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Database: PDB
Entry: 4TNK
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HEADER    ELECTRON TRANSPORT,PHOTOSYNTHESIS       04-JUN-14   4TNK              
TITLE     RT XFEL STRUCTURE OF PHOTOSYSTEM II 250 MICROSEC AFTER THE THIRD      
TITLE    2 ILLUMINATION AT 5.2 A RESOLUTION                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;                                
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-344;                                        
COMPND   5 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN 1,PHOTOSYSTEM II PROTEIN  
COMPND   6 D1 1;                                                                
COMPND   7 EC: 1.10.3.9;                                                        
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PHOTOSYSTEM II CORE LIGHT HARVESTING PROTEIN;              
COMPND  10 CHAIN: B, b;                                                         
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;                   
COMPND  18 EC: 1.10.3.9;                                                        
COMPND  19 MOL_ID: 5;                                                           
COMPND  20 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;                             
COMPND  21 CHAIN: E, e;                                                         
COMPND  22 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  23 MOL_ID: 6;                                                           
COMPND  24 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  25 CHAIN: F, f;                                                         
COMPND  26 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  27 MOL_ID: 7;                                                           
COMPND  28 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;                  
COMPND  29 CHAIN: H, h;                                                         
COMPND  30 SYNONYM: PSII-H;                                                     
COMPND  31 MOL_ID: 8;                                                           
COMPND  32 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  33 CHAIN: I, i;                                                         
COMPND  34 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;                                
COMPND  35 MOL_ID: 9;                                                           
COMPND  36 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;                  
COMPND  37 CHAIN: J, j;                                                         
COMPND  38 SYNONYM: PSII-J;                                                     
COMPND  39 MOL_ID: 10;                                                          
COMPND  40 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  41 CHAIN: K, k;                                                         
COMPND  42 SYNONYM: PSII-K;                                                     
COMPND  43 MOL_ID: 11;                                                          
COMPND  44 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  45 CHAIN: L, l;                                                         
COMPND  46 SYNONYM: PSII-L,PSII 5 KDA PROTEIN;                                  
COMPND  47 MOL_ID: 12;                                                          
COMPND  48 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;                  
COMPND  49 CHAIN: M, m;                                                         
COMPND  50 SYNONYM: PSII-M;                                                     
COMPND  51 MOL_ID: 13;                                                          
COMPND  52 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  53 CHAIN: O, o;                                                         
COMPND  54 SYNONYM: MSP;                                                        
COMPND  55 MOL_ID: 14;                                                          
COMPND  56 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  57 CHAIN: T, t;                                                         
COMPND  58 SYNONYM: PSII-TC;                                                    
COMPND  59 MOL_ID: 15;                                                          
COMPND  60 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  61 CHAIN: U, u;                                                         
COMPND  62 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;              
COMPND  63 MOL_ID: 16;                                                          
COMPND  64 MOLECULE: CYTOCHROME C-550;                                          
COMPND  65 CHAIN: V, v;                                                         
COMPND  66 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND  67 MOL_ID: 17;                                                          
COMPND  68 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  69 CHAIN: y, g;                                                         
COMPND  70 MOL_ID: 18;                                                          
COMPND  71 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  72 CHAIN: X, x;                                                         
COMPND  73 MOL_ID: 19;                                                          
COMPND  74 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Y;                  
COMPND  75 CHAIN: Y, G;                                                         
COMPND  76 FRAGMENT: SEE REMARK 999;                                            
COMPND  77 MOL_ID: 20;                                                          
COMPND  78 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  79 CHAIN: Z, z;                                                         
COMPND  80 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;                                                        
SOURCE  77 MOL_ID: 20;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  79 ORGANISM_TAXID: 197221;                                              
SOURCE  80 STRAIN: BP-1                                                         
KEYWDS    PHOTOSYNTHESIS, WATER OXIDATION, MEMBRANE PROTEIN, X-RAY FREE         
KEYWDS   2 ELECTRON LASER, ELECTRON TRANSPORT                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KERN,R.TRAN,R.ALONSO-MORI,S.KOROIDOV,N.ECHOLS,J.HATTNE,M.IBRAHIM,   
AUTHOR   2 S.GUL,H.LAKSMONO,R.G.SIERRA,R.J.GILDEA,G.HAN,J.HELLMICH,B.LASSALLE-  
AUTHOR   3 KAISER,R.CHATTERJEE,A.BREWSTER,C.A.STAN,C.GLOECKNER,A.LAMPE,         
AUTHOR   4 D.DIFIORE,D.MILATHIANAKI,A.R.FRY,M.M.SEIBERT,J.E.KOGLIN,E.GALLO,     
AUTHOR   5 J.UHLIG,D.SOKARAS,T.-C.WENG,P.H.ZWART,D.E.SKINNER,M.J.BOGAN,         
AUTHOR   6 M.MESSERSCHMIDT,P.GLATZEL,G.J.WILLIAMS,S.BOUTET,P.D.ADAMS,A.ZOUNI,   
AUTHOR   7 J.MESSINGER,N.K.SAUTER,U.BERGMANN,J.YANO,V.K.YACHANDRA               
REVDAT   4   04-DEC-19 4TNK    1       REMARK                                   
REVDAT   3   27-SEP-17 4TNK    1       REMARK                                   
REVDAT   2   23-JUL-14 4TNK    1       JRNL                                     
REVDAT   1   09-JUL-14 4TNK    0                                                
JRNL        AUTH   J.KERN,R.TRAN,R.ALONSO-MORI,S.KOROIDOV,N.ECHOLS,J.HATTNE,    
JRNL        AUTH 2 M.IBRAHIM,S.GUL,H.LAKSMONO,R.G.SIERRA,R.J.GILDEA,G.HAN,      
JRNL        AUTH 3 J.HELLMICH,B.LASSALLE-KAISER,R.CHATTERJEE,A.S.BREWSTER,      
JRNL        AUTH 4 C.A.STAN,C.GLOCKNER,A.LAMPE,D.DIFIORE,D.MILATHIANAKI,        
JRNL        AUTH 5 A.R.FRY,M.M.SEIBERT,J.E.KOGLIN,E.GALLO,J.UHLIG,D.SOKARAS,    
JRNL        AUTH 6 T.C.WENG,P.H.ZWART,D.E.SKINNER,M.J.BOGAN,M.MESSERSCHMIDT,    
JRNL        AUTH 7 P.GLATZEL,G.J.WILLIAMS,S.BOUTET,P.D.ADAMS,A.ZOUNI,           
JRNL        AUTH 8 J.MESSINGER,N.K.SAUTER,U.BERGMANN,J.YANO,V.K.YACHANDRA       
JRNL        TITL   TAKING SNAPSHOTS OF PHOTOSYNTHETIC WATER OXIDATION USING     
JRNL        TITL 2 FEMTOSECOND X-RAY DIFFRACTION AND SPECTROSCOPY.              
JRNL        REF    NAT COMMUN                    V.   5  4371 2014              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   25006873                                                     
JRNL        DOI    10.1038/NCOMMS5371                                           
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,         
REMARK   1  AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,     
REMARK   1  AUTH 3 P.H.ZWART,P.D.ADAMS                                          
REMARK   1  TITL   TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH 
REMARK   1  TITL 2 PHENIX.REFINE.                                               
REMARK   1  REF    ACTA CRYSTALLOGR. D BIOL.     V.  68   352 2012              
REMARK   1  REF  2 CRYSTALLOGR.                                                 
REMARK   1  REFN                   ESSN 1399-0047                               
REMARK   1  PMID   22505256                                                     
REMARK   1  DOI    10.1107/S0907444912001308                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.D.ADAMS,P.V.AFONINE,G.BUNKOCZI,V.B.CHEN,I.W.DAVIS,         
REMARK   1  AUTH 2 N.ECHOLS,J.J.HEADD,L.W.HUNG,G.J.KAPRAL,R.W.GROSSE-KUNSTLEVE, 
REMARK   1  AUTH 3 A.J.MCCOY,N.W.MORIARTY,R.OEFFNER,R.J.READ,D.C.RICHARDSON,    
REMARK   1  AUTH 4 J.S.RICHARDSON,T.C.TERWILLIGER,P.H.ZWART                     
REMARK   1  TITL   PHENIX: A COMPREHENSIVE PYTHON-BASED SYSTEM FOR              
REMARK   1  TITL 2 MACROMOLECULAR STRUCTURE SOLUTION.                           
REMARK   1  REF    ACTA CRYSTALLOGR. D BIOL.     V.  66   213 2010              
REMARK   1  REF  2 CRYSTALLOGR.                                                 
REMARK   1  REFN                   ESSN 1399-0047                               
REMARK   1  PMID   20124702                                                     
REMARK   1  DOI    10.1107/S0907444909052925                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1635+SVN)                 
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 5.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 68.41                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.406                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 68083                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.272                           
REMARK   3   R VALUE            (WORKING SET) : 0.271                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.888                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3328                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 68.4176 - 14.9500    1.00     2767   115  0.3377 0.3494        
REMARK   3     2 14.9500 - 11.8865    1.00     2771   145  0.2402 0.2175        
REMARK   3     3 11.8865 - 10.3899    1.00     2722   140  0.2159 0.2218        
REMARK   3     4 10.3899 -  9.4426    1.00     2772   144  0.2310 0.2718        
REMARK   3     5  9.4426 -  8.7673    1.00     2747   131  0.2239 0.2223        
REMARK   3     6  8.7673 -  8.2513    1.00     2740   153  0.2305 0.2816        
REMARK   3     7  8.2513 -  7.8387    1.00     2749   157  0.2401 0.2694        
REMARK   3     8  7.8387 -  7.4979    1.00     2757   128  0.2423 0.2765        
REMARK   3     9  7.4979 -  7.2096    1.00     2774   157  0.2491 0.2844        
REMARK   3    10  7.2096 -  6.9610    1.00     2683   126  0.2534 0.3034        
REMARK   3    11  6.9610 -  6.7436    1.00     2782   141  0.2608 0.2727        
REMARK   3    12  6.7436 -  6.5510    1.00     2768   153  0.2757 0.2923        
REMARK   3    13  6.5510 -  6.3786    1.00     2737   140  0.2860 0.2929        
REMARK   3    14  6.3786 -  6.2231    1.00     2786   131  0.2719 0.2963        
REMARK   3    15  6.2231 -  6.0817    1.00     2714   163  0.2936 0.3380        
REMARK   3    16  6.0817 -  5.9524    1.00     2765   140  0.2966 0.3055        
REMARK   3    17  5.9524 -  5.8334    1.00     2754   135  0.3138 0.3425        
REMARK   3    18  5.8334 -  5.7233    0.99     2701   154  0.3095 0.3645        
REMARK   3    19  5.7233 -  5.6212    0.98     2724   131  0.3294 0.3744        
REMARK   3    20  5.6212 -  5.5259    0.98     2698   134  0.3359 0.3382        
REMARK   3    21  5.5259 -  5.4368    0.94     2626   137  0.3434 0.3453        
REMARK   3    22  5.4368 -  5.3532    0.90     2427   126  0.3487 0.3494        
REMARK   3    23  5.3532 -  5.2745    0.88     2430   137  0.3448 0.3888        
REMARK   3    24  5.2745 -  5.2003    0.86     2361   110  0.3560 0.3839        
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)     : 0.787            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.937           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 176.2                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 207.6                          
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      :  0.005          52088                                  
REMARK   3   ANGLE     :  0.776          71528                                  
REMARK   3   CHIRALITY :  0.031           7238                                  
REMARK   3   PLANARITY :  0.004           8510                                  
REMARK   3   DIHEDRAL  : 18.635          18206                                  
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 'G'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'B'                                   
REMARK   3     SELECTION          : CHAIN 'N'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'C'                                   
REMARK   3     SELECTION          : CHAIN 'P'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'D'                                   
REMARK   3     SELECTION          : CHAIN 'Q'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'E'                                   
REMARK   3     SELECTION          : CHAIN 'R'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 6                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'F'                                   
REMARK   3     SELECTION          : CHAIN 'S'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 7                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'H'                                   
REMARK   3     SELECTION          : CHAIN 'W'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 8                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'I'                                   
REMARK   3     SELECTION          : CHAIN 'A'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 9                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'J'                                   
REMARK   3     SELECTION          : CHAIN 'B'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 10                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'K'                                   
REMARK   3     SELECTION          : CHAIN 'C'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 11                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'L'                                   
REMARK   3     SELECTION          : CHAIN 'D'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 12                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'M'                                   
REMARK   3     SELECTION          : CHAIN 'E'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 13                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'O'                                   
REMARK   3     SELECTION          : CHAIN 'F'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 14                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'T'                                   
REMARK   3     SELECTION          : CHAIN 'G'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 15                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'U'                                   
REMARK   3     SELECTION          : CHAIN 'H'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 16                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'V'                                   
REMARK   3     SELECTION          : CHAIN 'I'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 17                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'X'                                   
REMARK   3     SELECTION          : CHAIN 'J'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 18                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'Z'                                   
REMARK   3     SELECTION          : CHAIN 'L'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 19                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'M'                                   
REMARK   3     SELECTION          : CHAIN 'Y'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4TNK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201921.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 7850                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER                
REMARK 200  BEAMLINE                       : CXI                                
REMARK 200  X-RAY GENERATOR MODEL          : SLAC LCLS BEAMLINE CXI             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.77                               
REMARK 200  MONOCHROMATOR                  : NO MONOCHROMATOR, FEL BEAM WITH    
REMARK 200                                   20-30 EV BANDWIDTH                 
REMARK 200  OPTICS                         : KB MIRRORS                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : CS-PAD DETECTOR                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CCTBX.XFEL                         
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34679                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 5.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 68.410                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 88.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 41.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 5.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 3BZ1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG2000, 5 MM CALCIUM CHLORIDE, 100   
REMARK 280  MM PIPES, PH 7.0, BATCH, TEMPERATURE 298K, BATCH MODE               
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       66.30750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      153.41250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      114.64800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      153.41250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       66.30750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      114.64800            
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: 40-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, Y,            
REMARK 350                    AND CHAINS: Z, a, b, c, d, e, f, h, i, j,         
REMARK 350                    AND CHAINS: k, l, m, o, t, u, v, g, x,            
REMARK 350                    AND CHAINS: G, 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     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   492                                                      
REMARK 465     TRP B   493                                                      
REMARK 465     GLY B   494                                                      
REMARK 465     PHE B   495                                                      
REMARK 465     TYR B   496                                                      
REMARK 465     GLN B   497                                                      
REMARK 465     LYS B   498                                                      
REMARK 465     VAL B   499                                                      
REMARK 465     GLY B   500                                                      
REMARK 465     ASP B   501                                                      
REMARK 465     VAL B   502                                                      
REMARK 465     THR B   503                                                      
REMARK 465     THR B   504                                                      
REMARK 465     ARG B   505                                                      
REMARK 465     ARG B   506                                                      
REMARK 465     LYS B   507                                                      
REMARK 465     GLU B   508                                                      
REMARK 465     ALA B   509                                                      
REMARK 465     VAL B   510                                                      
REMARK 465     MET C    13                                                      
REMARK 465     VAL C    14                                                      
REMARK 465     THR C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     SER C    18                                                      
REMARK 465     ASN C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     ILE C    21                                                      
REMARK 465     PHE C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     THR C    24                                                      
REMARK 465     ASN C    25                                                      
REMARK 465     ARG C    26                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     ILE D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     ILE D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     PRO D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     ARG D    12                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     MET F     1                                                      
REMARK 465     THR F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     ASN F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     PRO F     6                                                      
REMARK 465     ASN F     7                                                      
REMARK 465     GLN F     8                                                      
REMARK 465     GLU F     9                                                      
REMARK 465     PRO F    10                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ASP I    36                                                      
REMARK 465     LEU I    37                                                      
REMARK 465     GLU I    38                                                      
REMARK 465     MET J     1                                                      
REMARK 465     MET J     2                                                      
REMARK 465     SER J     3                                                      
REMARK 465     GLU J     4                                                      
REMARK 465     GLY J     5                                                      
REMARK 465     GLY J     6                                                      
REMARK 465     MET K     1                                                      
REMARK 465     ILE K     2                                                      
REMARK 465     ASP K     3                                                      
REMARK 465     ALA K     4                                                      
REMARK 465     LEU K     5                                                      
REMARK 465     VAL K     6                                                      
REMARK 465     LEU K     7                                                      
REMARK 465     VAL K     8                                                      
REMARK 465     ALA K     9                                                      
REMARK 465     SER M    35                                                      
REMARK 465     SER M    36                                                      
REMARK 465     MET O     1                                                      
REMARK 465     LYS O     2                                                      
REMARK 465     TYR O     3                                                      
