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Database: PDB
Entry: 4TNJ
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HEADER    ELECTRON TRANSPORT,PHOTOSYNTHESIS       04-JUN-14   4TNJ              
TITLE     RT XFEL STRUCTURE OF PHOTOSYSTEM II 500 MS AFTER THE 2ND ILLUMINATION 
TITLE    2 (2F) AT 4.5 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 4TNJ    1       REMARK                                   
REVDAT   3   27-SEP-17 4TNJ    1       REMARK                                   
REVDAT   2   23-JUL-14 4TNJ    1       JRNL                                     
REVDAT   1   09-JUL-14 4TNJ    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.    4.50 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) : 4.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 72.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.364                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 103594                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.276                           
REMARK   3   R VALUE            (WORKING SET) : 0.276                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.896                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5072                            
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 72.9798 - 13.9511    1.00     3411   149  0.3138 0.3032        
REMARK   3     2 13.9511 - 11.0859    1.00     3387   176  0.2272 0.2217        
REMARK   3     3 11.0859 -  9.6882    1.00     3394   169  0.2200 0.2138        
REMARK   3     4  9.6882 -  8.8040    1.00     3379   168  0.2079 0.2239        
REMARK   3     5  8.8040 -  8.1739    1.00     3403   192  0.2234 0.2128        
REMARK   3     6  8.1739 -  7.6925    1.00     3409   185  0.2346 0.2807        
REMARK   3     7  7.6925 -  7.3077    1.00     3393   170  0.2384 0.2545        
REMARK   3     8  7.3077 -  6.9898    1.00     3347   175  0.2458 0.2869        
REMARK   3     9  6.9898 -  6.7209    1.00     3424   177  0.2569 0.2718        
REMARK   3    10  6.7209 -  6.4892    1.00     3417   173  0.2707 0.3124        
REMARK   3    11  6.4892 -  6.2864    1.00     3351   172  0.2636 0.2590        
REMARK   3    12  6.2864 -  6.1068    1.00     3428   174  0.2777 0.2912        
REMARK   3    13  6.1068 -  5.9461    1.00     3392   188  0.2801 0.3347        
REMARK   3    14  5.9461 -  5.8011    1.00     3404   162  0.2907 0.2844        
REMARK   3    15  5.8011 -  5.6692    1.00     3386   199  0.2995 0.3075        
REMARK   3    16  5.6692 -  5.5486    1.00     3382   157  0.2873 0.3259        
REMARK   3    17  5.5486 -  5.4377    1.00     3429   182  0.3082 0.3028        
REMARK   3    18  5.4377 -  5.3351    1.00     3335   181  0.3038 0.3356        
REMARK   3    19  5.3351 -  5.2398    1.00     3425   164  0.3126 0.3522        
REMARK   3    20  5.2398 -  5.1510    1.00     3374   177  0.3080 0.3008        
REMARK   3    21  5.1510 -  5.0680    0.99     3307   167  0.3202 0.2995        
REMARK   3    22  5.0680 -  4.9900    0.99     3393   198  0.3254 0.3408        
REMARK   3    23  4.9900 -  4.9167    0.98     3334   175  0.3196 0.3218        
REMARK   3    24  4.9167 -  4.8474    0.96     3276   163  0.3395 0.2994        
REMARK   3    25  4.8474 -  4.7819    0.95     3242   161  0.3352 0.3406        
REMARK   3    26  4.7819 -  4.7198    0.92     3052   155  0.3489 0.3529        
REMARK   3    27  4.7198 -  4.6608    0.86     2971   143  0.3623 0.3655        
REMARK   3    28  4.6608 -  4.6047    0.86     2948   161  0.3564 0.3870        
REMARK   3    29  4.6047 -  4.5512    0.81     2736   148  0.3683 0.3759        
REMARK   3    30  4.5512 -  4.5000    0.70     2393   111  0.3779 0.4248        
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)     : 0.648            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.666           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 152.7                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 174.0                          
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     :  0.757          71528                                  
REMARK   3   CHIRALITY :  0.029           7238                                  
REMARK   3   PLANARITY :  0.004           8510                                  
REMARK   3   DIHEDRAL  : 18.658          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 4TNJ 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_1000201918.                                   
