  59  TRP c  63                    
SITE     2 AP4 16 LEU c 279  PHE c 436  PHE c 437  CLA c 903                    
SITE     3 AP4 16 CLA c 905  CLA c 909  CLA c 910  CLA c 912                    
SITE     4 AP4 16 LHG d 410  PRO k  29  VAL k  30  LEU k  33                    
SITE     1 AP5 26 ARG c  26  TRP c  35  GLY c  38  ASN c  39                    
SITE     2 AP5 26 ARG c  41  LEU c  42  LEU c  45  LYS c  48                    
SITE     3 AP5 26 ALA c  52  ALA c 123  PHE c 127  ILE c 134                    
SITE     4 AP5 26 CLA c 909  CLA c 910  CLA c 911  PHE k  32                    
SITE     5 AP5 26 LEU k  33  ALA k  36  TRP k  39  GLN k  40                    
SITE     6 AP5 26 BCR k 102  ILE y  35  ILE y  36  LEU y  39                    
SITE     7 AP5 26 VAL z  20  ALA z  28                                          
SITE     1 AP6 14 HIS c  53  ALA c  57  LEU c 125  PHE c 146                    
SITE     2 AP6 14 PHE c 147  TYR c 149  PHE c 163  HIS c 164                    
SITE     3 AP6 14 VAL c 167  GLY c 171  CLA c 903  CLA c 910                    
SITE     4 AP6 14 CLA c 914  BCR c 918                                          
SITE     1 AP7  9 LEU c  50  VAL c 124  GLY c 128  TYR c 131                    
SITE     2 AP7  9 HIS c 132  TYR c 143  PHE c 147  CLA c 913                    
SITE     3 AP7  9 BCR c 918                                                     
SITE     1 AP8 12 ILE c 209  LEU c 213  GLY c 236  HIS c 237                    
SITE     2 AP8 12 ILE c 240  PHE c 264  CLA c 902  CLA c 906                    
SITE     3 AP8 12 CLA c 907  CLA c 908  PHE i  23  LEU i  24                    
SITE     1 AP9 21 LEU a  91  SER a 148  PHE a 155  ILE a 163                    
SITE     2 AP9 21 PRO c 217  PHE c 218  GLY c 219  GLY c 220                    
SITE     3 AP9 21 GLU c 221  GLY c 222  TRP c 223  VAL c 227                    
SITE     4 AP9 21 MET c 281  CYS c 288  PHE c 292  ASN c 293                    
SITE     5 AP9 21 ASN c 294  THR c 295  ASP c 360  PHE c 361                    
SITE     6 AP9 21 ARG c 362                                                     
SITE     1 AQ1 13 PHE a 197  GLU c  83  GLN c  84  GLY c  85                    
SITE     2 AQ1 13 SER c 406  ASN c 418  PHE c 419  VAL c 420                    
SITE     3 AQ1 13 TRP c 425  THR c 428  CLA c 905  TYR j  33                    
SITE     4 AQ1 13 DGD j 101                                                     
SITE     1 AQ2 12 PHE c 112  VAL c 116  ILE c 120  SER c 121                    
SITE     2 AQ2 12 VAL c 124  CLA c 913  CLA c 914  TYR k  15                    
SITE     3 AQ2 12 VAL z  51  GLY z  55  ASN z  58  PHE z  59                    
SITE     1 AQ3 17 VAL a 157  MET a 172  ILE a 176  THR a 179                    
SITE     2 AQ3 17 PHE a 180  MET a 183  CLA a 406  LHG b 620                    
SITE     3 AQ3 17 MET d 198  VAL d 201  ALA d 202  LEU d 205                    
SITE     4 AQ3 17 GLY d 206  PHO d 402  CLA d 403  PL9 d 405                    
SITE     5 AQ3 17 LEU l  30                                                     
SITE     1 AQ4 19 LEU a  41  ALA a  44  THR a  45  PHE a  48                    
SITE     2 AQ4 19 TYR a 126  GLN a 130  ALA a 146  TYR a 147                    
SITE     3 AQ4 19 PRO a 150  PRO a 279  CLA a 406  LEU d 205                    
SITE     4 AQ4 19 ALA d 208  LEU d 209  ILE d 213  TRP d 253                    