REMARK 465     ARG O     4                                                      
REMARK 465     ILE O     5                                                      
REMARK 465     LEU O     6                                                      
REMARK 465     MET O     7                                                      
REMARK 465     ALA O     8                                                      
REMARK 465     THR O     9                                                      
REMARK 465     LEU O    10                                                      
REMARK 465     LEU O    11                                                      
REMARK 465     ALA O    12                                                      
REMARK 465     VAL O    13                                                      
REMARK 465     CYS O    14                                                      
REMARK 465     LEU O    15                                                      
REMARK 465     GLY O    16                                                      
REMARK 465     ILE O    17                                                      
REMARK 465     PHE O    18                                                      
REMARK 465     SER O    19                                                      
REMARK 465     LEU O    20                                                      
REMARK 465     SER O    21                                                      
REMARK 465     ALA O    22                                                      
REMARK 465     PRO O    23                                                      
REMARK 465     ALA O    24                                                      
REMARK 465     PHE O    25                                                      
REMARK 465     ALA O    26                                                      
REMARK 465     ALA O    27                                                      
REMARK 465     LYS O    28                                                      
REMARK 465     GLN O    29                                                      
REMARK 465     MET U     1                                                      
REMARK 465     GLN U     2                                                      
REMARK 465     ARG U     3                                                      
REMARK 465     LEU U     4                                                      
REMARK 465     GLY U     5                                                      
REMARK 465     ARG U     6                                                      
REMARK 465     TRP U     7                                                      
REMARK 465     LEU U     8                                                      
REMARK 465     ALA U     9                                                      
REMARK 465     LEU U    10                                                      
REMARK 465     ALA U    11                                                      
REMARK 465     TYR U    12                                                      
REMARK 465     PHE U    13                                                      
REMARK 465     VAL U    14                                                      
REMARK 465     GLY U    15                                                      
REMARK 465     VAL U    16                                                      
REMARK 465     SER U    17                                                      
REMARK 465     LEU U    18                                                      
REMARK 465     LEU U    19                                                      
REMARK 465     GLY U    20                                                      
REMARK 465     TRP U    21                                                      
REMARK 465     ILE U    22                                                      
REMARK 465     ASN U    23                                                      
REMARK 465     TRP U    24                                                      
REMARK 465     SER U    25                                                      
REMARK 465     ALA U    26                                                      
REMARK 465     PRO U    27                                                      
REMARK 465     THR U    28                                                      
REMARK 465     LEU U    29                                                      
REMARK 465     ALA U    30                                                      
REMARK 465     ALA U    31                                                      
REMARK 465     THR U    32                                                      
REMARK 465     ALA U    33                                                      
REMARK 465     SER U    34                                                      
REMARK 465     THR U    35                                                      
REMARK 465     GLU U    36                                                      
REMARK 465     GLU U    37                                                      
REMARK 465     MET V     1                                                      
REMARK 465     LEU V     2                                                      
REMARK 465     LYS V     3                                                      
REMARK 465     LYS V     4                                                      
REMARK 465     CYS V     5                                                      
REMARK 465     VAL V     6                                                      
REMARK 465     TRP V     7                                                      
REMARK 465     LEU V     8                                                      
REMARK 465     ALA V     9                                                      
REMARK 465     VAL V    10                                                      
REMARK 465     ALA V    11                                                      
REMARK 465     LEU V    12                                                      
REMARK 465     CYS V    13                                                      
REMARK 465     LEU V    14                                                      
REMARK 465     CYS V    15                                                      
REMARK 465     LEU V    16                                                      
REMARK 465     TRP V    17                                                      
REMARK 465     GLN V    18                                                      
REMARK 465     PHE V    19                                                      
REMARK 465     THR V    20                                                      
REMARK 465     MET V    21                                                      
REMARK 465     GLY V    22                                                      
REMARK 465     THR V    23                                                      
REMARK 465     ALA V    24                                                      
REMARK 465     LEU V    25                                                      
REMARK 465     ALA V    26                                                      
REMARK 465     MET y     1                                                      
REMARK 465     GLY y     2                                                      
REMARK 465     ILE y     3                                                      
REMARK 465     PHE y     4                                                      
REMARK 465     ASN y     5                                                      
REMARK 465     GLY y     6                                                      
REMARK 465     ILE y     7                                                      
REMARK 465     ILE y     8                                                      
REMARK 465     GLU y     9                                                      
REMARK 465     PHE y    10                                                      
REMARK 465     LEU y    11                                                      
REMARK 465     SER y    12                                                      
REMARK 465     ASN y    13                                                      
REMARK 465     ILE y    14                                                      
REMARK 465     ASN y    15                                                      
REMARK 465     PHE y    16                                                      
REMARK 465     GLU y    17                                                      
REMARK 465     VAL y    18                                                      
REMARK 465     MET X    10                                                      
REMARK 465     ARG X    48                                                      
REMARK 465     SER X    49                                                      
REMARK 465     LEU X    50                                                      
REMARK 465     MET a     1                                                      
REMARK 465     THR a     2                                                      
REMARK 465     THR a     3                                                      
REMARK 465     THR a     4                                                      
REMARK 465     LEU a     5                                                      
REMARK 465     GLN a     6                                                      
REMARK 465     ARG a     7                                                      
REMARK 465     ARG a     8                                                      
REMARK 465     GLU a     9                                                      
REMARK 465     MET b     1                                                      
REMARK 465     GLU b   492                                                      
REMARK 465     TRP b   493                                                      
REMARK 465     GLY b   494                                                      
REMARK 465     PHE b   495                                                      
REMARK 465     TYR b   496                                                      
REMARK 465     GLN b   497                                                      
REMARK 465     LYS b   498                                                      
REMARK 465     VAL b   499                                                      
REMARK 465     GLY b   500                                                      
REMARK 465     ASP b   501                                                      
REMARK 465     VAL b   502                                                      
REMARK 465     THR b   503                                                      
REMARK 465     THR b   504                                                      
REMARK 465     ARG b   505                                                      
REMARK 465     ARG b   506                                                      
REMARK 465     LYS b   507                                                      
REMARK 465     GLU b   508                                                      
REMARK 465     ALA b   509                                                      
REMARK 465     VAL b   510                                                      
REMARK 465     MET c    13                                                      
REMARK 465     VAL c    14                                                      
REMARK 465     THR c    15                                                      
REMARK 465     LEU c    16                                                      
REMARK 465     SER c    17                                                      
REMARK 465     SER c    18                                                      
REMARK 465     ASN c    19                                                      
REMARK 465     SER c    20                                                      
REMARK 465     ILE c    21                                                      
REMARK 465     PHE c    22                                                      
REMARK 465     ALA c    23                                                      
REMARK 465     THR c    24                                                      
REMARK 465     ASN c    25                                                      
REMARK 465     ARG c    26                                                      
REMARK 465     MET d     1                                                      
REMARK 465     THR d     2                                                      
REMARK 465     ILE d     3                                                      
REMARK 465     ALA d     4                                                      
REMARK 465     ILE d     5                                                      
REMARK 465     GLY d     6                                                      
REMARK 465     ARG d     7                                                      
REMARK 465     ALA d     8                                                      
REMARK 465     PRO d     9                                                      
REMARK 465     ALA d    10                                                      
REMARK 465     GLU d    11                                                      
REMARK 465     ARG d    12                                                      
REMARK 465     MET e     1                                                      
REMARK 465     ALA e     2                                                      
REMARK 465     MET f     1                                                      
REMARK 465     THR f     2                                                      
REMARK 465     SER f     3                                                      
REMARK 465     ASN f     4                                                      
REMARK 465     THR f     5                                                      
REMARK 465     PRO f     6                                                      
REMARK 465     ASN f     7                                                      
REMARK 465     GLN f     8                                                      
REMARK 465     GLU f     9                                                      
REMARK 465     PRO f    10                                                      
REMARK 465     MET h     1                                                      
REMARK 465     ASP i    36                                                      
REMARK 465     LEU i    37                                                      
REMARK 465     GLU i    38                                                      
REMARK 465     MET j     1                                                      
REMARK 465     MET j     2                                                      
REMARK 465     SER j     3                                                      
REMARK 465     GLU j     4                                                      
REMARK 465     GLY j     5                                                      
REMARK 465     GLY j     6                                                      
REMARK 465     MET k     1                                                      
REMARK 465     ILE k     2                                                      
REMARK 465     ASP k     3                                                      
REMARK 465     ALA k     4                                                      
REMARK 465     LEU k     5                                                      
REMARK 465     VAL k     6                                                      
REMARK 465     LEU k     7                                                      
REMARK 465     VAL k     8                                                      
REMARK 465     ALA k     9                                                      
REMARK 465     SER m    35                                                      
REMARK 465     SER m    36                                                      
REMARK 465     MET o     1                                                      
REMARK 465     LYS o     2                                                      
REMARK 465     TYR o     3                                                      
REMARK 465     ARG o     4                                                      
REMARK 465     ILE o     5                                                      
REMARK 465     LEU o     6                                                      
REMARK 465     MET o     7                                                      
REMARK 465     ALA o     8                                                      
REMARK 465     THR o     9                                                      
REMARK 465     LEU o    10                                                      
REMARK 465     LEU o    11                                                      
REMARK 465     ALA o    12                                                      
REMARK 465     VAL o    13                                                      
REMARK 465     CYS o    14                                                      
REMARK 465     LEU o    15                                                      
REMARK 465     GLY o    16                                                      
REMARK 465     ILE o    17                                                      
REMARK 465     PHE o    18                                                      
REMARK 465     SER o    19                                                      
REMARK 465     LEU o    20                                                      
REMARK 465     SER o    21                                                      
REMARK 465     ALA o    22                                                      
REMARK 465     PRO o    23                                                      
REMARK 465     ALA o    24                                                      
REMARK 465     PHE o    25                                                      
REMARK 465     ALA o    26                                                      
REMARK 465     ALA o    27                                                      
REMARK 465     LYS o    28                                                      
REMARK 465     GLN o    29                                                      
REMARK 465     MET u     1                                                      
REMARK 465     GLN u     2                                                      
REMARK 465     ARG u     3                                                      
REMARK 465     LEU u     4                                                      
REMARK 465     GLY u     5                                                      
REMARK 465     ARG u     6                                                      
REMARK 465     TRP u     7                                                      
REMARK 465     LEU u     8                                                      
REMARK 465     ALA u     9                                                      
REMARK 465     LEU u    10                                                      
REMARK 465     ALA u    11                                                      
REMARK 465     TYR u    12                                                      
REMARK 465     PHE u    13                                                      
REMARK 465     VAL u    14                                                      
REMARK 465     GLY u    15                                                      
REMARK 465     VAL u    16                                                      
REMARK 465     SER u    17                                                      
REMARK 465     LEU u    18                                                      
REMARK 465     LEU u    19                                                      
REMARK 465     GLY u    20                                                      
REMARK 465     TRP u    21                                                      
REMARK 465     ILE u    22                                                      
REMARK 465     ASN u    23                                                      
REMARK 465     TRP u    24                                                      
REMARK 465     SER u    25                                                      
REMARK 465     ALA u    26                                                      
REMARK 465     PRO u    27                                                      
REMARK 465     THR u    28                                                      
REMARK 465     LEU u    29                                                      
REMARK 465     ALA u    30                                                      
REMARK 465     ALA u    31                                                      
REMARK 465     THR u    32                                                      
REMARK 465     ALA u    33                                                      
REMARK 465     SER u    34                                                      
REMARK 465     THR u    35                                                      
REMARK 465     GLU u    36                                                      
REMARK 465     GLU u    37                                                      
REMARK 465     MET v     1                                                      
REMARK 465     LEU v     2                                                      
REMARK 465     LYS v     3                                                      
REMARK 465     LYS v     4                                                      
REMARK 465     CYS v     5                                                      
REMARK 465     VAL v     6                                                      
REMARK 465     TRP v     7                                                      
REMARK 465     LEU v     8                                                      
REMARK 465     ALA v     9                                                      
REMARK 465     VAL v    10                                                      
REMARK 465     ALA v    11                                                      
REMARK 465     LEU v    12                                                      
REMARK 465     CYS v    13                                                      
REMARK 465     LEU v    14                                                      
REMARK 465     CYS v    15                                                      
REMARK 465     LEU v    16                                                      
REMARK 465     TRP v    17                                                      
REMARK 465     GLN v    18                                                      
REMARK 465     PHE v    19                                                      
REMARK 465     THR v    20                                                      
REMARK 465     MET v    21                                                      
REMARK 465     GLY v    22                                                      
REMARK 465     THR v    23                                                      
REMARK 465     ALA v    24                                                      
REMARK 465     LEU v    25                                                      
REMARK 465     ALA v    26                                                      
REMARK 465     MET g     1                                                      
REMARK 465     GLY g     2                                                      
REMARK 465     ILE g     3                                                      
REMARK 465     PHE g     4                                                      
REMARK 465     ASN g     5                                                      
REMARK 465     GLY g     6                                                      
REMARK 465     ILE g     7                                                      
REMARK 465     ILE g     8                                                      
REMARK 465     GLU g     9                                                      