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        : 16973                              
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   : 52965                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.970                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 131.4                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 52.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
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       66.14900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      153.98800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      114.35650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      153.98800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       66.14900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      114.35650            
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              2.11            
REMARK 500   O    TRP c   250     OG1  THR c   254              2.12            
REMARK 500   O    TRP C   291     OG1  THR C   305              2.13            
REMARK 500   O    TRP c   291     OG1  THR c   305              2.17            
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. =  13.8 DEGREES          
REMARK 500    PRO b 484   C   -  N   -  CA  ANGL. DEV. =  13.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  12      113.55    156.68                                   
REMARK 500    PRO A 141     -129.69    -74.18                                   
REMARK 500    TRP A 142      -10.47     57.87                                   
REMARK 500    LEU A 159      -50.96   -132.18                                   
REMARK 500    SER A 222       43.06   -109.78                                   
REMARK 500    GLU A 226       10.06   -147.12                                   
REMARK 500    ILE A 259      -84.54   -103.94                                   
REMARK 500    PHE A 302       32.40    -98.39                                   
REMARK 500    ARG A 334      -71.03    -27.38                                   
REMARK 500    ASP B 119       55.12    -91.78                                   
REMARK 500    ARG B 127      -71.75    -63.31                                   
REMARK 500    PRO B 183      175.19    -59.24                                   
REMARK 500    LEU B 218      -67.61    -95.18                                   
REMARK 500    ARG B 230       53.37     31.50                                   
REMARK 500    SER B 294       27.72    -79.83                                   
REMARK 500    ASP B 313       41.82    -91.60                                   
REMARK 500    THR B 436      -70.31    -33.73                                   
REMARK 500    SER B 480      -12.56     70.07                                   
REMARK 500    ILE B 482     -165.91   -117.54                                   
REMARK 500    PRO B 484     -143.81     -7.86                                   
REMARK 500    GLU B 485      164.38     62.54                                   
REMARK 500    LEU B 486       68.84   -155.03                                   
REMARK 500    PRO B 488     -108.51      5.33                                   
REMARK 500    GLU B 489       56.92    -65.19                                   
REMARK 500    GLN B 490      107.87   -167.15                                   
REMARK 500    GLU C  29     -149.64   -148.47                                   
REMARK 500    ARG C 135      -62.72   -121.66                                   
REMARK 500    SER C 144      112.05   -179.97                                   
REMARK 500    ASN C 201       59.14   -168.57                                   
REMARK 500    ILE C 209      -70.11    -53.63                                   
REMARK 500    TRP C 223     -145.28     61.06                                   
REMARK 500    LEU C 253       30.21    -96.38                                   
REMARK 500    PHE C 257     -145.97    -71.51                                   
REMARK 500    ARG C 320      -71.40    -59.53                                   
REMARK 500    PRO C 368       -9.54    -59.70                                   
REMARK 500    LEU C 375      114.06    -34.69                                   
REMARK 500    ASN C 382       12.46   -161.40                                   
REMARK 500    HIS C 398       33.97   -142.05                                   
REMARK 500    SER C 406       65.49     60.08                                   
REMARK 500    ALA C 411      -17.37    -49.62                                   
REMARK 500    SER C 416      -60.84   -176.83                                   
REMARK 500    PHE C 455       23.38   -150.16                                   
REMARK 500    GLU C 462      -76.04    -68.52                                   
REMARK 500    ARG D  26     -165.46   -102.53                                   
REMARK 500    VAL D  30      -83.56    -89.78                                   
REMARK 500    LEU D  37      -71.44    -56.83                                   
REMARK 500    SER D  65       16.45   -141.31                                   
REMARK 500    PRO D 140       37.12    -84.86                                   
REMARK 500    LEU D 158      -65.10   -128.95                                   
REMARK 500    ALA D 234       28.82    -76.04                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     248 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  406                                                       
REMARK 610     DGD A  408                                                       
REMARK 610     LHG A  409                                                       
REMARK 610     LMG A  410                                                       
REMARK 610     SQD A  413                                                       
REMARK 610     LMG A  415                                                       
REMARK 610     DGD B  620                                                       
REMARK 610     LMG B  621                                                       
REMARK 610     LMG B  624                                                       
REMARK 610     DGD B  625                                                       
REMARK 610     SQD B  626                                                       
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     DGD D  409                                                       
REMARK 610     LMT D  410                                                       
REMARK 610     LMG D  412                                                       
REMARK 610     LMG E  101                                                       