SITE     5 AQ4 19 PHE d 257  CLA d 401  LHG d 409                               
SITE     1 AQ5 23 MET a 183  PHE a 206  CLA a 406  CLA a 407                    
SITE     2 AQ5 23 PHO a 412  PRO d 149  VAL d 152  SER d 155                    
SITE     3 AQ5 23 VAL d 156  PHE d 181  LEU d 182  PHE d 185                    
SITE     4 AQ5 23 GLN d 186  TRP d 191  THR d 192  HIS d 197                    
SITE     5 AQ5 23 GLY d 200  VAL d 204  LEU d 205  SER d 282                    
SITE     6 AQ5 23 ALA d 283  VAL d 286  CLA d 401                               
SITE     1 AQ6 20 CLA b 609  ILE d  35  PRO d  39  CYS d  40                    
SITE     2 AQ6 20 LEU d  43  LEU d  89  LEU d  90  LEU d  91                    
SITE     3 AQ6 20 LEU d  92  TRP d  93  TRP d 104  THR d 112                    
SITE     4 AQ6 20 PHE d 113  LEU d 116  HIS d 117  VAL h  33                    
SITE     5 AQ6 20 GLY x  13  LEU x  14  GLY x  17  ALA x  18                    
SITE     1 AQ7 18 PHE a  52  ILE a  53  CLA b 608  MET d 198                    
SITE     2 AQ7 18 MET d 199  ALA d 202  HIS d 214  THR d 217                    
SITE     3 AQ7 18 TRP d 253  ALA d 260  PHE d 261  LEU d 267                    
SITE     4 AQ7 18 CLA d 401  LHG d 409  LEU l  23  VAL l  26                    
SITE     5 AQ7 18 LEU l  29  PHE t  10                                          
SITE     1 AQ8  5 GLY d  99  PHE d 101  THR d 102  ASP e  45                    
SITE     2 AQ8  5 LEU e  80                                                     
SITE     1 AQ9 11 PL9 a 410  ARG d  24  ARG d  26  ILE f  15                    
SITE     2 AQ9 11 PHE f  16  THR f  17  VAL f  18  VAL f  21                    
SITE     3 AQ9 11 VAL x  27  ILE x  31  ASP x  35                               
SITE     1 AR1 16 SER a 232  ASN a 234  TRP b   5  TYR b   6                    
SITE     2 AR1 16 ARG b   7  LEU b 461  PHE b 464  TRP b 468                    
SITE     3 AR1 16 CLA b 612  CLA b 614  LHG b 620  TYR d 141                    
SITE     4 AR1 16 ILE d 144  TRP d 266  PHE d 269  THR d 277                    
SITE     1 AR2 19 MET a  37  LHG b 620  ILE d 256  PHE d 257                    
SITE     2 AR2 19 ALA d 260  PHE d 261  SER d 262  ASN d 263                    
SITE     3 AR2 19 TRP d 266  PHE d 270  PHO d 402  PL9 d 405                    
SITE     4 AR2 19 ASN l  13  THR l  15  SER l  16  TYR l  18                    
SITE     5 AR2 19 LEU l  19  PHE t  17  ALA t  20                               
SITE     1 AR3 20 ARG a 140  TRP a 142  PHE a 273  TRP a 284                    
SITE     2 AR3 20 PHE a 285  SQD a 411  PHE c  33  TRP c  36                    
SITE     3 AR3 20 TRP c 443  ARG c 447  CLA c 905  CLA c 909                    
SITE     4 AR3 20 CLA c 911  GLU d 219  ASN d 220  ALA d 229                    
SITE     5 AR3 20 SER d 230  THR d 231  PHE d 232  DGD j 101                    
SITE     1 AR4 13 ILE e  13  ARG e  18  TYR e  19  HIS e  23                    
SITE     2 AR4 13 THR e  26  ILE e  27  LEU e  30  ARG f  19                    
SITE     3 AR4 13 TRP f  20  VAL f  23  HIS f  24  ALA f  27                    
SITE     4 AR4 13 ILE f  31                                                     
SITE     1 AR5 12 TYR d  42  LEU d  43  GLY d  46  GLY d  47                    
SITE     2 AR5 12 LEU d  49  THR d  50  PHE d 101  PRO f  29                    
SITE     3 AR5 12 THR f  30  PHE f  33  VAL j  21  VAL j  25                    