REMARK 465     PHE g    10                                                      
REMARK 465     LEU g    11                                                      
REMARK 465     SER g    12                                                      
REMARK 465     ASN g    13                                                      
REMARK 465     ILE g    14                                                      
REMARK 465     ASN g    15                                                      
REMARK 465     PHE g    16                                                      
REMARK 465     GLU g    17                                                      
REMARK 465     VAL g    18                                                      
REMARK 465     MET x    10                                                      
REMARK 465     ARG x    48                                                      
REMARK 465     SER x    49                                                      
REMARK 465     LEU x    50                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR C 143    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU C 462    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  20    CG   CD   CE   NZ                                   
REMARK 470     ARG O  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU O  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS O  85    CG   CD   CE   NZ                                   
REMARK 470     ARG O 233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU V  41    CG   CD   OE1  OE2                                  
REMARK 470     ARG y  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR c 143    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU c 462    CG   CD   OE1  OE2                                  
REMARK 470     LYS h  20    CG   CD   CE   NZ                                   
REMARK 470     ARG o  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU o  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS o  85    CG   CD   CE   NZ                                   
REMARK 470     ARG o 233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU v  41    CG   CD   OE1  OE2                                  
REMARK 470     ARG g  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    TRP c   250     OG1  THR c   254              2.13            
REMARK 500   O    TRP C   250     OG1  THR C   254              2.13            
REMARK 500   O    TRP c   291     OG1  THR c   305              2.15            
REMARK 500   O    TRP C   291     OG1  THR C   305              2.16            
REMARK 500   OD2  ASP u    56     OG1  THR u   115              2.17            
REMARK 500   O    ALA B   155     OG1  THR B   159              2.18            
REMARK 500   OD2  ASP U    56     OG1  THR U   115              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 484   C   -  N   -  CA  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    PRO b 484   C   -  N   -  CA  ANGL. DEV. =  13.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  12      114.87    157.41                                   
REMARK 500    PRO A 141     -128.53    -75.49                                   
REMARK 500    TRP A 142      -11.06     58.64                                   
REMARK 500    LEU A 159      -50.58   -131.85                                   
REMARK 500    SER A 222       42.56   -109.57                                   
REMARK 500    ILE A 259      -84.90   -104.06                                   
REMARK 500    PHE A 302       32.41    -98.83                                   
REMARK 500    SER A 305      -70.55    -77.34                                   
REMARK 500    ARG A 334      -72.15    -27.25                                   
REMARK 500    ASP B 119       54.86    -91.65                                   
REMARK 500    ARG B 127      -72.10    -63.47                                   
REMARK 500    PRO B 183      175.78    -59.24                                   
REMARK 500    LEU B 218      -67.97    -95.25                                   
REMARK 500    ARG B 230       53.27     31.45                                   
REMARK 500    ASP B 313       42.32    -90.75                                   
REMARK 500    LYS B 349      -39.98    -37.90                                   
REMARK 500    THR B 436      -70.24    -33.81                                   
REMARK 500    SER B 480      -13.16     70.35                                   
REMARK 500    ILE B 482     -165.34   -118.17                                   
REMARK 500    PRO B 484     -142.56     -7.45                                   
REMARK 500    GLU B 485      162.24     62.58                                   
REMARK 500    LEU B 486       69.38   -155.56                                   
REMARK 500    PRO B 488     -109.59      6.89                                   
REMARK 500    GLU B 489       57.02    -64.50                                   
REMARK 500    GLN B 490      108.16   -166.86                                   
REMARK 500    GLU C  29     -149.12   -148.60                                   
REMARK 500    ARG C 135      -62.13   -122.68                                   
REMARK 500    SER C 144      109.87   -179.18                                   
REMARK 500    ASN C 201       59.39   -168.51                                   
REMARK 500    TRP C 223     -145.87     60.93                                   
REMARK 500    LEU C 253       30.92    -97.09                                   
REMARK 500    PHE C 257     -144.84    -71.51                                   
REMARK 500    ARG C 320      -71.46    -59.42                                   
REMARK 500    THR C 355        2.95    -69.30                                   
REMARK 500    PRO C 368       -9.84    -59.77                                   
REMARK 500    LEU C 375      114.28    -34.48                                   
REMARK 500    ASN C 382       12.48   -161.87                                   
REMARK 500    HIS C 398       33.86   -142.14                                   
REMARK 500    ALA C 411      -17.15    -49.74                                   
REMARK 500    SER C 416      -59.62   -177.69                                   
REMARK 500    PHE C 455       22.92   -150.08                                   
REMARK 500    GLU C 462      -75.74    -68.70                                   
REMARK 500    ARG D  26     -164.63   -102.29                                   
REMARK 500    VAL D  30      -82.73    -89.29                                   
REMARK 500    LEU D  37      -71.92    -56.30                                   
REMARK 500    SER D  65       16.52   -141.23                                   
REMARK 500    PRO D 140       37.37    -85.29                                   
REMARK 500    LEU D 158      -64.67   -128.74                                   
REMARK 500    ALA D 234       28.72    -76.02                                   
REMARK 500    THR D 238       79.58   -100.40                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     250 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     PL9 A  407                                                       
REMARK 610     DGD A  409                                                       
REMARK 610     LHG A  410                                                       
REMARK 610     SQD A  413                                                       
REMARK 610     DGD B  620                                                       
REMARK 610     LMG B  621                                                       
REMARK 610     SQD B  622                                                       
REMARK 610     LMG B  625                                                       
REMARK 610     DGD B  626                                                       
REMARK 610     SQD B  627                                                       
REMARK 610     DGD C  514                                                       
REMARK 610     DGD C  515                                                       
REMARK 610     LMG C  517                                                       
REMARK 610     LHG C  518                                                       
REMARK 610     LMG C  521                                                       
REMARK 610     LMG D  406                                                       
REMARK 610     DGD D  407                                                       
REMARK 610     LMT D  408                                                       
REMARK 610     LMG D  409                                                       
REMARK 610     LMG E  101                                                       
REMARK 610     SQD F  103                                                       
REMARK 610     LMG I  101                                                       
REMARK 610     PL9 J  101                                                       
REMARK 610     LMG L  101                                                       
REMARK 610     LMG M  101                                                       
REMARK 610     LMG a  402                                                       
REMARK 610     PL9 a  407                                                       
REMARK 610     DGD a  408                                                       
REMARK 610     LHG a  409                                                       
REMARK 610     SQD a  412                                                       
REMARK 610     DGD b  601                                                       
REMARK 610     SQD b  602                                                       
REMARK 610     DGD b  625                                                       
REMARK 610     LMG b  626                                                       
REMARK 610     LMG b  627                                                       
REMARK 610     DGD c  515                                                       
REMARK 610     DGD c  516                                                       
REMARK 610     LMG c  518                                                       
REMARK 610     LHG c  519                                                       
REMARK 610     LMG c  522                                                       
REMARK 610     SQD d  403                                                       
REMARK 610     LMG d  408                                                       
REMARK 610     LMG d  409                                                       
REMARK 610     DGD d  410                                                       
REMARK 610     LMT d  411                                                       
REMARK 610     LMG d  412                                                       
REMARK 610     LMG e  101                                                       
REMARK 610     SQD f  103                                                       
REMARK 610     LMG i  102                                                       
REMARK 610     PL9 j  101                                                       
REMARK 610     LMG l  101                                                       
REMARK 610     LMG m  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 412  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD1                                                    
REMARK 620 2 OEX A 412   O1  124.8                                              
REMARK 620 3 OEX A 412   O2   61.2  63.6                                        
REMARK 620 4 OEX A 412   O5   94.5  61.1  63.8                                  
REMARK 620 5 GLU A 189   OE1 167.1  65.5 128.2  84.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 412  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD2                                                    
REMARK 620 2 OEX A 412   O5  110.9                                              
REMARK 620 3 OEX A 412   O4   68.4  87.2                                        
REMARK 620 4 GLU A 333   OE2 125.0 107.3  75.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 412  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 OEX A 412   O1   81.8                                              
REMARK 620 3 OEX A 412   O5  128.5  90.4                                        
REMARK 620 4 OEX A 412   O3  142.5  89.7  87.7                                  
REMARK 620 5 HIS A 332   NE2  77.6 157.5 109.5 101.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 401  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2  98.8                                              
REMARK 620 3 HIS D 214   NE2 122.0 109.7                                        
REMARK 620 4 HIS D 268   NE2  79.5 157.4  89.6                                  
REMARK 620 5 BCT D 402   O2   86.1  87.2 142.5  70.2                            
REMARK 620 6 BCT D 402   O3  131.9  93.6  96.2  72.2  48.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 412  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 OEX A 412   O2  136.6                                              
REMARK 620 3 OEX A 412   O3   96.3  88.7                                        
REMARK 620 4 OEX A 412   O4   83.6  92.2 178.9                                  
REMARK 620 5 OEX A 412   O5  106.8 116.3  89.5  89.6                            
REMARK 620 6 GLU C 354   OE2  66.7  73.3  74.7 106.2 161.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 412  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 OEX A 412   O1  112.2                                              
REMARK 620 3 OEX A 412   O2  157.6  89.9                                        
REMARK 620 4 OEX A 412   O3   93.0  86.9  84.5                                  
REMARK 620 5 ALA A 344   OXT  99.3 130.7  66.4 129.6                            
REMARK 620 6 GLU C 354   OE1  66.3 156.9  92.1  70.5  70.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 510  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  39   OD1                                                    
REMARK 620 2 CLA C 510   NA   96.1                                              
REMARK 620 3 CLA C 510   NB   74.4  92.3                                        
REMARK 620 4 CLA C 510   NC   84.2 176.8  90.9                                  
REMARK 620 5 CLA C 510   ND  104.9  90.6 177.1  86.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM F 101   NA   87.8                                              
REMARK 620 3 HEM F 101   NB  103.5  89.8                                        
REMARK 620 4 HEM F 101   NC   88.9 176.0  88.6                                  
REMARK 620 5 HEM F 101   ND   67.3  89.5 170.8  91.4                            
REMARK 620 6 HIS F  24   NE2 158.0  70.2  77.4 113.1 111.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA K 102  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP K  19   OD2                                                    
REMARK 620 2 ASP K  23   OD1 120.2                                              
REMARK 620 3 ASP K  23   OD2 114.8  41.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM V 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  67   NE2                                                    
REMARK 620 2 HEM V 201   NA   86.9                                              
REMARK 620 3 HEM V 201   NB   87.9  90.4                                        
REMARK 620 4 HEM V 201   NC   88.1 175.0  90.0                                  
REMARK 620 5 HEM V 201   ND   81.7  88.6 169.6  90.2                            
REMARK 620 6 HIS V 118   NE2 168.0  89.4 103.5  95.3  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 411  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD1                                                    
REMARK 620 2 OEX a 411   O1  124.1                                              
REMARK 620 3 OEX a 411   O2   60.8  63.4                                        
REMARK 620 4 OEX a 411   O5   95.4  61.3  63.9                                  
REMARK 620 5 GLU a 189   OE1 171.6  61.4 123.9  81.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 411  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD2                                                    
REMARK 620 2 OEX a 411   O5  108.9                                              
REMARK 620 3 OEX a 411   O4   68.2  87.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 411  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 OEX a 411   O1   84.6                                              
REMARK 620 3 OEX a 411   O5  133.5  90.3                                        
REMARK 620 4 OEX a 411   O3  138.3  89.6  87.7                                  
REMARK 620 5 HIS a 332   NE2  74.1 157.5 109.5 101.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a 413  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS a 272   NE2  93.7                                              
REMARK 620 3 HIS d 214   NE2 120.8 110.2                                        
REMARK 620 4 HIS d 268   NE2  77.1 155.8  93.6                                  
REMARK 620 5 BCT d 404   O2   87.8  87.2 143.9  70.2                            
REMARK 620 6 BCT d 404   O3  133.9  97.5  96.7  74.5  48.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 411  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 OEX a 411   O2  135.4                                              
REMARK 620 3 OEX a 411   O3   95.6  88.7                                        
REMARK 620 4 OEX a 411   O4   84.1  92.2 179.0                                  
REMARK 620 5 OEX a 411   O5  108.2 116.2  89.5  89.6                            
REMARK 620 6 GLU c 354   OE2  66.7  72.4  73.1 107.6 160.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 411  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 342   OD1                                                    
REMARK 620 2 OEX a 411   O1  111.4                                              
REMARK 620 3 OEX a 411   O2  158.6  89.8                                        
REMARK 620 4 OEX a 411   O3   94.2  86.8  84.5                                  
REMARK 620 5 ALA a 344   OXT 100.5 128.8  65.5 130.4                            
REMARK 620 6 GLU c 354   OE1  66.0 158.6  93.5  72.5  71.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 510  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c  39   OD1                                                    
REMARK 620 2 CLA c 510   NA   96.8                                              
REMARK 620 3 CLA c 510   NB   75.9  92.2                                        
REMARK 620 4 CLA c 510   NC   83.4 176.7  91.0                                  
REMARK 620 5 CLA c 510   ND  103.4  90.6 177.1  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM f 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e  23   NE2                                                    
REMARK 620 2 HEM f 101   NA   87.0                                              
REMARK 620 3 HEM f 101   NB  106.2  89.9                                        
REMARK 620 4 HEM f 101   NC   91.0 176.7  88.1                                  
REMARK 620 5 HEM f 101   ND   66.3  90.0 172.5  91.6                            
REMARK 620 6 HIS f  24   NE2 158.7  71.7  74.9 110.3 112.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA k 101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP k  19   OD2                                                    
REMARK 620 2 ASP k  23   OD1 128.6                                              
REMARK 620 3 ASP k  23   OD2 113.9  43.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM v 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS v  67   NE2                                                    
REMARK 620 2 HEM v 201   NA   85.2                                              
REMARK 620 3 HEM v 201   NB   86.0  88.6                                        
REMARK 620 4 HEM v 201   NC   89.6 174.8  90.9                                  
REMARK 620 5 HEM v 201   ND   83.6  89.8 169.6  89.8                            
REMARK 620 6 HIS v 118   NE2 170.1  87.5 100.4  97.8  89.8                      
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 FE2 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 411                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD B 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM F 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR F 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD F 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG I 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT I 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 J 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR J 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA K 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG L 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG M 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT M 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT M 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR y 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD a 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 410                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD b 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG c 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD d 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT d 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR f 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR i 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG i 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT i 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 j 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR j 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA k 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG l 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG m 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA o 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM v 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR g 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR x 101                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4TNH   RELATED DB: PDB                                   
REMARK 900 PHOTOSYSTEM II IN THE DARK STATE AT 4.9 A RESOLUTION                 
REMARK 900 RELATED ID: 4TNI   RELATED DB: PDB                                   
REMARK 900 PHOTOSYSTEM II 500 MS AFTER THE THIRD ILLUMINATION (3F) AT 4.6 A     
REMARK 900 RESOLUTION                                                           
REMARK 900 RELATED ID: 4TNJ   RELATED DB: PDB                                   
REMARK 900 PHOTOSYSTEM II 500 MS AFTER THE SECOND ILLUMINATION (2F) AT 4.5 A    
REMARK 900 RESOLUTION                                                           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 MOLECULE 19 (PHOTOSYSTEM II PROTEIN Y): THE DEPOSITORS STATE THAT    
REMARK 999 THE SAMPLE SEQUENCE IS MDWRVLVVLLPVLLAAGWAVRNILPYAVKQVQKLLQKAKAA     
REMARK 999 (UNP Q8DKM3).                                                        
DBREF  4TNK A    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  4TNK B    1   510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  4TNK C   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  4TNK D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  4TNK E    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  4TNK F    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  4TNK H    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  4TNK I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4TNK J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4TNK K    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  4TNK L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4TNK M    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  4TNK O    1   272  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  4TNK T    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  4TNK U    1   134  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  4TNK V    1   163  UNP    P0A386   CY550_THEEB      1    163             