REMARK 610     SQD F  102                                                       
REMARK 610     LMG I  101                                                       
REMARK 610     PL9 J  101                                                       
REMARK 610     LMG M  101                                                       
REMARK 610     LMG a  402                                                       
REMARK 610     PL9 a  409                                                       
REMARK 610     DGD a  411                                                       
REMARK 610     LHG a  412                                                       
REMARK 610     LMG a  413                                                       
REMARK 610     SQD a  415                                                       
REMARK 610     DGD b  601                                                       
REMARK 610     SQD b  602                                                       
REMARK 610     DGD b  624                                                       
REMARK 610     LMG b  625                                                       
REMARK 610     LMG b  628                                                       
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  402                                                       
REMARK 610     LMG d  407                                                       
REMARK 610     DGD d  408                                                       
REMARK 610     LMT d  409                                                       
REMARK 610     LMG d  410                                                       
REMARK 610     LMG e  101                                                       
REMARK 610     SQD f  103                                                       
REMARK 610     LMG i  101                                                       
REMARK 610     PL9 j  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  124.3                                              
REMARK 620 3 OEX A 412   O2   60.4  63.8                                        
REMARK 620 4 OEX A 412   O5   94.8  60.5  64.3                                  
REMARK 620 5 GLU A 189   OE1 169.0  63.7 126.7  82.8                            
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  106.7                                              
REMARK 620 3 OEX A 412   O4   68.1  87.4                                        
REMARK 620 4 GLU A 333   OE2 127.5 107.3  74.7                                  
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   83.1                                              
REMARK 620 3 OEX A 412   O5  127.5  90.7                                        
REMARK 620 4 OEX A 412   O3  143.8  89.5  87.8                                  
REMARK 620 5 HIS A 332   NE2  74.7 157.2 106.8 105.4                            
REMARK 620 6 ASP A 342   OD2  66.2  89.8 166.2  78.5  76.8                      
REMARK 620 N                    1     2     3     4     5                       
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  96.4                                              
REMARK 620 3 HIS D 214   NE2 125.2 113.8                                        
REMARK 620 4 HIS D 268   NE2  79.8 154.9  87.8                                  
REMARK 620 5 BCT D 404   O3  129.9  91.6  95.2  73.0                            
REMARK 620 6 BCT D 404   O2   84.0  81.5 142.4  73.5  48.5                      
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   96.8  88.6                                        
REMARK 620 4 OEX A 412   O4   83.9  92.0 178.2                                  
REMARK 620 5 OEX A 412   O5  107.3 115.9  89.0  89.2                            
REMARK 620 6 GLU C 354   OE2  67.1  74.1  71.4 110.3 158.2                      
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  111.4                                              
REMARK 620 3 OEX A 412   O2  159.1  89.3                                        
REMARK 620 4 OEX A 412   O3   93.3  87.0  85.3                                  
REMARK 620 5 ALA A 344   OXT  98.9 130.1  67.4 130.9                            
REMARK 620 N                    1     2     3     4                             
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   96.2                                              
REMARK 620 3 CLA C 510   NB   75.2  92.2                                        
REMARK 620 4 CLA C 510   NC   84.2 176.7  91.0                                  
REMARK 620 5 CLA C 510   ND  104.1  90.7 177.0  86.0                            
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   87.3                                              
REMARK 620 3 HEM F 101   NB  104.3  89.3                                        
REMARK 620 4 HEM F 101   NC   89.3 175.5  88.7                                  
REMARK 620 5 HEM F 101   ND   67.2  90.4 171.6  90.9                            
REMARK 620 6 HIS F  24   NE2 157.7  70.4  75.3 112.9 112.5                      
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 132.5                                              
REMARK 620 3 ASP K  23   OD2 124.7  46.4                                        
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   88.6  89.8                                        
REMARK 620 4 HEM V 201   NC   88.5 175.4  90.1                                  
REMARK 620 5 HEM V 201   ND   81.5  88.6 170.0  90.7                            
REMARK 620 6 HIS V 118   NE2 169.4  87.3 100.3  97.2  89.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 414  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD1                                                    
REMARK 620 2 OEX a 414   O1  126.1                                              
REMARK 620 3 OEX a 414   O2   62.6  63.6                                        
REMARK 620 4 OEX a 414   O5   97.5  61.0  63.9                                  
REMARK 620 5 GLU a 189   OE1 170.0  62.7 125.4  82.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 414  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD2                                                    
REMARK 620 2 OEX a 414   O5  110.5                                              
REMARK 620 3 OEX a 414   O4   66.9  87.6                                        
REMARK 620 4 GLU a 333   OE2 123.1 107.7  74.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 414  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 OEX a 414   O1   85.0                                              
REMARK 620 3 OEX a 414   O5  129.2  90.6                                        