SITE     1 AR6  2 ARG f  45  GLU v  23                                          
SITE     1 AR7  7 CLA b 602  CLA b 610  PHE h  34  LEU h  37                    
SITE     2 AR7  7 PHE h  38  PHE h  41  ILE x   3                               
SITE     1 AR8 16 TYR b 193  PHE b 250  TYR b 258  TYR b 273                    
SITE     2 AR8 16 GLN b 274  SER b 277  TYR b 279  GLY d  86                    
SITE     3 AR8 16 HIS d  87  LEU d 162  GLY d 163  TYR h  49                    
SITE     4 AR8 16 ASN h  50  VAL h  60  SER h  61  TRP h  62                    
SITE     1 AR9 20 GLN a 199  LEU a 200  PHE a 300  ASN a 301                    
SITE     2 AR9 20 PHE a 302  SER a 305  ASN c 405  ASN c 415                    
SITE     3 AR9 20 SER c 416  ASN c 418  CLA c 905  DGD c 917                    
SITE     4 AR9 20 LHG d 410  PHE j  29  ALA j  32  TYR j  33                    
SITE     5 AR9 20 GLY j  37  SER j  38  SER j  39  GLN v  34                    
SITE     1 AS1  4 GLY j  31  ALA j  34  GLY j  35  LEU j  36                    
SITE     1 AS2 14 PHE c  62  LEU c 119  ALA j  14  THR j  15                    
SITE     2 AS2 14 MET j  19  ILE k  28  LEU k  31  PHE k  32                    
SITE     3 AS2 14 ALA k  34  PHE k  37  VAL k  38  BCR k 102                    
SITE     4 AS2 14 ILE y  28  GLY y  29                                          
SITE     1 AS3  9 ALA c  55  GLY c  58  LEU c  59  SER c 122                    
SITE     2 AS3  9 CLA c 912  PHE k  32  TRP k  39  BCR k 101                    
SITE     3 AS3  9 SER z  16                                                     
SITE     1 AS4 13 ARG B  18  SER B 104  TRP B 115  CLA B 615                    
SITE     2 AS4 13 BCR B 622  ARG L   7  ARG l  14  TYR l  18                    
SITE     3 AS4 13 LEU l  21  VAL m  15  LEU m  16  TYR m  26                    
SITE     4 AS4 13 PHE t  23                                                     
SITE     1 AS5  3 THR o 138  ASN o 200  VAL o 201                               
SITE     1 AS6 19 ALA v  36  CYS v  37  CYS v  40  HIS v  41                    
SITE     2 AS6 19 THR v  46  THR v  48  LEU v  52  ASP v  53                    
SITE     3 AS6 19 LEU v  54  THR v  58  LEU v  59  LEU v  72                    
SITE     4 AS6 19 TYR v  75  MET v  76  TYR v  82  ILE v  88                    
SITE     5 AS6 19 HIS v  92  PRO v  93  MET v 104                               
SITE     1 AS7  6 GLN O  36  TYR O  38  PRO O 245  ALA O 246                    
SITE     2 AS7  6 ASN c  19  SER c  20                                          
SITE     1 AS8  6 GLN O  36  TYR O  38  PRO O 245  ALA O 246                    
SITE     2 AS8  6 ASN c  19  SER c  20                                          
SITE     1 AS9  6 GLN O  36  TYR O  38  PRO O 245  ALA O 246                    
SITE     2 AS9  6 ASN c  19  SER c  20                                          
SITE     1 AT1  9 ASP O  33  SER O  34  SER O  35  THR O  37                    
SITE     2 AT1  9 TYR O  38  ALA O 246  ASN c  19  SER c  20                    
SITE     3 AT1  9 ALA c  23                                                     
SITE     1 AT2  9 ASP O  33  SER O  34  SER O  35  THR O  37                    
SITE     2 AT2  9 TYR O  38  ALA O 246  ASN c  19  SER c  20                    
SITE     3 AT2  9 ALA c  23                                                     
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