DBREF  4TNK y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  4TNK X   10    50  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  4TNK Y    1    28  PDB    4TNK     4TNK             1     28             
DBREF  4TNK Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  4TNK a    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  4TNK b    1   510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  4TNK c   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  4TNK d    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  4TNK e    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  4TNK f    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  4TNK h    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  4TNK i    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4TNK j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4TNK k    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  4TNK l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4TNK m    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  4TNK o    1   272  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  4TNK t    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  4TNK u    1   134  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  4TNK v    1   163  UNP    P0A386   CY550_THEEB      1    163             
DBREF  4TNK g    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  4TNK x   10    50  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  4TNK G    1    28  PDB    4TNK     4TNK             1     28             
DBREF  4TNK z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
SEQRES   1 A  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 A  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 A  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 A  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 A  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 A  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 A  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 A  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 A  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 A  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 A  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 A  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 A  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 A  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 A  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 A  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 A  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 A  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 A  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 A  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 A  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 A  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 A  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 A  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 A  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 A  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 A  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 B  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 B  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 B  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 B  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 B  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 B  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 B  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 B  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 B  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 B  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 B  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 B  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 B  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 B  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 B  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 B  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 B  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 B  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 B  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 B  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 B  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 B  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 B  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 B  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 B  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 B  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 B  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 B  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 B  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 B  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 B  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 B  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 B  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 B  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 B  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 B  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 B  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 B  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 B  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 B  510  GLU ALA VAL                                                  
SEQRES   1 C  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 C  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 C  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 C  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 C  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 C  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 C  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 C  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 C  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 C  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 C  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 C  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 C  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 C  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 C  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 C  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 C  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 C  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 C  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 C  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 C  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 C  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 C  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 C  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 C  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 C  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 C  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 C  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 C  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 C  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 C  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 C  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 C  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 C  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 C  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 C  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 D  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 D  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 D  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 D  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 D  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 D  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 D  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 D  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 D  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 D  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 D  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 D  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 D  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 D  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 D  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 D  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 D  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 D  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 D  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 D  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 D  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 D  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 D  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 D  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 D  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 D  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 D  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 D  352  LEU                                                          
SEQRES   1 E   84  MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE          
SEQRES   2 E   84  ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR          
SEQRES   3 E   84  ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER          
SEQRES   4 E   84  THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO          
SEQRES   5 E   84  ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU          
SEQRES   6 E   84  VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR          
SEQRES   7 E   84  PHE LEU GLU GLN LEU LYS                                      
SEQRES   1 F   45  MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR          
SEQRES   2 F   45  PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU          
SEQRES   3 F   45  ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA          
SEQRES   4 F   45  MET GLN PHE ILE GLN ARG                                      
SEQRES   1 H   66  MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO          
SEQRES   2 H   66  LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY          
SEQRES   3 H   66  THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU          
SEQRES   4 H   66  VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR          
SEQRES   5 H   66  LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU          
SEQRES   6 H   66  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   46  MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU          
SEQRES   2 K   46  ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO          
SEQRES   3 K   46  VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP          
SEQRES   4 K   46  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   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 M   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 M   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 O  272  MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL          
SEQRES   2 O  272  CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA          
SEQRES   3 O  272  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   4 O  272  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   5 O  272  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   6 O  272  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   7 O  272  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   8 O  272  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   9 O  272  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES  10 O  272  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES  11 O  272  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  12 O  272  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  13 O  272  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  14 O  272  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  15 O  272  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  16 O  272  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  17 O  272  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  18 O  272  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  19 O  272  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  20 O  272  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  21 O  272  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 T   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 T   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 T   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 U  134  MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE          
SEQRES   2 U  134  VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA          
SEQRES   3 U  134  PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU          
SEQRES   4 U  134  VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY          
SEQRES   5 U  134  GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE          
SEQRES   6 U  134  ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU          
SEQRES   7 U  134  ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL          
SEQRES   8 U  134  LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE          
SEQRES   9 U  134  LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL          
SEQRES  10 U  134  GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN          
SEQRES  11 U  134  GLY LEU TYR LYS                                              
SEQRES   1 V  163  MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS          
SEQRES   2 V  163  LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA          
SEQRES   3 V  163  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   4 V  163  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   5 V  163  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   6 V  163  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   7 V  163  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   8 V  163  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   9 V  163  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES  10 V  163  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES  11 V  163  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  12 V  163  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  13 V  163  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 y   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 y   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 y   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 y   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 X   41  MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY          
SEQRES   2 X   41  LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA          
SEQRES   3 X   41  VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG          
SEQRES   4 X   41  SER LEU                                                      
SEQRES   1 Y   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 Y   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 Y   28  UNK UNK                                                      
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  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 a  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 a  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 a  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 a  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 a  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 a  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 a  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 a  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 a  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 a  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 a  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 a  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 a  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 a  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 a  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 a  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 a  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 a  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 a  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 a  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 a  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 a  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 a  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 a  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 a  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 a  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 b  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 b  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 b  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 b  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 b  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 b  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 b  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 b  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 b  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 b  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 b  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 b  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 b  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 b  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 b  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 b  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 b  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 b  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 b  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 b  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 b  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 b  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 b  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 b  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 b  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 b  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 b  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 b  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 b  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 b  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 b  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 b  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 b  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 b  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 b  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 b  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 b  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 b  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 b  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 b  510  GLU ALA VAL                                                  
SEQRES   1 c  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 c  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 c  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 c  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 c  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 c  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 c  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 c  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 c  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 c  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 c  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 c  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 c  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 c  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 c  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 c  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 c  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 c  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 c  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 c  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 c  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 c  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 c  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 c  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 c  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 c  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 c  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 c  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 c  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 c  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 c  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 c  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 c  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 c  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 c  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 c  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 d  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 d  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 d  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 d  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 d  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 d  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 d  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 d  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 d  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 d  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 d  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 d  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 d  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 d  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 d  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 d  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 d  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 d  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 d  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 d  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 d  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 d  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 d  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 d  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 d  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 d  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 d  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 d  352  LEU                                                          
SEQRES   1 e   84  MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE          
SEQRES   2 e   84  ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR          
SEQRES   3 e   84  ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER          
SEQRES   4 e   84  THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO          
SEQRES   5 e   84  ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU          
SEQRES   6 e   84  VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR          
SEQRES   7 e   84  PHE LEU GLU GLN LEU LYS                                      
SEQRES   1 f   45  MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR          
SEQRES   2 f   45  PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU          
SEQRES   3 f   45  ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA          
SEQRES   4 f   45  MET GLN PHE ILE GLN ARG                                      
SEQRES   1 h   66  MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO          
SEQRES   2 h   66  LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY          
SEQRES   3 h   66  THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU          
SEQRES   4 h   66  VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR          
SEQRES   5 h   66  LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU          
SEQRES   6 h   66  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   46  MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU          