REMARK 620 4 OEX a 414   O3  142.5  89.4  87.7                                  
REMARK 620 5 HIS a 332   NE2  70.8 155.4 107.6 107.2                            
REMARK 620 6 ASP a 342   OD2  63.0  89.8 167.7  80.0  75.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a 403  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS a 272   NE2  96.3                                              
REMARK 620 3 HIS d 214   NE2 120.4 112.2                                        
REMARK 620 4 HIS d 268   NE2  78.4 156.6  89.7                                  
REMARK 620 5 BCT d 403   O2   87.1  85.3 143.5  71.7                            
REMARK 620 6 BCT d 403   O3  133.4  94.5  96.5  74.1  48.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 414  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 OEX a 414   O2  136.8                                              
REMARK 620 3 OEX a 414   O3   98.0  88.7                                        
REMARK 620 4 OEX a 414   O4   82.3  92.0 178.6                                  
REMARK 620 5 OEX a 414   O5  107.6 115.2  89.1  89.5                            
REMARK 620 6 GLU c 354   OE2  68.4  73.2  73.0 108.4 160.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 414  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 342   OD1                                                    
REMARK 620 2 OEX a 414   O1  109.3                                              
REMARK 620 3 OEX a 414   O2  161.2  89.3                                        
REMARK 620 4 OEX a 414   O3   93.0  87.1  85.4                                  
REMARK 620 5 ALA a 344   OXT 101.6 129.0  66.6 131.3                            
REMARK 620 6 GLU c 354   OE1  66.9 158.2  95.0  72.0  71.8                      
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   95.8                                              
REMARK 620 3 CLA c 510   NB   75.2  92.2                                        
REMARK 620 4 CLA c 510   NC   84.5 176.7  91.0                                  
REMARK 620 5 CLA c 510   ND  104.2  90.7 177.1  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   87.6                                              
REMARK 620 3 HEM f 101   NB  103.5  89.5                                        
REMARK 620 4 HEM f 101   NC   88.5 175.0  88.4                                  
REMARK 620 5 HEM f 101   ND   67.4  90.2 170.8  91.2                            
REMARK 620 6 HIS f  24   NE2 157.7  70.2  78.1 113.7 110.3                      
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 124.2                                              
REMARK 620 3 ASP k  23   OD2 115.3  41.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM v 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS v  67   NE2                                                    
REMARK 620 2 HEM v 201   NA   86.2                                              
REMARK 620 3 HEM v 201   NB   86.5  89.3                                        
REMARK 620 4 HEM v 201   NC   89.3 175.5  90.2                                  
REMARK 620 5 HEM v 201   ND   83.7  89.8 170.2  90.0                            
REMARK 620 6 HIS v 118   NE2 170.4  86.9 100.2  97.6  89.6                      
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 CLA A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 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 LMG A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD B 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 628                 
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 BCR 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 DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT D 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM F 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD F 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG I 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT I 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 J 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR J 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA K 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG M 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT M 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT M 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR y 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD a 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 416                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD b 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT b 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG c 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD d 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT d 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR f 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG i 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT i 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 j 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR j 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA k 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 RT STRUCTURE OF THE DARK STATE OF PHOTOSYSTEM II                     
REMARK 900 RELATED ID: 4TNI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4TNK   RELATED DB: PDB                                   
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  4TNJ A    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  4TNJ B    1   510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  4TNJ C   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  4TNJ D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  4TNJ E    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  4TNJ F    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  4TNJ H    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  4TNJ I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4TNJ J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4TNJ K    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  4TNJ L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4TNJ M    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  4TNJ O    1   272  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  4TNJ T    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  4TNJ U    1   134  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  4TNJ V    1   163  UNP    P0A386   CY550_THEEB      1    163             
DBREF  4TNJ y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  4TNJ X   10    50  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  4TNJ Y    1    28  PDB    4TNJ     4TNJ             1     28             