SEQRES   2 k   46  ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO          
SEQRES   3 k   46  VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP          
SEQRES   4 k   46  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   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 m   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 m   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 o  272  MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL          
SEQRES   2 o  272  CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA          
SEQRES   3 o  272  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   4 o  272  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   5 o  272  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   6 o  272  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   7 o  272  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   8 o  272  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   9 o  272  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES  10 o  272  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES  11 o  272  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  12 o  272  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  13 o  272  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  14 o  272  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  15 o  272  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  16 o  272  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  17 o  272  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  18 o  272  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  19 o  272  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  20 o  272  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  21 o  272  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 t   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 t   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 t   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 u  134  MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE          
SEQRES   2 u  134  VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA          
SEQRES   3 u  134  PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU          
SEQRES   4 u  134  VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY          
SEQRES   5 u  134  GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE          
SEQRES   6 u  134  ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU          
SEQRES   7 u  134  ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL          
SEQRES   8 u  134  LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE          
SEQRES   9 u  134  LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL          
SEQRES  10 u  134  GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN          
SEQRES  11 u  134  GLY LEU TYR LYS                                              
SEQRES   1 v  163  MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS          
SEQRES   2 v  163  LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA          
SEQRES   3 v  163  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   4 v  163  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   5 v  163  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   6 v  163  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   7 v  163  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   8 v  163  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   9 v  163  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES  10 v  163  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES  11 v  163  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  12 v  163  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  13 v  163  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 g   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 g   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 g   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 g   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 x   41  MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY          
SEQRES   2 x   41  LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA          
SEQRES   3 x   41  VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG          
SEQRES   4 x   41  SER LEU                                                      
SEQRES   1 G   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 G   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 G   28  UNK UNK                                                      
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    FE2  A 401       1                                                       
HET    CLA  A 402      65                                                       
HET    CLA  A 403      65                                                       
HET    CLA  A 404      65                                                       
HET    PHO  A 405      64                                                       
HET    CLA  A 406      65                                                       
HET    PL9  A 407      45                                                       
HET    BCR  A 408      40                                                       
HET    DGD  A 409      56                                                       
HET    LHG  A 410      39                                                       
HET     CL  A 411       1                                                       
HET    OEX  A 412      10                                                       
HET    SQD  A 413      51                                                       
HET    SQD  A 414      54                                                       
HET    CLA  B 601      65                                                       
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    BCR  B 616      40                                                       
HET    BCR  B 617      40                                                       
HET    BCR  B 618      40                                                       
HET    BCR  B 619      40                                                       
HET    DGD  B 620      58                                                       
HET    LMG  B 621      49                                                       
HET    SQD  B 622      43                                                       
HET    LMT  B 623      35                                                       
HET    LMT  B 624      35                                                       
HET    LMG  B 625      49                                                       
HET    DGD  B 626      52                                                       
HET    SQD  B 627      47                                                       
HET    LMT  B 628      35                                                       
HET    LMT  B 629      35                                                       
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    BCR  C 513      40                                                       
HET    DGD  C 514      53                                                       
HET    DGD  C 515      62                                                       
HET    DGD  C 516      66                                                       
HET    LMG  C 517      45                                                       
HET    LHG  C 518      37                                                       
HET    CLA  C 519      65                                                       
HET    BCR  C 520      40                                                       
HET    LMG  C 521      48                                                       
HET    PHO  D 401      64                                                       
HET    BCT  D 402       4                                                       
HET    CLA  D 403      65                                                       
HET    CLA  D 404      65                                                       
HET    PL9  D 405      55                                                       
HET    LMG  D 406      48                                                       
HET    DGD  D 407      63                                                       
HET    LMT  D 408      31                                                       
HET    LMG  D 409      46                                                       
HET    LMG  E 101      44                                                       
HET    HEM  F 101      43                                                       
HET    BCR  F 102      40                                                       
HET    SQD  F 103      45                                                       
HET    CLA  H 101      65                                                       
HET    BCR  H 102      40                                                       
HET    LMG  I 101      43                                                       
HET    LMT  I 102      35                                                       
HET    PL9  J 101      35                                                       
HET    BCR  J 102      40                                                       
HET    BCR  K 101      40                                                       
HET     CA  K 102       1                                                       
HET    LMG  L 101      51                                                       
HET    LMG  M 101      42                                                       
HET    LMT  M 102      35                                                       
HET    LMT  M 103      35                                                       
HET     CA  O 301       1                                                       
HET    HEM  V 201      43                                                       
HET    BCR  y 101      40                                                       
HET    SQD  a 401      54                                                       
HET    LMG  a 402      42                                                       
HET    CLA  a 403      65                                                       
HET    CLA  a 404      65                                                       
HET    CLA  a 405      65                                                       
HET    CLA  a 406      65                                                       
HET    PL9  a 407      45                                                       
HET    DGD  a 408      56                                                       
HET    LHG  a 409      39                                                       
HET     CL  a 410       1                                                       
HET    OEX  a 411      10                                                       
HET    SQD  a 412      51                                                       
HET    FE2  a 413       1                                                       
HET    DGD  b 601      52                                                       
HET    SQD  b 602      47                                                       
HET    LMT  b 603      35                                                       
HET    LMT  b 604      35                                                       
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    CLA  b 618      65                                                       
HET    CLA  b 619      65                                                       
HET    CLA  b 620      65                                                       
HET    BCR  b 621      40                                                       
HET    BCR  b 622      40                                                       
HET    BCR  b 623      40                                                       
HET    BCR  b 624      40                                                       
HET    DGD  b 625      58                                                       
HET    LMG  b 626      49                                                       
HET    LMG  b 627      42                                                       
HET    LMT  b 628      35                                                       
HET    LMT  b 629      35                                                       
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    BCR  c 513      40                                                       
HET    BCR  c 514      40                                                       
HET    DGD  c 515      53                                                       
HET    DGD  c 516      62                                                       
HET    DGD  c 517      66                                                       
HET    LMG  c 518      45                                                       
HET    LHG  c 519      37                                                       
HET    CLA  c 520      65                                                       
HET    BCR  c 521      40                                                       
HET    LMG  c 522      48                                                       
HET    PHO  d 401      64                                                       
HET    PHO  d 402      64                                                       
HET    SQD  d 403      43                                                       
HET    BCT  d 404       4                                                       
HET    CLA  d 405      65                                                       
HET    CLA  d 406      65                                                       
HET    PL9  d 407      55                                                       
HET    LMG  d 408      49                                                       
HET    LMG  d 409      48                                                       
HET    DGD  d 410      63                                                       
HET    LMT  d 411      31                                                       
HET    LMG  d 412      46                                                       
HET    LMG  e 101      44                                                       
HET    HEM  f 101      43                                                       
HET    BCR  f 102      40                                                       
HET    SQD  f 103      45                                                       
HET    BCR  i 101      40                                                       
HET    LMG  i 102      43                                                       
HET    LMT  i 103      35                                                       
HET    PL9  j 101      35                                                       
HET    BCR  j 102      40                                                       
HET     CA  k 101       1                                                       
HET    LMG  l 101      51                                                       
HET    LMG  m 101      42                                                       
HET     CA  o 301       1                                                       
HET    HEM  v 201      43                                                       
HET    BCR  g 101      40                                                       
HET    BCR  x 101      40                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN A                                                     
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     BCR BETA-CAROTENE                                                    
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM      CL CHLORIDE ION                                                     
HETNAM     OEX CA-MN4-O5 CLUSTER                                                
HETNAM     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      CA CALCIUM ION                                                      
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     HEM HEME                                                             
FORMUL  41  FE2    2(FE 2+)                                                     
FORMUL  42  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  45  PHO    4(C55 H74 N4 O5)                                             
FORMUL  47  PL9    6(C53 H80 O2)                                                
FORMUL  48  BCR    24(C40 H56)                                                  
FORMUL  49  DGD    14(C51 H96 O15)                                              
FORMUL  50  LHG    4(C38 H75 O10 P)                                             
FORMUL  51   CL    2(CL 1-)                                                     
FORMUL  52  OEX    2(CA MN4 O5)                                                 
FORMUL  53  SQD    10(C41 H78 O12 S)                                            
FORMUL  75  LMG    22(C45 H86 O10)                                              
FORMUL  77  LMT    14(C24 H46 O11)                                              
FORMUL  06  BCT    2(C H O3 1-)                                                 
FORMUL  15  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  25   CA    4(CA 2+)                                                     
HELIX    1 AA1 ASN A   12  THR A   22  1                                  11    
HELIX    2 AA2 PHE A   33  ALA A   55  1                                  23    
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  MET A  293  1                                  27    
HELIX   17 AB8 THR A  316  HIS A  332  1                                  17    
HELIX   18 AB9 GLU A  333  HIS A  337  5                                   5    
HELIX   19 AC1 PRO B    4  ILE B   13  5                                  10    
HELIX   20 AC2 ASP B   15  ALA B   43  1                                  29    
HELIX   21 AC3 PRO B   54  GLN B   58  5                                   5    
HELIX   22 AC4 VAL B   62  ARG B   68  1                                   7    
HELIX   23 AC5 SER B   92  TYR B  117  1                                  26    
HELIX   24 AC6 LEU B  120  ARG B  124  5                                   5    
HELIX   25 AC7 ASP B  134  PHE B  156  1                                  23    
HELIX   26 AC8 GLY B  186  ASN B  191  5                                   6    
HELIX   27 AC9 ASN B  194  VAL B  219  1                                  26    
HELIX   28 AD1 PRO B  222  LEU B  229  1                                   8    
HELIX   29 AD2 ASN B  233  GLU B  235  5                                   3    
HELIX   30 AD3 THR B  236  TYR B  258  1                                  23    
HELIX   31 AD4 PRO B  264  GLY B  269  1                                   6    
HELIX   32 AD5 THR B  271  SER B  277  1                                   7    
HELIX   33 AD6 SER B  278  SER B  294  1                                  17    
HELIX   34 AD7 THR B  297  ILE B  305  1                                   9    
HELIX   35 AD8 PRO B  306  TYR B  312  1                                   7    
HELIX   36 AD9 ASP B  313  ASN B  318  5                                   6    
HELIX   37 AE1 PRO B  329  GLY B  333  5                                   5    
HELIX   38 AE2 ARG B  384  SER B  388  5                                   5    
HELIX   39 AE3 SER B  391  GLY B  396  1                                   6    
HELIX   40 AE4 ASP B  413  ILE B  425  1                                  13    
HELIX   41 AE5 SER B  446  PHE B  475  1                                  30    
HELIX   42 AE6 ALA C   34  ILE C   43  5                                  10    
HELIX   43 AE7 LEU C   45  PHE C   75  1                                  31    
HELIX   44 AE8 PRO C   80  GLN C   84  5                                   5    
HELIX   45 AE9 LEU C   88  LEU C   95  1                                   8    
HELIX   46 AF1 GLY C  100  GLU C  104  5                                   5    
HELIX   47 AF2 THR C  108  ARG C  135  1                                  28    
HELIX   48 AF3 ASP C  153  PHE C  181  1                                  29    
HELIX   49 AF4 ASP C  205  PHE C  210  1                                   6    
HELIX   50 AF5 GLY C  211  LYS C  215  5                                   5    
HELIX   51 AF6 GLY C  222  VAL C  227  5                                   6    
HELIX   52 AF7 ASN C  229  LEU C  253  1                                  25    
HELIX   53 AF8 GLY C  258  PHE C  264  1                                   7    
HELIX   54 AF9 SER C  267  ASN C  293  1                                  27    
HELIX   55 AG1 THR C  305  LEU C  324  1                                  20    
HELIX   56 AG2 ASN C  327  ALA C  331  5                                   5    
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 TRP D   14  LYS D   23  1                                  10    
HELIX   64 AH1 VAL D   30  PHE D   54  1                                  25    
HELIX   65 AH2 SER D   57  GLY D   62  1                                   6    
HELIX   66 AH3 SER D   66  GLY D   70  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  PHE D  146  1                                   7    
HELIX   70 AH7 PHE D  146  LEU D  158  1                                  13    
HELIX   71 AH8 LEU D  158  GLN D  164  1                                   7    
HELIX   72 AH9 SER D  166  ALA D  170  5                                   5    
HELIX   73 AI1 VAL D  175  ASN D  190  1                                  16    
HELIX   74 AI2 TRP D  191  LEU D  193  5                                   3    
HELIX   75 AI3 ASN D  194  ASN D  220  1                                  27    
HELIX   76 AI4 SER D  245  PHE D  257  1                                  13    
HELIX   77 AI5 ASN D  263  LEU D  291  1                                  29    
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  SER E   16  1                                   8    
HELIX   83 AJ2 SER E   16  THR E   40  1                                  25    
HELIX   84 AJ3 GLY E   41  PHE E   47  1                                   7    
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 THR H   27  ASN H   50  1                                  24    
HELIX   89 AJ8 GLU I    2  SER I   25  1                                  24    
HELIX   90 AJ9 PRO J    9  ALA J   32  1                                  24    
HELIX   91 AK1 PRO K   12  ILE K   17  5                                   6    
HELIX   92 AK2 PHE K   18  ASP K   23  1                                   6    
HELIX   93 AK3 VAL K   24  PRO K   26  5                                   3    
HELIX   94 AK4 VAL K   27  VAL K   43  1                                  17    
HELIX   95 AK5 ASN L   13  ASN L   37  1                                  25    
HELIX   96 AK6 LEU M    6  SER M   31  1                                  26    
HELIX   97 AK7 GLY O   40  LYS O   44  5                                   5    
HELIX   98 AK8 LEU O  208  VAL O  213  1                                   6    
HELIX   99 AK9 GLU T    2  PHE T   23  1                                  22    
HELIX  100 AL1 ASN U   41  LEU U   47  1                                   7    
HELIX  101 AL2 ASN U   61  TYR U   68  5                                   8    
HELIX  102 AL3 PRO U   73  ASN U   82  1                                  10    
HELIX  103 AL4 SER U   87  ILE U   94  5                                   8    
HELIX  104 AL5 THR U   98  LEU U  109  1                                  12    
HELIX  105 AL6 GLU U  118  GLU U  123  1                                   6    
HELIX  106 AL7 GLY U  124  ASP U  126  5                                   3    
HELIX  107 AL8 THR V   48  CYS V   63  1                                  16    
HELIX  108 AL9 CYS V   63  VAL V   68  1                                   6    
HELIX  109 AM1 GLY V   69  ILE V   71  5                                   3    
HELIX  110 AM2 ARG V   81  LEU V   87  1                                   7    
HELIX  111 AM3 ASN V   94  MET V  102  1                                   9    
HELIX  112 AM4 SER V  120  ALA V  124  5                                   5    