DBREF  4TNJ Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  4TNJ a    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  4TNJ b    1   510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  4TNJ c   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  4TNJ d    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  4TNJ e    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  4TNJ f    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  4TNJ h    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  4TNJ i    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4TNJ j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4TNJ k    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  4TNJ l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4TNJ m    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  4TNJ o    1   272  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  4TNJ t    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  4TNJ u    1   134  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  4TNJ v    1   163  UNP    P0A386   CY550_THEEB      1    163             
DBREF  4TNJ g    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  4TNJ x   10    50  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  4TNJ G    1    28  PDB    4TNJ     4TNJ             1     28             
DBREF  4TNJ 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    CLA  A 405      65                                                       
HET    PL9  A 406      45                                                       
HET    BCR  A 407      40                                                       
HET    DGD  A 408      56                                                       
HET    LHG  A 409      39                                                       
HET    LMG  A 410      51                                                       
HET     CL  A 411       1                                                       
HET    OEX  A 412      10                                                       
HET    SQD  A 413      51                                                       
HET    SQD  A 414      54                                                       
HET    LMG  A 415      42                                                       
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    LMT  B 622      35                                                       
HET    LMT  B 623      35                                                       
HET    LMG  B 624      49                                                       
HET    DGD  B 625      52                                                       
HET    SQD  B 626      47                                                       
HET    LMT  B 627      35                                                       
HET    LMT  B 628      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      48                                                       
HET    DGD  D 409      63                                                       
HET    LMT  D 410      31                                                       
HET    BCR  D 411      40                                                       
HET    LMG  D 412      46                                                       
HET    LMG  E 101      44                                                       
HET    HEM  F 101      43                                                       
HET    SQD  F 102      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     CA  K 101       1                                                       
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    FE2  a 403       1                                                       
HET    CLA  a 404      65                                                       
HET    CLA  a 405      65                                                       
HET    CLA  a 406      65                                                       
HET    PHO  a 407      64                                                       
HET    CLA  a 408      65                                                       
HET    PL9  a 409      45                                                       
HET    BCR  a 410      40                                                       
HET    DGD  a 411      56                                                       
HET    LHG  a 412      39                                                       
HET    LMG  a 413      51                                                       
HET    OEX  a 414      10                                                       
HET    SQD  a 415      51                                                       
HET     CL  a 416       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    BCR  b 620      40                                                       
HET    BCR  b 621      40                                                       
HET    BCR  b 622      40                                                       
HET    BCR  b 623      40                                                       
HET    DGD  b 624      58                                                       
HET    LMG  b 625      49                                                       
HET    LMT  b 626      35                                                       
HET    LMT  b 627      35                                                       
HET    LMG  b 628      49                                                       
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    SQD  d 402      43                                                       
HET    BCT  d 403       4                                                       
HET    CLA  d 404      65                                                       
HET    CLA  d 405      65                                                       
HET    PL9  d 406      55                                                       
HET    LMG  d 407      48                                                       
HET    DGD  d 408      63                                                       
HET    LMT  d 409      31                                                       
HET    LMG  d 410      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    LMG  i 101      43                                                       
HET    LMT  i 102      35                                                       
HET    PL9  j 101      35                                                       
HET    BCR  j 102      40                                                       
HET     CA  k 101       1                                                       