HELIX  113 AM5 PRO V  128  LEU V  133  1                                   6    
HELIX  114 AM6 THR V  134  GLY V  153  1                                  20    
HELIX  115 AM7 GLY V  153  GLY V  158  1                                   6    
HELIX  116 AM8 GLY V  159  TYR V  163  5                                   5    
HELIX  117 AM9 GLN y   21  ARG y   42  1                                  22    
HELIX  118 AN1 THR X   13  GLN X   42  1                                  30    
HELIX  119 AN2 UNK Y    2  UNK Y   12  1                                  11    
HELIX  120 AN3 UNK Y   14  UNK Y   25  1                                  12    
HELIX  121 AN4 THR Z    2  SER Z   29  1                                  28    
HELIX  122 AN5 ARG Z   35  VAL Z   62  1                                  28    
HELIX  123 AN6 ASN a   12  THR a   22  1                                  11    
HELIX  124 AN7 PHE a   33  ALA a   55  1                                  23    
HELIX  125 AN8 SER a   70  GLY a   74  5                                   5    
HELIX  126 AN9 PRO a   95  ALA a   99  5                                   5    
HELIX  127 AO1 SER a  101  ASN a  108  1                                   8    
HELIX  128 AO2 GLY a  109  LEU a  137  1                                  29    
HELIX  129 AO3 TRP a  142  TYR a  147  1                                   6    
HELIX  130 AO4 TYR a  147  LEU a  159  1                                  13    
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 ASN a  247  ILE a  259  1                                  13    
HELIX  137 AP2 PHE a  260  SER a  264  5                                   5    
HELIX  138 AP3 ASN a  267  MET a  293  1                                  27    
HELIX  139 AP4 THR a  316  HIS a  332  1                                  17    
HELIX  140 AP5 GLU a  333  HIS a  337  5                                   5    
HELIX  141 AP6 PRO b    4  ILE b   13  5                                  10    
HELIX  142 AP7 ASP b   15  ALA b   43  1                                  29    
HELIX  143 AP8 PRO b   54  GLN b   58  5                                   5    
HELIX  144 AP9 VAL b   62  ARG b   68  1                                   7    
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  GLU b  235  5                                   3    
HELIX  152 AQ8 THR b  236  TYR b  258  1                                  23    
HELIX  153 AQ9 PRO b  264  GLY b  269  1                                   6    
HELIX  154 AR1 THR b  271  SER b  277  1                                   7    
HELIX  155 AR2 SER b  278  SER b  294  1                                  17    
HELIX  156 AR3 THR b  297  ILE b  305  1                                   9    
HELIX  157 AR4 PRO b  306  TYR b  312  1                                   7    
HELIX  158 AR5 ASP b  313  ASN b  318  5                                   6    
HELIX  159 AR6 PRO b  329  GLY b  333  5                                   5    
HELIX  160 AR7 ARG b  384  SER b  388  5                                   5    
HELIX  161 AR8 SER b  391  GLY b  396  1                                   6    
HELIX  162 AR9 ASP b  413  ILE b  425  1                                  13    
HELIX  163 AS1 SER b  446  PHE b  475  1                                  30    
HELIX  164 AS2 ALA c   34  ILE c   43  5                                  10    
HELIX  165 AS3 LEU c   45  PHE c   75  1                                  31    
HELIX  166 AS4 PRO c   80  GLN c   84  5                                   5    
HELIX  167 AS5 LEU c   88  LEU c   95  1                                   8    
HELIX  168 AS6 GLY c  100  GLU c  104  5                                   5    
HELIX  169 AS7 THR c  108  ARG c  135  1                                  28    
HELIX  170 AS8 ASP c  153  PHE c  181  1                                  29    
HELIX  171 AS9 ASP c  205  PHE c  210  1                                   6    
HELIX  172 AT1 GLY c  211  LYS c  215  5                                   5    
HELIX  173 AT2 GLY c  222  VAL c  227  5                                   6    
HELIX  174 AT3 ASN c  229  LEU c  253  1                                  25    
HELIX  175 AT4 GLY c  258  PHE c  264  1                                   7    
HELIX  176 AT5 SER c  267  ASN c  293  1                                  27    
HELIX  177 AT6 THR c  305  LEU c  324  1                                  20    
HELIX  178 AT7 ASN c  327  ALA c  331  5                                   5    
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 GLU c  464  MET c  469  5                                   6    
HELIX  185 AU5 TRP d   14  LYS d   23  1                                  10    
HELIX  186 AU6 VAL d   30  PHE d   54  1                                  25    
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 ASP d  100  LEU d  107  1                                   8    
HELIX  190 AV1 GLY d  108  GLY d  137  1                                  30    
HELIX  191 AV2 PRO d  140  PHE d  146  1                                   7    
HELIX  192 AV3 PHE d  146  LEU d  158  1                                  13    
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 SER d  245  PHE d  257  1                                  13    
HELIX  199 AW1 ASN d  263  LEU d  291  1                                  29    
HELIX  200 AW2 PHE d  298  ASP d  308  1                                  11    
HELIX  201 AW3 THR d  313  GLN d  334  1                                  22    
HELIX  202 AW4 PRO d  335  ASN d  338  5                                   4    
HELIX  203 AW5 PRO d  342  LEU d  346  5                                   5    
HELIX  204 AW6 PRO e    9  SER e   16  1                                   8    
HELIX  205 AW7 SER e   16  THR e   40  1                                  25    
HELIX  206 AW8 GLY e   41  PHE e   47  1                                   7    
HELIX  207 AW9 GLU e   71  GLN e   82  1                                  12    
HELIX  208 AX1 THR f   17  GLN f   41  1                                  25    
HELIX  209 AX2 THR h    5  LEU h   11  1                                   7    
HELIX  210 AX3 THR h   27  ASN h   50  1                                  24    
HELIX  211 AX4 GLU i    2  SER i   25  1                                  24    
HELIX  212 AX5 PRO j    9  ALA j   32  1                                  24    
HELIX  213 AX6 PRO k   12  ILE k   17  5                                   6    
HELIX  214 AX7 PHE k   18  ASP k   23  1                                   6    
HELIX  215 AX8 VAL k   24  PRO k   26  5                                   3    
HELIX  216 AX9 VAL k   27  VAL k   43  1                                  17    
HELIX  217 AY1 ASN l   13  ASN l   37  1                                  25    
HELIX  218 AY2 LEU m    6  SER m   31  1                                  26    
HELIX  219 AY3 THR o   32  ILE o   36  5                                   5    
HELIX  220 AY4 GLY o   40  LYS o   44  5                                   5    
HELIX  221 AY5 LEU o  208  VAL o  213  1                                   6    
HELIX  222 AY6 GLU t    2  PHE t   23  1                                  22    
HELIX  223 AY7 ASN u   41  LEU u   47  1                                   7    
HELIX  224 AY8 ASN u   61  TYR u   68  5                                   8    
HELIX  225 AY9 PRO u   73  ASN u   82  1                                  10    
HELIX  226 AZ1 SER u   87  ILE u   94  5                                   8    
HELIX  227 AZ2 THR u   98  LEU u  109  1                                  12    
HELIX  228 AZ3 GLU u  118  GLU u  123  1                                   6    
HELIX  229 AZ4 GLY u  124  ASP u  126  5                                   3    
HELIX  230 AZ5 THR v   48  CYS v   63  1                                  16    
HELIX  231 AZ6 CYS v   63  VAL v   68  1                                   6    
HELIX  232 AZ7 GLY v   69  ILE v   71  5                                   3    
HELIX  233 AZ8 ARG v   81  LEU v   87  1                                   7    
HELIX  234 AZ9 ASN v   94  MET v  102  1                                   9    
HELIX  235 BA1 SER v  120  ALA v  124  5                                   5    
HELIX  236 BA2 PHE v  127  ARG v  131  5                                   5    
HELIX  237 BA3 THR v  134  GLY v  153  1                                  20    
HELIX  238 BA4 GLY v  153  GLY v  158  1                                   6    
HELIX  239 BA5 GLN g   21  ARG g   42  1                                  22    
HELIX  240 BA6 THR x   13  GLN x   42  1                                  30    
HELIX  241 BA7 UNK G    2  UNK G   12  1                                  11    
HELIX  242 BA8 UNK G   14  UNK G   25  1                                  12    
HELIX  243 BA9 THR z    2  SER z   29  1                                  28    
HELIX  244 BB1 ARG z   35  VAL z   62  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  SER B 177   N  VAL B 168           
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  THR B 398   N  ARG B 347           
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  ARG C 197   N  LEU C 185           
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  56  PRO O  57  0                                        
SHEET    2 AB1 2 SER O 161  ILE O 162 -1  O  ILE O 162   N  TYR O  56           
SHEET    1 AB210 PHE O  91  PRO O  93  0                                        
SHEET    2 AB210 ARG O  65  LYS O  79 -1  N  VAL O  78   O  VAL O  92           
SHEET    3 AB210 GLU O 258  GLU O 270 -1  O  GLN O 262   N  THR O  74           
SHEET    4 AB210 GLU O 236  LEU O 246 -1  N  SER O 243   O  ILE O 261           
SHEET    5 AB210 LEU O 218  LYS O 229 -1  N  ALA O 228   O  ALA O 238           
SHEET    6 AB210 PHE O 168  PRO O 175 -1  N  VAL O 174   O  THR O 219           
SHEET    7 AB210 VAL O 152  SER O 154 -1  N  SER O 154   O  LYS O 169           
SHEET    8 AB210 LEU O 119  ILE O 127 -1  N  PHE O 121   O  ALA O 153           
SHEET    9 AB210 LEU O 104  VAL O 113 -1  N  GLN O 108   O  GLU O 124           
SHEET   10 AB210 ARG O  65  LYS O  79 -1  N  LEU O  71   O  LEU O 104           
SHEET    1 AB3 3 LYS O  95  LEU O  96  0                                        
SHEET    2 AB3 3 PHE O 129  GLN O 135 -1  O  GLN O 135   N  LYS O  95           
SHEET    3 AB3 3 ARG O 141  THR O 147 -1  O  ILE O 142   N  VAL O 134           
SHEET    1 AB4 2 ILE U  55  ASP U  56  0                                        
SHEET    2 AB4 2 PHE U 112  THR U 113  1  O  THR U 113   N  ILE U  55           
SHEET    1 AB5 2 THR V  35  PRO V  37  0                                        
SHEET    2 AB5 2 THR V  44  THR V  46 -1  O  ILE V  45   N  VAL V  36           
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  SER b 177   N  VAL b 168           
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  SER b 400   N  VAL b 345           
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  ARG c 197   N  LEU c 185           
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  56  PRO o  57  0                                        
SHEET    2 AC6 2 SER o 161  ILE o 162 -1  O  ILE o 162   N  TYR o  56           
SHEET    1 AC710 PHE o  91  PRO o  93  0                                        
SHEET    2 AC710 ARG o  65  LYS o  79 -1  N  VAL o  78   O  VAL o  92           
SHEET    3 AC710 GLU o 258  GLU o 270 -1  O  LYS o 260   N  LEU o  77           
SHEET    4 AC710 GLU o 236  LEU o 246 -1  N  SER o 243   O  ILE o 261           
SHEET    5 AC710 LEU o 218  LYS o 229 -1  N  GLN o 222   O  GLU o 244           
SHEET    6 AC710 PHE o 168  PRO o 175 -1  N  VAL o 174   O  THR o 219           
SHEET    7 AC710 LYS o 149  SER o 154 -1  N  LYS o 149   O  ASN o 173           
SHEET    8 AC710 LEU o 119  ILE o 127 -1  N  PHE o 121   O  ALA o 153           
SHEET    9 AC710 LEU o 104  VAL o 113 -1  N  GLN o 108   O  GLU o 124           
SHEET   10 AC710 ARG o  65  LYS o  79 -1  N  LEU o  71   O  LEU o 104           
SHEET    1 AC8 3 LYS o  95  LEU o  96  0                                        
SHEET    2 AC8 3 PHE o 129  GLN o 135 -1  O  GLN o 135   N  LYS o  95           
SHEET    3 AC8 3 ARG o 141  THR o 147 -1  O  ILE o 142   N  VAL o 134           
SHEET    1 AC9 2 ILE u  55  ASP u  56  0                                        
SHEET    2 AC9 2 PHE u 112  THR u 113  1  O  THR u 113   N  ILE u  55           
SHEET    1 AD1 2 THR v  35  PRO v  37  0                                        
SHEET    2 AD1 2 THR v  44  THR v  46 -1  O  ILE v  45   N  VAL v  36           
SSBOND   1 CYS O   45    CYS O   70                          1555   1555  2.03  
SSBOND   2 CYS o   45    CYS o   70                          1555   1555  2.03  
LINK         OD1 ASP A 170                CA1  OEX A 412     1555   1555  3.03  
LINK         OD2 ASP A 170                MN4  OEX A 412     1555   1555  2.67  
LINK         OE1 GLU A 189                CA1  OEX A 412     1555   1555  3.04  
LINK         OE2 GLU A 189                MN1  OEX A 412     1555   1555  2.49  
LINK         NE2 HIS A 215                FE   FE2 A 401     1555   1555  2.57  
LINK         NE2 HIS A 272                FE   FE2 A 401     1555   1555  2.56  
LINK         NE2 HIS A 332                MN1  OEX A 412     1555   1555  2.57  
LINK         OE1 GLU A 333                MN3  OEX A 412     1555   1555  2.56  
LINK         OE2 GLU A 333                MN4  OEX A 412     1555   1555  2.77  
LINK         OD1 ASP A 342                MN2  OEX A 412     1555   1555  2.59  
LINK         OXT ALA A 344                MN2  OEX A 412     1555   1555  2.62  
LINK         OD1 ASN C  39                MG   CLA C 510     1555   1555  2.95  
LINK         OE1 GLU C 354                MN2  OEX A 412     1555   1555  2.77  
LINK         OE2 GLU C 354                MN3  OEX A 412     1555   1555  2.65  
LINK         NE2 HIS D 214                FE   FE2 A 401     1555   1555  2.50  
LINK         NE2 HIS D 268                FE   FE2 A 401     1555   1555  2.73  
LINK         NE2 HIS E  23                FE   HEM F 101     1555   1555  2.58  
LINK         NE2 HIS F  24                FE   HEM F 101     1555   1555  2.62  
LINK         OD2 ASP K  19                CA    CA K 102     1555   1555  2.55  
LINK         OD1 ASP K  23                CA    CA K 102     1555   1555  3.16  
LINK         OD2 ASP K  23                CA    CA K 102     1555   1555  2.98  
LINK         OE1 GLU O 140                CA    CA O 301     1555   1555  2.67  
LINK         NE2 HIS V  67                FE   HEM V 201     1555   1555  2.47  
LINK         NE2 HIS V 118                FE   HEM V 201     1555   1555  2.57  
LINK         C   UNK Y   1                 N   UNK Y   2     1555   1555  1.33  
LINK         C   UNK Y   2                 N   UNK Y   3     1555   1555  1.33  
LINK         C   UNK Y   3                 N   UNK Y   4     1555   1555  1.33  
LINK         C   UNK Y   4                 N   UNK Y   5     1555   1555  1.33  
LINK         C   UNK Y   5                 N   UNK Y   6     1555   1555  1.33  
LINK         C   UNK Y   6                 N   UNK Y   7     1555   1555  1.33  
LINK         C   UNK Y   7                 N   UNK Y   8     1555   1555  1.33  
LINK         C   UNK Y   8                 N   UNK Y   9     1555   1555  1.33  
LINK         C   UNK Y   9                 N   UNK Y  10     1555   1555  1.33  
LINK         C   UNK Y  10                 N   UNK Y  11     1555   1555  1.33  
LINK         C   UNK Y  11                 N   UNK Y  12     1555   1555  1.33  
LINK         C   UNK Y  12                 N   UNK Y  13     1555   1555  1.33  
LINK         C   UNK Y  13                 N   UNK Y  14     1555   1555  1.33  
LINK         C   UNK Y  14                 N   UNK Y  15     1555   1555  1.33  
LINK         C   UNK Y  15                 N   UNK Y  16     1555   1555  1.33  
LINK         C   UNK Y  16                 N   UNK Y  17     1555   1555  1.33  
LINK         C   UNK Y  17                 N   UNK Y  18     1555   1555  1.33  
LINK         C   UNK Y  18                 N   UNK Y  19     1555   1555  1.33  
LINK         C   UNK Y  19                 N   UNK Y  20     1555   1555  1.33  
LINK         C   UNK Y  20                 N   UNK Y  21     1555   1555  1.33  
LINK         C   UNK Y  21                 N   UNK Y  22     1555   1555  1.33  
LINK         C   UNK Y  22                 N   UNK Y  23     1555   1555  1.33  
LINK         C   UNK Y  23                 N   UNK Y  24     1555   1555  1.33  
LINK         C   UNK Y  24                 N   UNK Y  25     1555   1555  1.33  
LINK         C   UNK Y  25                 N   UNK Y  26     1555   1555  1.33  
LINK         C   UNK Y  26                 N   UNK Y  27     1555   1555  1.33  
LINK         C   UNK Y  27                 N   UNK Y  28     1555   1555  1.33  
LINK         OD1 ASP a 170                CA1  OEX a 411     1555   1555  3.04  
LINK         OD2 ASP a 170                MN4  OEX a 411     1555   1555  2.65  
LINK         OE1 GLU a 189                CA1  OEX a 411     1555   1555  3.09  
LINK         OE2 GLU a 189                MN1  OEX a 411     1555   1555  2.54  
LINK         NE2 HIS a 215                FE   FE2 a 413     1555   1555  2.61  
LINK         NE2 HIS a 272                FE   FE2 a 413     1555   1555  2.55  
LINK         NE2 HIS a 332                MN1  OEX a 411     1555   1555  2.57  
LINK         OE1 GLU a 333                MN3  OEX a 411     1555   1555  2.57  
LINK         OD1 ASP a 342                MN2  OEX a 411     1555   1555  2.62  
LINK         OXT ALA a 344                MN2  OEX a 411     1555   1555  2.67  
LINK         OD1 ASN c  39                MG   CLA c 510     1555   1555  2.98  
LINK         OE1 GLU c 354                MN2  OEX a 411     1555   1555  2.80  
LINK         OE2 GLU c 354                MN3  OEX a 411     1555   1555  2.71  
LINK         NE2 HIS d 214                FE   FE2 a 413     1555   1555  2.54  
LINK         NE2 HIS d 268                FE   FE2 a 413     1555   1555  2.71  
LINK         NE2 HIS e  23                FE   HEM f 101     1555   1555  2.61  
LINK         NE2 HIS f  24                FE   HEM f 101     1555   1555  2.63  
LINK         OD2 ASP k  19                CA    CA k 101     1555   1555  2.67  
LINK         OD1 ASP k  23                CA    CA k 101     1555   1555  2.97  
LINK         OD2 ASP k  23                CA    CA k 101     1555   1555  2.91  
LINK         OE1 GLU o 140                CA    CA o 301     1555   1555  2.68  
LINK         NE2 HIS v  67                FE   HEM v 201     1555   1555  2.51  
LINK         NE2 HIS v 118                FE   HEM v 201     1555   1555  2.67  
LINK         C   UNK G   1                 N   UNK G   2     1555   1555  1.33  
LINK         C   UNK G   2                 N   UNK G   3     1555   1555  1.33  
LINK         C   UNK G   3                 N   UNK G   4     1555   1555  1.33  
LINK         C   UNK G   4                 N   UNK G   5     1555   1555  1.33  
LINK         C   UNK G   5                 N   UNK G   6     1555   1555  1.33  
LINK         C   UNK G   6                 N   UNK G   7     1555   1555  1.33  
LINK         C   UNK G   7                 N   UNK G   8     1555   1555  1.33  
LINK         C   UNK G   8                 N   UNK G   9     1555   1555  1.33  
LINK         C   UNK G   9                 N   UNK G  10     1555   1555  1.33  
LINK         C   UNK G  10                 N   UNK G  11     1555   1555  1.33  
LINK         C   UNK G  11                 N   UNK G  12     1555   1555  1.33  
LINK         C   UNK G  12                 N   UNK G  13     1555   1555  1.33  
LINK         C   UNK G  13                 N   UNK G  14     1555   1555  1.33  
LINK         C   UNK G  14                 N   UNK G  15     1555   1555  1.33  
LINK         C   UNK G  15                 N   UNK G  16     1555   1555  1.33  
LINK         C   UNK G  16                 N   UNK G  17     1555   1555  1.33  
LINK         C   UNK G  17                 N   UNK G  18     1555   1555  1.33  
LINK         C   UNK G  18                 N   UNK G  19     1555   1555  1.33  
LINK         C   UNK G  19                 N   UNK G  20     1555   1555  1.33  
LINK         C   UNK G  20                 N   UNK G  21     1555   1555  1.33  
LINK         C   UNK G  21                 N   UNK G  22     1555   1555  1.33  
LINK         C   UNK G  22                 N   UNK G  23     1555   1555  1.33  
LINK         C   UNK G  23                 N   UNK G  24     1555   1555  1.33  
LINK         C   UNK G  24                 N   UNK G  25     1555   1555  1.33  
LINK         C   UNK G  25                 N   UNK G  26     1555   1555  1.33  
LINK         C   UNK G  26                 N   UNK G  27     1555   1555  1.33  
LINK         C   UNK G  27                 N   UNK G  28     1555   1555  1.33  
LINK        FE   FE2 A 401                 O2  BCT D 402     1555   1555  2.70  
LINK        FE   FE2 A 401                 O3  BCT D 402     1555   1555  2.67  
LINK        FE   FE2 a 413                 O2  BCT d 404     1555   1555  2.64  
LINK        FE   FE2 a 413                 O3  BCT d 404     1555   1555  2.68  
CISPEP   1 THR V   89    PRO V   90          0        -0.84                     
CISPEP   2 THR v   89    PRO v   90          0        -0.93                     
SITE     1 AC1  5 HIS A 215  HIS A 272  HIS D 214  HIS D 268                    
SITE     2 AC1  5 BCT D 402                                                     
SITE     1 AC2 24 PHE A 119  TYR A 147  PRO A 150  SER A 153                    
SITE     2 AC2 24 VAL A 157  MET A 183  PHE A 186  GLN A 187                    
SITE     3 AC2 24 ILE A 192  LEU A 193  HIS A 198  GLY A 201                    
SITE     4 AC2 24 VAL A 205  PHE A 206  VAL A 283  THR A 286                    
SITE     5 AC2 24 ILE A 290  CLA A 403  CLA A 404  PHO A 405                    
SITE     6 AC2 24 LEU D 182  LEU D 205  CLA D 403  PHE T  17                    
SITE     1 AC3 14 THR A  45  VAL A 157  PHE A 158  MET A 172                    
SITE     2 AC3 14 ILE A 176  THR A 179  MET A 183  CLA A 402                    
SITE     3 AC3 14 PHO A 405  MET D 198  VAL D 201  ALA D 202                    
SITE     4 AC3 14 CLA D 403  PL9 D 405                                          
SITE     1 AC4 14 GLN A 199  VAL A 202  ALA A 203  TRP A 278                    
SITE     2 AC4 14 CLA A 402  PL9 A 407  PHE D 157  VAL D 175                    
SITE     3 AC4 14 ILE D 178  PHE D 179  PHE D 181  LEU D 182                    
SITE     4 AC4 14 PHO D 401  CLA D 403                                          
SITE     1 AC5 17 ALA A  44  THR A  45  ILE A 115  TYR A 126                    
SITE     2 AC5 17 GLN A 130  TYR A 147  VAL A 283  CLA A 402                    
SITE     3 AC5 17 CLA A 403  SQD A 414  LEU D 205  ALA D 208                    
SITE     4 AC5 17 LEU D 209  ALA D 212  ILE D 213  TRP D 253                    
SITE     5 AC5 17 PHE D 257                                                     
SITE     1 AC6 14 ILE A  36  PRO A  39  THR A  40  PHE A  93                    
SITE     2 AC6 14 PRO A  95  ILE A  96  TRP A  97  LEU A 114                    
SITE     3 AC6 14 HIS A 118  LEU A 121  BCR A 408  VAL I   8                    
SITE     4 AC6 14 TYR I   9  PHE I  15                                          
SITE     1 AC7 15 HIS A 215  LEU A 218  HIS A 252  PHE A 255                    
SITE     2 AC7 15 SER A 264  PHE A 265  LEU A 271  PHE A 274                    
SITE     3 AC7 15 CLA A 404  PHE D  38  ALA D  41  TYR D  42                    
SITE     4 AC7 15 LEU D  45  THR F  25  PL9 J 101                               
SITE     1 AC8  8 LEU A  42  ALA A  43  TRP A 105  LEU A 106                    
SITE     2 AC8  8 CLA A 406  SQD A 414  PHE I  15  LMT b 603                    
SITE     1 AC9 14 PHE A  93  TRP A  97  GLU A  98  PHE A 155                    
SITE     2 AC9 14 LEU C 214  LYS C 215  SER C 216  PRO C 217                    
SITE     3 AC9 14 PHE C 218  TRP C 223  PHE C 284  LYS I   5                    
SITE     4 AC9 14 TYR I   9  GLY O  38                                          
SITE     1 AD1 15 ARG A 140  TRP A 142  PHE A 273  SQD A 413                    
SITE     2 AD1 15 TRP C  36  TRP C 443  ARG C 447  CLA C 507                    
SITE     3 AD1 15 CLA C 509  CLA C 519  ASN D 220  ALA D 229                    
SITE     4 AD1 15 SER D 230  THR D 231  PHE D 232                               
SITE     1 AD2  2 ASN A 181  LYS D 317                                          
SITE     1 AD3  9 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 AD3  9 HIS A 337  ASP A 342  ALA A 344  GLU C 354                    
SITE     3 AD3  9 ARG C 357                                                     
SITE     1 AD4 15 ASN A 267  SER A 270  PHE A 273  PHE A 274                    
SITE     2 AD4 15 TRP A 278  LHG A 410  TRP C  35  TRP C  36                    
SITE     3 AD4 15 DGD C 515  DGD C 516  LHG C 518  PHE D 232                    
SITE     4 AD4 15 ARG D 233  BCR J 102  PHE K  37                               
SITE     1 AD5 13 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 AD5 13 THR A  45  PHO A 405  BCR A 408  TRP b 113                    
SITE     3 AD5 13 TYR b 117  CLA b 610  CLA b 620  BCR b 622                    
SITE     4 AD5 13 BCR b 624                                                     
SITE     1 AD6  9 TRP B 185  PRO B 187  PHE B 190  ILE B 207                    
SITE     2 AD6  9 VAL B 208  PHE H  41  ILE H  44  CLA H 101                    
SITE     3 AD6  9 BCR H 102                                                     
SITE     1 AD7 19 ARG B  68  LEU B  69  ALA B 146  LEU B 149                    
SITE     2 AD7 19 CYS B 150  PHE B 153  VAL B 198  HIS B 201                    
SITE     3 AD7 19 HIS B 202  ALA B 248  VAL B 252  THR B 262                    
SITE     4 AD7 19 CLA B 603  CLA B 604  CLA B 605  CLA B 608                    
SITE     5 AD7 19 PHE H  38  LEU H  42  CLA H 101                               
SITE     1 AD8 20 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 AD8 20 LEU B 149  VAL B 245  ALA B 248  ALA B 249                    
SITE     3 AD8 20 VAL B 252  PHE B 451  HIS B 455  PHE B 458                    
SITE     4 AD8 20 ALA B 459  PHE B 462  CLA B 602  CLA B 604                    
SITE     5 AD8 20 CLA B 606  CLA B 611  CLA B 612  CLA B 614                    
SITE     1 AD9 20 THR B  27  VAL B  30  ALA B  31  TRP B  33                    
SITE     2 AD9 20 ALA B  34  VAL B  62  PHE B  65  MET B  66                    
SITE     3 AD9 20 ARG B  68  LEU B  69  VAL B  96  HIS B 100                    
SITE     4 AD9 20 LEU B 103  GLY B 147  ALA B 205  CLA B 602                    
SITE     5 AD9 20 CLA B 603  CLA B 605  CLA B 609  CLA B 611                    
SITE     1 AE1 17 LEU B  69  TRP B  91  ALA B  99  LEU B 103                    
SITE     2 AE1 17 LEU B 106  GLY B 152  PHE B 153  PHE B 156                    
SITE     3 AE1 17 HIS B 157  PHE B 162  PRO B 164  CLA B 602                    
SITE     4 AE1 17 CLA B 604  CLA B 615  BCR B 619  LMT B 623                    
SITE     5 AE1 17 SQD a 401                                                     
SITE     1 AE2 20 TRP B  33  MET B  37  TYR B  40  GLN B  58                    
SITE     2 AE2 20 GLY B  59  PHE B  61  THR B 327  GLY B 328                    
SITE     3 AE2 20 PRO B 329  TRP B 450  ALA B 454  CLA B 603                    
SITE     4 AE2 20 BCR B 616  BCR B 617  BCR B 618  LMG B 621                    
SITE     5 AE2 20 LMG B 625  MET D 281  LEU L  27  PHE M  14                    
SITE     1 AE3 15 THR B 236  SER B 239  ALA B 243  PHE B 246                    
SITE     2 AE3 15 PHE B 247  HIS B 466  LEU B 474  CLA B 608                    
SITE     3 AE3 15 CLA B 609  SQD B 622  PHE D 120  ILE D 123                    
SITE     4 AE3 15 MET D 126  LEU D 127  PHE D 130                               
SITE     1 AE4 15 PHE B 139  ALA B 212  PHE B 215  HIS B 216                    
SITE     2 AE4 15 PRO B 221  PRO B 222  LEU B 229  CLA B 602                    
SITE     3 AE4 15 CLA B 607  CLA B 609  THR H  27  MET H  31                    
SITE     4 AE4 15 PHE H  34  MET H  35  BCR H 102                               
SITE     1 AE5 15 HIS B  23  LEU B 135  PHE B 139  HIS B 142                    
SITE     2 AE5 15 LEU B 143  ALA B 146  VAL B 237  SER B 240                    
SITE     3 AE5 15 SER B 241  CLA B 604  CLA B 607  CLA B 608                    
SITE     4 AE5 15 CLA B 611  CLA B 614  BCR H 102                               
SITE     1 AE6 18 TRP B   5  TYR B   6  ARG B   7  VAL B   8                    
SITE     2 AE6 18 HIS B   9  THR B  10  LEU B 238  ILE B 242                    
SITE     3 AE6 18 LEU B 461  PHE B 462  GLY B 465  TRP B 468                    
SITE     4 AE6 18 HIS B 469  ARG B 472  CLA B 611  CLA B 612                    
SITE     5 AE6 18 CLA B 613  LMG B 625                                          
SITE     1 AE7 18 HIS B   9  LEU B  19  ALA B  22  HIS B  23                    
SITE     2 AE7 18 HIS B  26  THR B  27  ILE B 234  VAL B 237                    
SITE     3 AE7 18 LEU B 238  SER B 241  VAL B 245  CLA B 603                    
SITE     4 AE7 18 CLA B 604  CLA B 609  CLA B 610  CLA B 612                    
SITE     5 AE7 18 CLA B 613  CLA B 614                                          
SITE     1 AE8  9 HIS B   9  HIS B  26  VAL B  30  PHE B 462                    
SITE     2 AE8  9 CLA B 603  CLA B 610  CLA B 611  CLA B 613                    
SITE     3 AE8  9 LMG B 625                                                     
SITE     1 AE9 11 VAL B   8  HIS B   9  VAL B  11  TRP B 115                    
SITE     2 AE9 11 CLA B 610  CLA B 611  CLA B 612  BCR B 616                    
SITE     3 AE9 11 SQD B 627  VAL L  10  LMG m 101                               
SITE     1 AF1 11 HIS B  23  MET B 138  ILE B 141  HIS B 142                    
SITE     2 AF1 11 LEU B 145  CLA B 603  CLA B 609  CLA B 611                    
SITE     3 AF1 11 CLA B 615  BCR B 619  LEU H  14                               
SITE     1 AF2 11 LEU B  24  ALA B 110  TRP B 113  HIS B 114                    
SITE     2 AF2 11 LEU B 120  CLA B 605  CLA B 614  BCR B 619                    
SITE     3 AF2 11 THR H   5  LEU H   7  SQD a 401                               
SITE     1 AF3  9 MET B  25  LEU B  29  TRP B 115  CLA B 606                    
SITE     2 AF3  9 CLA B 613  BCR B 617  BCR B 618  LEU M  13                    
SITE     3 AF3  9 PHE t  19                                                     
SITE     1 AF4 10 TRP B  33  SER B  36  MET B  37  CLA B 606                    
SITE     2 AF4 10 BCR B 616  BCR B 618  LMT B 629  ILE t   4                    
SITE     3 AF4 10 ALA t  11  PHE t  17                                          
SITE     1 AF5  6 GLY B  32  TRP B  33  GLY B 105  CLA B 606                    
SITE     2 AF5  6 BCR B 616  BCR B 617                                          
SITE     1 AF6  9 LEU B 109  CYS B 112  TYR B 117  CLA B 605                    
SITE     2 AF6  9 CLA B 614  CLA B 615  LMT B 623  SQD a 401                    
SITE     3 AF6  9 PHE t  18                                                     
SITE     1 AF7 13 TYR B 193  PHE B 250  TYR B 258  TYR B 273                    
SITE     2 AF7 13 SER B 277  HIS D  87  LEU D 162  TYR H  49                    
SITE     3 AF7 13 ASN H  50  VAL H  60  SER H  61  TRP H  62                    
SITE     4 AF7 13 CLA H 101                                                     
SITE     1 AF8 11 TYR B  40  THR B 327  GLY B 328  PRO B 329                    
SITE     2 AF8 11 LYS B 332  CLA B 606  ILE D 284  PHE L  35                    
SITE     3 AF8 11 ASN M   4  LEU M   6  LMT M 103                               
SITE     1 AF9 10 LYS B 227  ALA B 228  ARG B 230  LEU B 474                    
SITE     2 AF9 10 CLA B 607  LMT B 624  LYS D  23  TRP D  32                    
SITE     3 AF9 10 ARG D 134  LEU D 135                                          
SITE     1 AG1  4 TRP B  91  PHE B 162  CLA B 605  BCR B 619                    
SITE     1 AG2  7 ARG B 224  LYS B 227  SQD B 622  ASP D  16                    
SITE     2 AG2  7 ASP D  19  ALA H  32  MET H  35                               
SITE     1 AG3 14 ASN A 234  TRP B   5  TYR B   6  ARG B   7                    
SITE     2 AG3 14 PHE B 464  TRP B 468  CLA B 606  CLA B 610                    
SITE     3 AG3 14 CLA B 612  ARG D 139  TYR D 141  PHE D 269                    
SITE     4 AG3 14 PHE D 273  LMG L 101                                          
SITE     1 AG4  7 TRP B  75  ASP B  87  GLY B  89  PHE B  90                    
SITE     2 AG4  7 LMT B 628  ILE a  46  LMG i 102                               
SITE     1 AG5 12 ARG B  18  LEU B  29  SER B 104  PHE B 108                    
SITE     2 AG5 12 CLA B 613  ASN L   4  ARG l  14  TYR l  18                    
SITE     3 AG5 12 TYR m  26  LMG m 101  PHE t  19  PHE t  23                    
SITE     1 AG6  8 ASP B  87  DGD B 626  ALA a 100  MET i   1                    
SITE     2 AG6  8 LEU i   4  BCR i 101  LMG i 102  LYS o  95                    
SITE     1 AG7  4 ALA B  43  BCR B 617  LMG a 402  VAL t   7                    
SITE     1 AG8 17 LEU C  95  LEU C 168  GLY C 171  ALA C 172                    
SITE     2 AG8 17 ILE C 224  VAL C 233  HIS C 237  ILE C 240                    
SITE     3 AG8 17 ALA C 278  MET C 282  VAL C 296  TYR C 297                    
SITE     4 AG8 17 CLA C 502  CLA C 503  CLA C 505  CLA C 506                    
SITE     5 AG8 17 BCR C 513                                                     
SITE     1 AG9 17 TRP C  63  HIS C  91  TRP C  97  LEU C 174                    
SITE     2 AG9 17 LYS C 178  PHE C 182  LEU C 279  MET C 282                    
SITE     3 AG9 17 ALA C 286  TYR C 297  HIS C 430  LEU C 433                    
SITE     4 AG9 17 PHE C 437  CLA C 501  CLA C 503  CLA C 508                    
SITE     5 AG9 17 CLA C 509                                                     
SITE     1 AH1 14 ILE C  60  VAL C  61  ALA C  64  THR C  68                    
SITE     2 AH1 14 LEU C  88  HIS C  91  ILE C  92  VAL C 114                    
SITE     3 AH1 14 HIS C 118  CLA C 501  CLA C 502  CLA C 509                    
SITE     4 AH1 14 CLA C 511  LMG C 517                                          
SITE     1 AH2 16 PHE A  33  MET A 127  TRP A 131  PHE C 264                    
SITE     2 AH2 16 ILE C 265  TYR C 274  GLY C 277  ALA C 278                    
SITE     3 AH2 16 MET C 281  HIS C 441  LEU C 442  ALA C 445                    
SITE     4 AH2 16 ARG C 449  CLA C 506  BCR C 513  PHE I  23                    
SITE     1 AH3 14 LEU C 165  LEU C 213  ILE C 243  GLY C 247                    
SITE     2 AH3 14 TRP C 250  HIS C 251  THR C 255  PRO C 256                    
SITE     3 AH3 14 PHE C 257  TRP C 259  ALA C 260  PHE C 264                    
SITE     4 AH3 14 CLA C 501  CLA C 506                                          
SITE     1 AH4 15 MET C 157  LEU C 161  HIS C 164  ILE C 240                    
SITE     2 AH4 15 PHE C 264  TRP C 266  TYR C 271  TYR C 274                    
SITE     3 AH4 15 SER C 275  LEU C 279  CLA C 501  CLA C 504                    
SITE     4 AH4 15 CLA C 505  CLA C 508  BCR C 513                               
SITE     1 AH5 17 LHG A 410  TRP C  36  ALA C  37  ASN C  39                    
SITE     2 AH5 17 ALA C  40  GLU C 269  LEU C 276  PHE C 436                    
SITE     3 AH5 17 PHE C 437  GLY C 440  TRP C 443  HIS C 444                    
SITE     4 AH5 17 ARG C 447  CLA C 508  CLA C 509  DGD C 515                    
SITE     5 AH5 17 CLA C 519                                                     
SITE     1 AH6 19 ASN C  39  LEU C  42  LEU C  49  ALA C  52                    
SITE     2 AH6 19 HIS C  53  HIS C  56  TYR C 149  TRP C 151                    
SITE     3 AH6 19 GLY C 268  TYR C 271  LEU C 272  SER C 275                    
SITE     4 AH6 19 LEU C 279  CLA C 502  CLA C 506  CLA C 507                    
SITE     5 AH6 19 CLA C 509  CLA C 510  CLA C 511                               
SITE     1 AH7 16 LHG A 410  ASN C  39  HIS C  56  LEU C  59                    
SITE     2 AH7 16 LEU C 279  PHE C 436  PHE C 437  CLA C 502                    
SITE     3 AH7 16 CLA C 503  CLA C 507  CLA C 508  CLA C 510                    
SITE     4 AH7 16 CLA C 519  PRO K  29  VAL K  30  LEU K  33                    
SITE     1 AH8 22 GLN C  28  TRP C  35  GLY C  38  ASN C  39                    
SITE     2 AH8 22 ARG C  41  LEU C  42  LYS C  48  ALA C  52                    
SITE     3 AH8 22 PHE C 127  ILE C 134  CLA C 508  CLA C 509                    
SITE     4 AH8 22 PHE K  32  TRP K  39  GLN K  40  BCR K 101                    
SITE     5 AH8 22 MET Z  19  VAL Z  20  VAL Z  23  PRO Z  24                    
SITE     6 AH8 22 ILE y  35  LEU y  46                                          
SITE     1 AH9 11 HIS C  53  ALA C  57  PHE C 147  PHE C 163                    
SITE     2 AH9 11 HIS C 164  VAL C 167  LEU C 174  CLA C 503                    
SITE     3 AH9 11 CLA C 508  CLA C 512  BCR C 520                               
SITE     1 AI1  9 VAL C  54  VAL C 124  GLY C 128  TYR C 131                    
SITE     2 AI1  9 HIS C 132  PRO C 137  PHE C 147  CLA C 511                    
SITE     3 AI1  9 BCR C 520                                                     
SITE     1 AI2 12 ILE C 209  TYR C 212  LEU C 213  VAL C 227                    
SITE     2 AI2 12 ASP C 232  VAL C 233  GLY C 236  ILE C 240                    
SITE     3 AI2 12 PHE C 264  CLA C 501  CLA C 504  CLA C 506                    
SITE     1 AI3 16 LEU A  91  PHE A 155  ILE A 163  PRO C 217                    
SITE     2 AI3 16 PHE C 218  GLY C 219  GLY C 220  GLY C 222                    
SITE     3 AI3 16 VAL C 225  SER C 226  PHE C 284  CYS C 288                    
SITE     4 AI3 16 PHE C 292  ASN C 294  PHE C 361  ARG C 362                    
SITE     1 AI4 20 PHE A 197  LEU A 297  SQD A 413  TYR C  82                    
SITE     2 AI4 20 GLU C  83  GLN C  84  GLY C  85  LEU C 404                    
SITE     3 AI4 20 SER C 406  ASN C 418  PHE C 419  VAL C 420                    
SITE     4 AI4 20 TRP C 425  SER C 429  CLA C 507  DGD C 516                    
SITE     5 AI4 20 CLA C 519  LMG C 521  TYR J  33  BCR J 102                    
SITE     1 AI5 22 LEU A 200  TRP A 278  PHE A 300  ASN A 301                    
SITE     2 AI5 22 SER A 305  SQD A 413  ASN C 405  SER C 406                    
SITE     3 AI5 22 VAL C 407  ASN C 415  SER C 416  ASN C 418                    
SITE     4 AI5 22 DGD C 515  CLA C 519  LMG D 409  PHE J  29                    
SITE     5 AI5 22 ALA J  32  TYR J  33  GLY J  37  SER J  38                    
SITE     6 AI5 22 SER J  39  GLN V  60                                          
SITE     1 AI6  8 TRP C  97  PHE C 109  VAL C 113  VAL C 114                    
SITE     2 AI6  8 VAL C 117  HIS C 118  CLA C 503  PHE Z  59                    
SITE     1 AI7  7 TYR A 262  ASN A 266  SQD A 413  TRP C  35                    
SITE     2 AI7  7 LMG E 101  BCR J 102  PHE K  45                               
SITE     1 AI8 18 PHE A 285  LHG A 410  TRP C  63  MET C  67                    
SITE     2 AI8 18 PHE C  70  GLN C  84  GLY C  85  ILE C  87                    
SITE     3 AI8 18 LEU C 404  TRP C 425  SER C 429  CLA C 507                    
SITE     4 AI8 18 CLA C 509  DGD C 515  DGD C 516  LMG C 521                    
SITE     5 AI8 18 PRO K  26  VAL K  30                                          
SITE     1 AI9  9 PHE C 112  VAL C 116  SER C 121  VAL C 124                    
SITE     2 AI9  9 CLA C 511  CLA C 512  TYR K  15  GLY Z  55                    
SITE     3 AI9  9 ASN Z  58                                                     
SITE     1 AJ1  7 HIS C  74  DGD C 515  CLA C 519  BCR J 102                    
SITE     2 AJ1  7 ASP K  23  VAL K  27  ILE y  25                               
SITE     1 AJ2 23 PHE A 206  ALA A 209  LEU A 210  MET A 214                    
SITE     2 AJ2 23 LEU A 258  CLA A 404  ALA D  41  TRP D  48                    
SITE     3 AJ2 23 ILE D 114  GLY D 118  LEU D 122  PHE D 125                    
SITE     4 AJ2 23 GLN D 129  ASN D 142  ALA D 145  PHE D 146                    
SITE     5 AJ2 23 ALA D 148  PRO D 149  PHE D 153  PHE D 173                    
SITE     6 AJ2 23 PRO D 275  LEU D 279  CLA D 403                               
SITE     1 AJ3  8 HIS A 215  GLU A 244  TYR A 246  HIS A 272                    
SITE     2 AJ3  8 FE2 A 401  TYR D 244  LYS D 264  HIS D 268                    
SITE     1 AJ4 24 PHE A 206  CLA A 402  CLA A 403  CLA A 404                    
SITE     2 AJ4 24 TRP D  48  LEU D 122  VAL D 152  PHE D 153                    
SITE     3 AJ4 24 SER D 155  VAL D 156  LEU D 182  PHE D 185                    
SITE     4 AJ4 24 GLN D 186  TRP D 191  THR D 192  HIS D 197                    
SITE     5 AJ4 24 GLY D 200  VAL D 201  VAL D 204  LEU D 279                    
SITE     6 AJ4 24 SER D 282  ALA D 283  VAL D 286  PHO D 401                    
SITE     1 AJ5 14 LEU D  43  LEU D  89  LEU D  90  LEU D  91                    
SITE     2 AJ5 14 LEU D  92  TRP D  93  THR D 112  PHE D 113                    
SITE     3 AJ5 14 HIS D 117  PHE D 120  LMT D 408  GLY X  22                    
SITE     4 AJ5 14 LEU X  23  GLY X  26                                          
SITE     1 AJ6 14 CLA A 403  MET D 199  HIS D 214  THR D 217                    
SITE     2 AJ6 14 TRP D 253  ALA D 260  PHE D 261  LEU D 267                    
SITE     3 AJ6 14 PHE D 270  PHE D 273  LMG D 406  VAL L  26                    
SITE     4 AJ6 14 LMG L 101  PHE T  10                                          
SITE     1 AJ7 11 PHE D 257  ALA D 260  PHE D 261  SER D 262                    
SITE     2 AJ7 11 ASN D 263  TRP D 266  PL9 D 405  THR L  15                    
SITE     3 AJ7 11 TYR L  18  LEU L  19  PHE T  17                               
SITE     1 AJ8  6 ASP D 100  PHE D 101  THR D 102  LMT D 408                    
SITE     2 AJ8  6 ASP E  45  VAL E  46                                          
SITE     1 AJ9  8 LEU D  92  TRP D  93  GLY D  99  CLA D 404                    
SITE     2 AJ9  8 DGD D 407  ILE X  21  SER X  25  GLY X  26                    
SITE     1 AK1 13 DGD C 516  TYR D  67  GLY D  70  ASN D  72                    
SITE     2 AK1 13 PHE D  73  ILE F  37  MET F  40  GLN F  41                    
SITE     3 AK1 13 BCR F 102  PHE J  28  GLY J  31  ALA J  32                    
SITE     4 AK1 13 GLY J  37                                                     
SITE     1 AK2  7 TYR A 262  LHG C 518  PHE D  27  PRO E   9                    
SITE     2 AK2  7 PHE E  10  SER E  11  PL9 J 101                               
SITE     1 AK3 15 ARG E   8  PHE E  10  ILE E  13  ARG E  18                    
SITE     2 AK3 15 TYR E  19  HIS E  23  THR E  26  LEU E  30                    
SITE     3 AK3 15 ILE F  15  ARG F  19  TRP F  20  VAL F  23                    
SITE     4 AK3 15 HIS F  24  ALA F  27  ILE F  31                               
SITE     1 AK4 10 TYR D  42  GLY D  47  LEU D  49  THR D  50                    
SITE     2 AK4 10 PHE D 101  LMG D 409  PRO F  29  PHE F  33                    
SITE     3 AK4 10 VAL J  25  PL9 J 101                                          
SITE     1 AK5  9 TRP D  21  ARG D  24  ARG D  26  GLU E   7                    
SITE     2 AK5  9 PHE F  16  THR F  17  VAL F  18  THR X  33                    
SITE     3 AK5  9 ASP X  44                                                     
SITE     1 AK6 17 GLU B 184  GLY B 189  PHE B 190  GLY B 197                    
SITE     2 AK6 17 HIS B 201  ALA B 205  VAL B 208  PHE B 247                    
SITE     3 AK6 17 CLA B 601  CLA B 602  DGD B 620  VAL D 154                    
SITE     4 AK6 17 PHE H  38  PHE H  41  ILE H  45  LEU H  46                    
SITE     5 AK6 17 TYR H  49                                                     
SITE     1 AK7 10 CLA B 601  CLA B 608  CLA B 609  PHE H  34                    
SITE     2 AK7 10 MET H  35  LEU H  37  PHE H  38  PHE H  41                    
SITE     3 AK7 10 THR X  11  LEU X  16                                          
SITE     1 AK8  6 MET I   1  THR I   3  LEU I   4  LMT I 102                    
SITE     2 AK8  6 DGD b 601  LMT b 603                                          
SITE     1 AK9  4 THR I   3  ILE I   6  ILE I  10  LMG I 101                    
SITE     1 AL1  3 PL9 A 407  LMG E 101  BCR F 102                               
SITE     1 AL2  7 SQD A 413  DGD C 515  LHG C 518  LMG C 521                    
SITE     2 AL2  7 ILE J  22  PHE J  29  TYR J  33                               
SITE     1 AL3 10 ALA C  55  LEU C  59  VAL C 116  LEU C 119                    
SITE     2 AL3 10 SER C 122  ALA C 123  CLA C 510  PHE K  32                    
SITE     3 AL3 10 VAL Z  13  BCR y 101                                          
SITE     1 AL4  2 ASP K  19  ASP K  23                                          
SITE     1 AL5 14 SER A 232  ASN A 234  TRP B   5  TYR B   6                    
SITE     2 AL5 14 LMG B 625  TRP D 266  PHE D 269  PHE D 270                    
SITE     3 AL5 14 PHE D 273  PL9 D 405  GLU L  11  ASN L  13                    
SITE     4 AL5 14 SER L  16  ILE L  24                                          
SITE     1 AL6 10 ILE M  23  GLU M  30  SER M  31  SQD b 602                    
SITE     2 AL6 10 CLA b 618  PRO l   9  VAL l  10  ILE m  24                    
SITE     3 AL6 10 GLN m  28  GLN m  32                                          
SITE     1 AL7  4 MET M   1  GLU M   2  TYR b  40  GLN m   5                    
SITE     1 AL8  7 TYR B  40  LMG B 621  GLN M   5  LEU M   6                    
SITE     2 AL8  7 MET m   1  GLU m   2  MET t   1                               
SITE     1 AL9  2 GLU O 140  HIS O 257                                          
SITE     1 AM1 14 ALA V  62  CYS V  63  CYS V  66  HIS V  67                    
SITE     2 AM1 14 THR V  74  LEU V  78  ASP V  79  LEU V  80                    
SITE     3 AM1 14 THR V  84  LEU V  85  TYR V 101  MET V 102                    
SITE     4 AM1 14 TYR V 108  HIS V 118                                          
SITE     1 AM2 15 ALA J  14  THR J  15  LEU K  25  ILE K  28                    
SITE     2 AM2 15 LEU K  31  ALA K  34  PHE K  37  VAL K  38                    
SITE     3 AM2 15 ALA K  41  BCR K 101  VAL Z  13  PHE Z  17                    
SITE     4 AM2 15 ILE y  28  GLY y  29  GLY y  32                               
SITE     1 AM3 12 TRP B 113  TYR B 117  CLA B 605  CLA B 615                    
SITE     2 AM3 12 BCR B 619  TRP a  20  ASN a  26  ARG a  27                    
SITE     3 AM3 12 LEU a  28  THR a  45  BCR i 101  LMG i 102                    
SITE     1 AM4  9 ALA B  43  TRP B  75  SER B  76  LEU B  98                    
SITE     2 AM4  9 LMT B 629  LEU a  72  ASP a 103  ARG d 304                    
SITE     3 AM4  9 GLY o 138                                                     
SITE     1 AM5 23 PHE a 119  TYR a 147  PRO a 150  SER a 153                    
SITE     2 AM5 23 VAL a 157  MET a 183  PHE a 186  GLN a 187                    
SITE     3 AM5 23 HIS a 198  GLY a 201  VAL a 205  PHE a 206                    
SITE     4 AM5 23 VAL a 283  THR a 286  ILE a 290  CLA a 404                    
SITE     5 AM5 23 CLA a 405  LEU d 182  LEU d 205  PHO d 401                    
SITE     6 AM5 23 CLA d 405  LMG d 409  PHE t  17                               
SITE     1 AM6 14 THR a  45  VAL a 157  PHE a 158  MET a 172                    
SITE     2 AM6 14 ILE a 176  THR a 179  PHE a 180  MET a 183                    
SITE     3 AM6 14 CLA a 403  MET d 198  VAL d 201  PHO d 401                    
SITE     4 AM6 14 CLA d 405  PL9 d 407                                          
SITE     1 AM7 15 GLN a 199  VAL a 202  ALA a 203  LEU a 210                    
SITE     2 AM7 15 CLA a 403  PL9 a 407  PHE d 157  VAL d 175                    
SITE     3 AM7 15 ILE d 178  PHE d 179  PHE d 181  LEU d 182                    
SITE     4 AM7 15 PHO d 402  CLA d 405  PL9 j 101                               
SITE     1 AM8 14 ILE a  36  PRO a  39  THR a  40  PHE a  93                    
SITE     2 AM8 14 PRO a  95  ILE a  96  TRP a  97  LEU a 114                    
SITE     3 AM8 14 HIS a 118  LEU a 121  DGD a 408  TYR i   9                    
SITE     4 AM8 14 PHE i  15  BCR i 101                                          
SITE     1 AM9 14 HIS a 215  LEU a 218  HIS a 252  PHE a 255                    
SITE     2 AM9 14 SER a 264  PHE a 265  LEU a 271  PHE a 274                    
SITE     3 AM9 14 CLA a 405  PHE d  38  ALA d  41  TYR d  42                    
SITE     4 AM9 14 THR f  25  PL9 j 101                                          
SITE     1 AN1 14 PHE a  93  TRP a  97  GLU a  98  LEU a 121                    
SITE     2 AN1 14 CLA a 406  LEU c 214  LYS c 215  SER c 216                    
SITE     3 AN1 14 PRO c 217  PHE c 218  TRP c 223  LYS i   5                    
SITE     4 AN1 14 TYR i   9  GLY o  38                                          
SITE     1 AN2 15 ARG a 140  TRP a 142  PHE a 273  SQD a 412                    
SITE     2 AN2 15 TRP c  36  PHE c 436  TRP c 443  ARG c 447                    
SITE     3 AN2 15 CLA c 507  CLA c 520  ASN d 220  ALA d 229                    
SITE     4 AN2 15 SER d 230  THR d 231  PHE d 232                               
SITE     1 AN3  3 HIS a 332  GLU a 333  LYS d 317                               
SITE     1 AN4 10 GLN a 165  ASP a 170  GLU a 189  HIS a 332                    
SITE     2 AN4 10 GLU a 333  HIS a 337  ASP a 342  ALA a 344                    
SITE     3 AN4 10 GLU c 354  ARG c 357                                          
SITE     1 AN5 14 ASN a 267  SER a 270  PHE a 273  PHE a 274                    
SITE     2 AN5 14 TRP a 278  LHG a 409  TRP c  36  CLA c 507                    
SITE     3 AN5 14 DGD c 517  LHG c 519  PHE d 232  ARG d 233                    
SITE     4 AN5 14 BCR j 102  PHE k  37                                          
SITE     1 AN6  5 HIS a 215  HIS a 272  HIS d 214  HIS d 268                    
SITE     2 AN6  5 BCT d 404                                                     
SITE     1 AN7  7 ILE A  46  LMG I 101  TRP b  75  ASP b  87                    
SITE     2 AN7  7 PHE b  90  LMT b 603  LMT b 628                               
SITE     1 AN8 11 ARG L  14  TYR L  18  TYR M  26  LMG M 101                    
SITE     2 AN8 11 PHE T  19  PHE T  23  ARG b  18  SER b 104                    
SITE     3 AN8 11 CLA b 618  BCR b 621  ASN l   4                               
SITE     1 AN9  6 BCR A 408  LMG I 101  LYS O  95  GLY b  85                    
SITE     2 AN9  6 ASP b  87  DGD b 601                                          
SITE     1 AO1  5 ILE T   4  VAL T   7  ALA b  43  LEU b 437                    
SITE     2 AO1  5 BCR b 622                                                     
SITE     1 AO2  8 TRP b 185  PRO b 187  PHE b 190  ILE b 207                    
SITE     2 AO2  8 CLA b 606  PHE h  41  ILE h  44  BCR x 101                    
SITE     1 AO3 17 GLU b 184  GLY b 189  PHE b 190  GLY b 197                    
SITE     2 AO3 17 HIS b 201  ALA b 204  ALA b 205  VAL b 208                    
SITE     3 AO3 17 PHE b 247  CLA b 605  CLA b 607  VAL d 154                    
SITE     4 AO3 17 PHE h  38  PHE h  41  ILE h  45  LEU h  46                    
SITE     5 AO3 17 TYR h  49                                                     
SITE     1 AO4 20 ARG b  68  LEU b  69  ALA b 146  LEU b 149                    
SITE     2 AO4 20 CYS b 150  PHE b 153  VAL b 198  HIS b 201                    
SITE     3 AO4 20 HIS b 202  PHE b 247  ALA b 248  VAL b 252                    
SITE     4 AO4 20 THR b 262  CLA b 606  CLA b 608  CLA b 609                    
SITE     5 AO4 20 CLA b 610  CLA b 613  PHE h  38  LEU h  42                    
SITE     1 AO5 21 TRP b  33  PHE b  61  PHE b  65  ARG b  68                    
SITE     2 AO5 21 LEU b 149  VAL b 245  ALA b 248  ALA b 249                    
SITE     3 AO5 21 VAL b 252  PHE b 451  HIS b 455  PHE b 458                    
SITE     4 AO5 21 ALA b 459  PHE b 462  CLA b 607  CLA b 609                    
SITE     5 AO5 21 CLA b 611  CLA b 615  CLA b 616  CLA b 617                    
SITE     6 AO5 21 CLA b 619                                                     
SITE     1 AO6 20 THR b  27  VAL b  30  ALA b  31  TRP b  33                    
SITE     2 AO6 20 ALA b  34  VAL b  62  PHE b  65  MET b  66                    
SITE     3 AO6 20 ARG b  68  LEU b  69  VAL b  96  HIS b 100                    
SITE     4 AO6 20 LEU b 103  ALA b 205  CLA b 607  CLA b 608                    
SITE     5 AO6 20 CLA b 610  CLA b 613  CLA b 614  CLA b 616                    
SITE     1 AO7 17 SQD A 414  LEU b  69  TRP b  91  ALA b  99                    
SITE     2 AO7 17 LEU b 103  LEU b 106  GLY b 152  PHE b 153                    
SITE     3 AO7 17 PHE b 156  HIS b 157  PHE b 162  PRO b 164                    
SITE     4 AO7 17 CLA b 607  CLA b 609  CLA b 620  BCR b 624                    
SITE     5 AO7 17 LMT b 628                                                     
SITE     1 AO8 17 TRP b  33  TYR b  40  GLN b  58  GLY b  59                    
SITE     2 AO8 17 PHE b  61  THR b 327  GLY b 328  PRO b 329                    
SITE     3 AO8 17 TRP b 450  ALA b 454  CLA b 608  CLA b 617                    
SITE     4 AO8 17 BCR b 622  BCR b 623  LMG b 626  MET d 281                    
SITE     5 AO8 17 LEU l  27                                                     
SITE     1 AO9 17 THR b 236  SER b 239  ALA b 243  PHE b 246                    
SITE     2 AO9 17 PHE b 247  PHE b 463  HIS b 466  LEU b 474                    
SITE     3 AO9 17 CLA b 613  CLA b 614  PHE d 120  ILE d 123                    
SITE     4 AO9 17 MET d 126  LEU d 127  PHE d 130  SQD d 403                    
SITE     5 AO9 17 LEU h  43                                                     
SITE     1 AP1 18 PHE b 139  ALA b 212  PHE b 215  HIS b 216                    
SITE     2 AP1 18 PRO b 221  PRO b 222  LEU b 229  CLA b 607                    
SITE     3 AP1 18 CLA b 609  CLA b 612  CLA b 614  SQD d 403                    
SITE     4 AP1 18 THR h  27  THR h  28  MET h  31  PHE h  34                    
SITE     5 AP1 18 MET h  35  BCR x 101                                          
SITE     1 AP2 14 HIS b  23  LEU b 135  PHE b 139  HIS b 142                    
SITE     2 AP2 14 LEU b 143  THR b 236  VAL b 237  SER b 240                    
SITE     3 AP2 14 CLA b 609  CLA b 612  CLA b 613  CLA b 616                    
SITE     4 AP2 14 CLA b 619  BCR x 101                                          
SITE     1 AP3 19 TRP b   5  TYR b   6  ARG b   7  VAL b   8                    
SITE     2 AP3 19 HIS b   9  THR b  10  ILE b 242  LEU b 461                    
SITE     3 AP3 19 PHE b 462  GLY b 465  TRP b 468  HIS b 469                    
SITE     4 AP3 19 ARG b 472  CLA b 608  CLA b 616  CLA b 617                    
SITE     5 AP3 19 CLA b 618  LMG d 408  LMG l 101                               
SITE     1 AP4 16 HIS b   9  LEU b  19  HIS b  23  HIS b  26                    
SITE     2 AP4 16 THR b  27  ILE b 234  VAL b 237  LEU b 238                    
SITE     3 AP4 16 SER b 241  CLA b 608  CLA b 609  CLA b 614                    
SITE     4 AP4 16 CLA b 615  CLA b 617  CLA b 618  CLA b 619                    
SITE     1 AP5  9 HIS b   9  HIS b  26  PHE b 462  CLA b 608                    
SITE     2 AP5  9 CLA b 611  CLA b 615  CLA b 616  CLA b 618                    
SITE     3 AP5  9 LMG d 408                                                     
SITE     1 AP6 13 LMG M 101  VAL b   8  HIS b   9  VAL b  11                    
SITE     2 AP6 13 LEU b  12  LEU b  29  TRP b 115  SQD b 602                    
SITE     3 AP6 13 CLA b 615  CLA b 616  CLA b 617  BCR b 621                    
SITE     4 AP6 13 VAL l  10                                                     
SITE     1 AP7 13 HIS b  23  MET b 138  ILE b 141  HIS b 142                    
SITE     2 AP7 13 LEU b 145  CLA b 608  CLA b 614  CLA b 616                    
SITE     3 AP7 13 CLA b 620  BCR b 624  LEU h   7  LEU h  14                    
SITE     4 AP7 13 ASN h  15                                                     
SITE     1 AP8 10 SQD A 414  LEU b  24  ALA b 110  TRP b 113                    
SITE     2 AP8 10 HIS b 114  LEU b 122  CLA b 610  CLA b 619                    
SITE     3 AP8 10 THR h   5  LEU h   7                                          
SITE     1 AP9  8 PHE T  19  MET b  25  TRP b 115  SQD b 602                    
SITE     2 AP9  8 CLA b 618  BCR b 622  BCR b 623  LEU m  13                    
SITE     1 AQ1 15 SQD A 414  ILE T   4  PHE T   8  ALA T  11                    
SITE     2 AQ1 15 PHE T  17  PHE T  18  ILE T  21  PHE T  22                    
SITE     3 AQ1 15 TRP b  33  SER b  36  MET b  37  LMT b 604                    
SITE     4 AQ1 15 CLA b 611  BCR b 621  BCR b 623                               
SITE     1 AQ2  8 LEU b  29  GLY b  32  TRP b  33  ILE b 101                    
SITE     2 AQ2  8 GLY b 105  CLA b 611  BCR b 621  BCR b 622                    
SITE     1 AQ3  9 SQD A 414  PHE T  18  PHE T  22  LEU b 109                    
SITE     2 AQ3  9 ALA b 110  CYS b 112  TYR b 117  CLA b 610                    
SITE     3 AQ3  9 CLA b 619                                                     
SITE     1 AQ4 12 TYR b 193  PHE b 250  TYR b 258  TYR b 273                    
SITE     2 AQ4 12 SER b 277  HIS d  87  LEU d 162  TYR h  49                    
SITE     3 AQ4 12 ASN h  50  VAL h  60  SER h  61  TRP h  62                    
SITE     1 AQ5 11 TYR b  40  THR b 327  GLY b 328  PRO b 329                    
SITE     2 AQ5 11 LYS b 332  PHE b 453  CLA b 611  ILE d 284                    
SITE     3 AQ5 11 PHE l  35  ASN m   4  LEU m   6                               
SITE     1 AQ6  8 LEU A  72  ASP A 103  ARG D 304  GLY O 138                    
SITE     2 AQ6  8 ALA b  43  TRP b  75  SER b  76  LEU b  98                    
SITE     1 AQ7  4 TRP b  91  PHE b 162  DGD b 601  CLA b 610                    
SITE     1 AQ8  7 ARG b 224  LYS b 227  ASP d  16  ASP d  19                    
SITE     2 AQ8  7 SQD d 403  ALA h  32  MET h  35                               
SITE     1 AQ9 17 LEU c  95  LEU c 168  GLY c 171  ALA c 172                    
SITE     2 AQ9 17 LEU c 175  ILE c 224  VAL c 233  HIS c 237                    
SITE     3 AQ9 17 ILE c 240  ALA c 278  MET c 282  VAL c 296                    
SITE     4 AQ9 17 TYR c 297  CLA c 502  CLA c 503  CLA c 506                    
SITE     5 AQ9 17 BCR c 514                                                     
SITE     1 AR1 16 TRP c  63  HIS c  91  TRP c  97  GLY c 171                    
SITE     2 AR1 16 LYS c 178  PHE c 182  LEU c 279  MET c 282                    
SITE     3 AR1 16 ALA c 286  TYR c 297  HIS c 430  LEU c 433                    
SITE     4 AR1 16 PHE c 437  CLA c 501  CLA c 503  CLA c 508                    
SITE     1 AR2 14 ILE c  60  VAL c  61  ALA c  64  THR c  68                    
SITE     2 AR2 14 LEU c  88  HIS c  91  ILE c  92  VAL c 114                    
SITE     3 AR2 14 HIS c 118  CLA c 501  CLA c 502  CLA c 509                    
SITE     4 AR2 14 CLA c 511  LMG c 518                                          
SITE     1 AR3 18 PHE a  33  MET a 127  GLY a 128  TRP a 131                    
SITE     2 AR3 18 PHE c 264  ILE c 265  TYR c 274  GLY c 277                    
SITE     3 AR3 18 ALA c 278  MET c 281  HIS c 441  LEU c 442                    
SITE     4 AR3 18 ALA c 445  ARG c 449  CLA c 506  BCR c 514                    
SITE     5 AR3 18 VAL i  12  PHE i  23                                          
SITE     1 AR4 12 LEU c 165  ILE c 243  GLY c 247  TRP c 250                    
SITE     2 AR4 12 HIS c 251  THR c 255  PRO c 256  PHE c 257                    
SITE     3 AR4 12 TRP c 259  ALA c 260  PHE c 264  CLA c 506                    
SITE     1 AR5 13 MET c 157  LEU c 161  HIS c 164  PHE c 264                    
SITE     2 AR5 13 TRP c 266  TYR c 271  TYR c 274  SER c 275                    
SITE     3 AR5 13 LEU c 279  CLA c 501  CLA c 504  CLA c 505                    
SITE     4 AR5 13 CLA c 508                                                     
SITE     1 AR6 17 LHG a 409  SQD a 412  TRP c  36  ALA c  37                    
SITE     2 AR6 17 ASN c  39  ALA c  40  GLU c 269  LEU c 276                    
SITE     3 AR6 17 PHE c 436  PHE c 437  GLY c 440  TRP c 443                    
SITE     4 AR6 17 HIS c 444  ARG c 447  CLA c 508  CLA c 509                    
SITE     5 AR6 17 DGD c 516                                                     
SITE     1 AR7 18 ASN c  39  LEU c  42  LEU c  49  ALA c  52                    
SITE     2 AR7 18 HIS c  53  HIS c  56  TYR c 149  TRP c 151                    
SITE     3 AR7 18 GLY c 268  TYR c 271  LEU c 272  SER c 275                    
SITE     4 AR7 18 LEU c 279  CLA c 502  CLA c 506  CLA c 507                    
SITE     5 AR7 18 CLA c 509  CLA c 511                                          
SITE     1 AR8 15 ASN c  39  HIS c  56  LEU c  59  TRP c  63                    
SITE     2 AR8 15 LEU c 279  PHE c 436  PHE c 437  CLA c 503                    
SITE     3 AR8 15 CLA c 507  CLA c 508  CLA c 510  CLA c 520                    
SITE     4 AR8 15 PRO k  29  VAL k  30  LEU k  33                               
SITE     1 AR9 20 TRP c  35  GLY c  38  ASN c  39  ARG c  41                    
SITE     2 AR9 20 LEU c  42  LEU c  45  LYS c  48  ALA c  52                    
SITE     3 AR9 20 PHE c 127  ILE c 134  CLA c 509  BCR c 513                    
SITE     4 AR9 20 ILE g  35  LEU g  46  PHE k  32  TRP k  39                    
SITE     5 AR9 20 GLN k  40  MET z  19  VAL z  20  PRO z  24                    
SITE     1 AS1 13 HIS c  53  ALA c  57  PHE c 147  PHE c 163                    
SITE     2 AS1 13 HIS c 164  VAL c 167  ILE c 170  GLY c 171                    
SITE     3 AS1 13 LEU c 174  CLA c 503  CLA c 508  CLA c 512                    
SITE     4 AS1 13 BCR c 521                                                     
SITE     1 AS2 10 LEU c  50  VAL c  54  VAL c 124  GLY c 128                    
SITE     2 AS2 10 TYR c 131  HIS c 132  PRO c 137  PHE c 147                    
SITE     3 AS2 10 CLA c 511  BCR c 521                                          
SITE     1 AS3 12 ALA c  55  VAL c 116  LEU c 119  ILE c 120                    
SITE     2 AS3 12 SER c 122  ALA c 123  CLA c 510  BCR c 521                    
SITE     3 AS3 12 BCR g 101  PHE k  18  PHE k  32  VAL z  13                    
SITE     1 AS4 11 ILE c 209  TYR c 212  LEU c 213  VAL c 227                    
SITE     2 AS4 11 ASP c 232  VAL c 233  GLY c 236  ILE c 240                    
SITE     3 AS4 11 PHE c 264  CLA c 501  CLA c 504                               
SITE     1 AS5 16 LEU a  91  PHE a 155  ILE a 163  PRO c 217                    
SITE     2 AS5 16 PHE c 218  GLY c 219  GLY c 220  GLY c 222                    
SITE     3 AS5 16 VAL c 225  SER c 226  PHE c 284  CYS c 288                    
SITE     4 AS5 16 PHE c 292  ASN c 294  PHE c 361  ARG c 362                    
SITE     1 AS6 18 PHE a 197  TYR c  82  GLU c  83  GLN c  84                    
SITE     2 AS6 18 GLY c  85  LEU c 404  SER c 406  ASN c 418                    
SITE     3 AS6 18 PHE c 419  VAL c 420  TRP c 425  CLA c 507                    
SITE     4 AS6 18 DGD c 517  LHG c 519  CLA c 520  LMG c 522                    
SITE     5 AS6 18 TYR j  33  BCR j 102                                          
SITE     1 AS7 21 TRP a 278  PHE a 300  ASN a 301  PHE a 302                    
SITE     2 AS7 21 SER a 305  SQD a 412  ASN c 405  SER c 406                    
SITE     3 AS7 21 VAL c 407  ASN c 415  SER c 416  ASN c 418                    
SITE     4 AS7 21 DGD c 516  CLA c 520  PHE j  29  ALA j  32                    
SITE     5 AS7 21 TYR j  33  GLY j  37  SER j  38  SER j  39                    
SITE     6 AS7 21 GLN v  60                                                     
SITE     1 AS8  7 TRP c  97  PHE c 109  VAL c 113  VAL c 117                    
SITE     2 AS8  7 HIS c 118  CLA c 503  PHE z  59                               
SITE     1 AS9  8 TYR a 262  ASN a 266  SQD a 412  TRP c  35                    
SITE     2 AS9  8 DGD c 516  LMG e 101  BCR j 102  PHE k  45                    
SITE     1 AT1 17 PHE a 285  LHG a 409  TRP c  63  MET c  67                    
SITE     2 AT1 17 PHE c  70  GLN c  84  GLY c  85  ILE c  87                    
SITE     3 AT1 17 LEU c 404  TRP c 425  SER c 429  CLA c 509                    
SITE     4 AT1 17 DGD c 516  DGD c 517  LMG c 522  PRO k  26                    
SITE     5 AT1 17 VAL k  30                                                     
SITE     1 AT2  9 PHE c 112  VAL c 116  SER c 121  VAL c 124                    
SITE     2 AT2  9 CLA c 511  CLA c 512  BCR c 513  TYR k  15                    
SITE     3 AT2  9 GLY z  55                                                     
SITE     1 AT3  6 HIS c  74  DGD c 516  CLA c 520  ILE g  25                    
SITE     2 AT3  6 BCR j 102  ASP k  23                                          
SITE     1 AT4 18 LEU a  41  ALA a  44  THR a  45  ILE a 115                    
SITE     2 AT4 18 TYR a 126  GLN a 130  TYR a 147  LEU a 174                    
SITE     3 AT4 18 VAL a 283  CLA a 403  CLA a 404  LEU d 205                    
SITE     4 AT4 18 ALA d 208  LEU d 209  ALA d 212  ILE d 213                    
SITE     5 AT4 18 TRP d 253  PHE d 257                                          
SITE     1 AT5 19 PHE a 206  ALA a 209  LEU a 210  MET a 214                    
SITE     2 AT5 19 LEU a 258  CLA a 405  ALA d  41  TRP d  48                    
SITE     3 AT5 19 GLY d 118  LEU d 122  PHE d 125  GLN d 129                    
SITE     4 AT5 19 ASN d 142  PHE d 146  PHE d 153  PHE d 173                    
SITE     5 AT5 19 PRO d 275  LEU d 279  CLA d 405                               
SITE     1 AT6 10 ALA b 228  ARG b 230  LEU b 474  CLA b 612                    
SITE     2 AT6 10 CLA b 613  LMT b 629  LYS d  23  TRP d  32                    
SITE     3 AT6 10 ARG d 134  LEU d 135                                          
SITE     1 AT7  8 HIS a 215  GLU a 244  TYR a 246  HIS a 272                    
SITE     2 AT7  8 FE2 a 413  TYR d 244  LYS d 264  HIS d 268                    
SITE     1 AT8 23 PHE a 206  CLA a 403  CLA a 404  CLA a 405                    
SITE     2 AT8 23 TRP d  48  LEU d 122  VAL d 152  PHE d 153                    
SITE     3 AT8 23 VAL d 156  LEU d 182  PHE d 185  GLN d 186                    
SITE     4 AT8 23 TRP d 191  THR d 192  HIS d 197  GLY d 200                    
SITE     5 AT8 23 VAL d 201  VAL d 204  LEU d 279  SER d 282                    
SITE     6 AT8 23 ALA d 283  VAL d 286  PHO d 402                               
SITE     1 AT9 14 LEU d  43  LEU d  89  LEU d  90  LEU d  91                    
SITE     2 AT9 14 LEU d  92  TRP d  93  THR d 112  PHE d 113                    
SITE     3 AT9 14 HIS d 117  PHE d 120  LMT d 411  GLY x  22                    
SITE     4 AT9 14 LEU x  23  GLY x  26                                          
SITE     1 AU1 12 PHE a  52  CLA a 404  MET d 199  HIS d 214                    
SITE     2 AU1 12 THR d 217  TRP d 253  ALA d 260  PHE d 261                    
SITE     3 AU1 12 LEU d 267  VAL l  26  LMG l 101  PHE t  10                    
SITE     1 AU2 13 ASN a 234  TRP b   5  TYR b   6  ARG b   7                    
SITE     2 AU2 13 PHE b 464  TRP b 468  CLA b 615  CLA b 617                    
SITE     3 AU2 13 ARG d 139  TYR d 141  PHE d 269  PHE d 273                    
SITE     4 AU2 13 LMG l 101                                                     
SITE     1 AU3 13 CLA a 403  PHE d 257  ILE d 259  ALA d 260                    
SITE     2 AU3 13 PHE d 261  SER d 262  ASN d 263  TRP d 266                    
SITE     3 AU3 13 THR l  15  TYR l  18  LEU l  19  PHE t  17                    
SITE     4 AU3 13 ALA t  20                                                     
SITE     1 AU4  7 ASP d 100  PHE d 101  THR d 102  LMT d 411                    
SITE     2 AU4  7 LEU e  42  ASP e  45  VAL e  46                               
SITE     1 AU5  8 LEU d  92  TRP d  93  GLY d  99  CLA d 406                    
SITE     2 AU5  8 DGD d 410  ILE x  21  SER x  25  GLY x  26                    
SITE     1 AU6 12 TYR d  67  GLY d  70  ASN d  72  PHE d  73                    
SITE     2 AU6 12 ILE f  37  MET f  40  GLN f  41  PHE j  28                    
SITE     3 AU6 12 GLY j  31  ALA j  32  GLY j  37  PL9 j 101                    
SITE     1 AU7  7 TYR a 262  LHG c 519  PHE d  27  PRO e   9                    
SITE     2 AU7  7 PHE e  10  SER e  11  PL9 j 101                               
SITE     1 AU8 15 ARG e   8  PHE e  10  ILE e  13  ARG e  18                    
SITE     2 AU8 15 TYR e  19  HIS e  23  THR e  26  LEU e  30                    
SITE     3 AU8 15 ILE f  15  ARG f  19  TRP f  20  VAL f  23                    
SITE     4 AU8 15 HIS f  24  ALA f  27  ILE f  31                               
SITE     1 AU9  9 TYR d  42  LEU d  49  THR d  50  PHE d 101                    
SITE     2 AU9  9 PRO f  29  PHE f  33  VAL j  21  VAL j  25                    
SITE     3 AU9  9 PL9 j 101                                                     
SITE     1 AV1  8 TRP d  21  ARG d  24  ARG d  26  GLU e   7                    
SITE     2 AV1  8 PHE f  16  THR f  17  VAL f  18  THR x  33                    
SITE     1 AV2  7 LMT B 628  ILE a  38  LEU a  42  ALA a  43                    
SITE     2 AV2  7 SQD a 401  CLA a 406  PHE i  15                               
SITE     1 AV3  7 DGD B 626  LMT B 628  SQD a 401  MET i   1                    
SITE     2 AV3  7 THR i   3  LEU i   4  LMT i 103                               
SITE     1 AV4  5 THR i   3  ILE i   6  ILE i  10  PHE i  14                    
SITE     2 AV4  5 LMG i 102                                                     
SITE     1 AV5  6 CLA a 405  PL9 a 407  LMG d 412  LMG e 101                    
SITE     2 AV5  6 BCR f 102  VAL j  16                                          
SITE     1 AV6  7 SQD a 412  DGD c 516  LHG c 519  LMG c 522                    
SITE     2 AV6  7 BCR g 101  PHE j  29  TYR j  33                               
SITE     1 AV7  2 ASP k  19  ASP k  23                                          
SITE     1 AV8 14 SER a 232  ASN a 234  TRP b   5  TYR b   6                    
SITE     2 AV8 14 CLA b 615  TRP d 266  PHE d 269  PL9 d 407                    
SITE     3 AV8 14 LMG d 408  GLU l  11  LEU l  12  ASN l  13                    
SITE     4 AV8 14 SER l  16  ILE l  24                                          
SITE     1 AV9  9 CLA B 613  SQD B 627  VAL L  10  ILE M  24                    
SITE     2 AV9  9 GLN M  28  GLN M  32  ILE m  23  GLU m  30                    
SITE     3 AV9  9 SER m  31                                                     
SITE     1 AW1  2 GLU o 140  HIS o 257                                          
SITE     1 AW2 15 ALA v  62  CYS v  63  CYS v  66  HIS v  67                    
SITE     2 AW2 15 THR v  74  LEU v  78  ASP v  79  LEU v  80                    
SITE     3 AW2 15 THR v  84  LEU v  85  TYR v 101  MET v 102                    
SITE     4 AW2 15 TYR v 108  HIS v 118  PRO v 119                               
SITE     1 AW3 16 BCR c 513  ILE g  28  GLY g  29  GLY g  32                    
SITE     2 AW3 16 ALA j  14  THR j  15  BCR j 102  LEU k  25                    
SITE     3 AW3 16 ILE k  28  LEU k  31  ALA k  34  PHE k  37                    
SITE     4 AW3 16 VAL k  38  ALA k  41  VAL z  13  PHE z  17                    
SITE     1 AW4  9 CLA b 605  CLA b 613  CLA b 614  MET h  35                    
SITE     2 AW4  9 LEU h  37  PHE h  38  PHE h  41  THR x  11                    
SITE     3 AW4  9 LEU x  16                                                     
CRYST1  132.615  229.296  306.825  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      0.007541  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004361  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003259        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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