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     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     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
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     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETNAM     PHO PHEOPHYTIN A                                                     
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  46  PL9    6(C53 H80 O2)                                                
FORMUL  47  BCR    24(C40 H56)                                                  
FORMUL  48  DGD    14(C51 H96 O15)                                              
FORMUL  49  LHG    4(C38 H75 O10 P)                                             
FORMUL  50  LMG    22(C45 H86 O10)                                              
FORMUL  51   CL    2(CL 1-)                                                     
FORMUL  52  OEX    2(CA MN4 O5)                                                 
FORMUL  53  SQD    10(C41 H78 O12 S)                                            
FORMUL  77  LMT    14(C24 H46 O11)                                              
FORMUL  06  PHO    4(C55 H74 N4 O5)                                             
FORMUL  09  BCT    2(C H O3 1-)                                                 
FORMUL  19  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  27   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  TYR A  147  1                                   6    
HELIX    8 AA8 TYR A  147  LEU A  159  1                                  13    
HELIX    9 AA9 LEU A  159  GLY A  166  1                                   8    
HELIX   10 AB1 SER A  167  GLY A  171  5                                   5    
HELIX   11 AB2 ILE A  176  ASN A  191  1                                  16    
HELIX   12 AB3 ILE A  192  MET A  194  5                                   3    
HELIX   13 AB4 HIS A  195  SER A  222  1                                  28    
HELIX   14 AB5 SER A  232  TYR A  237  5                                   6    
HELIX   15 AB6 ASN A  247  ILE A  259  1                                  13    
HELIX   16 AB7 PHE A  260  SER A  264  5                                   5    
HELIX   17 AB8 ASN A  267  MET A  293  1                                  27    
HELIX   18 AB9 THR A  316  HIS A  332  1                                  17    
HELIX   19 AC1 GLU A  333  HIS A  337  5                                   5    
HELIX   20 AC2 PRO B    4  ILE B   13  5                                  10    
HELIX   21 AC3 ASP B   15  ALA B   43  1                                  29    
HELIX   22 AC4 PRO B   54  GLN B   58  5                                   5    
HELIX   23 AC5 VAL B   62  ARG B   68  1                                   7    
HELIX   24 AC6 SER B   92  TYR B  117  1                                  26    
HELIX   25 AC7 LEU B  120  ARG B  124  5                                   5    
HELIX   26 AC8 ASP B  134  PHE B  156  1                                  23    
HELIX   27 AC9 GLY B  186  ASN B  191  5                                   6    
HELIX   28 AD1 ASN B  194  VAL B  219  1                                  26    
HELIX   29 AD2 PRO B  222  LEU B  229  1                                   8    
HELIX   30 AD3 ASN B  233  GLU B  235  5                                   3    
HELIX   31 AD4 THR B  236  TYR B  258  1                                  23    
HELIX   32 AD5 PRO B  264  GLY B  269  1                                   6    
HELIX   33 AD6 THR B  271  SER B  277  1                                   7    
HELIX   34 AD7 SER B  278  SER B  294  1                                  17    
HELIX   35 AD8 THR B  297  ILE B  305  1                                   9    
HELIX   36 AD9 PRO B  306  TYR B  312  1                                   7    
HELIX   37 AE1 ASP B  313  ASN B  318  5                                   6    
HELIX   38 AE2 PRO B  329  GLY B  333  5                                   5    
HELIX   39 AE3 ARG B  384  SER B  388  5                                   5    
HELIX   40 AE4 SER B  391  GLY B  396  1                                   6    
HELIX   41 AE5 ASP B  413  ILE B  425  1                                  13    
HELIX   42 AE6 SER B  446  PHE B  475  1                                  30    
HELIX   43 AE7 ALA C   34  ILE C   43  5                                  10    
HELIX   44 AE8 LEU C   45  PHE C   75  1                                  31    
HELIX   45 AE9 PRO C   80  GLN C   84  5                                   5    
HELIX   46 AF1 LEU C   88  LEU C   95  1                                   8    
HELIX   47 AF2 GLY C  100  GLU C  104  5                                   5    
HELIX   48 AF3 THR C  108  ARG C  135  1                                  28    
HELIX   49 AF4 ASP C  153  PHE C  181  1                                  29    
HELIX   50 AF5 ASP C  205  PHE C  210  1                                   6    
HELIX   51 AF6 GLY C  211  LYS C  215  5                                   5    
HELIX   52 AF7 GLY C  222  VAL C  227  5                                   6    
HELIX   53 AF8 ASN C  229  LEU C  253  1                                  25    
HELIX   54 AF9 GLY C  258  PHE C  264  1                                   7    
HELIX   55 AG1 SER C  267  ASN C  293  1                                  27    
HELIX   56 AG2 THR C  305  LEU C  324  1                                  20    
HELIX   57 AG3 ASN C  327  ALA C  331  5                                   5    
HELIX   58 AG4 GLY C  353  TRP C  359  5                                   7    
HELIX   59 AG5 LEU C  366  PRO C  368  5                                   3    
HELIX   60 AG6 ASP C  376  ASP C  383  1                                   8    
HELIX   61 AG7 GLN C  385  THR C  397  1                                  13    
HELIX   62 AG8 SER C  421  GLY C  454  1                                  34    
HELIX   63 AG9 GLU C  464  MET C  469  5                                   6    
HELIX   64 AH1 TRP D   14  LYS D   23  1                                  10    
HELIX   65 AH2 VAL D   30  PHE D   54  1                                  25    
HELIX   66 AH3 SER D   57  GLY D   62  1                                   6    
HELIX   67 AH4 SER D   66  GLY D   70  5                                   5    
HELIX   68 AH5 ASP D  100  LEU D  107  1                                   8    
HELIX   69 AH6 GLY D  108  GLY D  137  1                                  30    
HELIX   70 AH7 PRO D  140  PHE D  146  1                                   7    
HELIX   71 AH8 PHE D  146  LEU D  158  1                                  13    
HELIX   72 AH9 LEU D  158  GLN D  164  1                                   7    
HELIX   73 AI1 SER D  166  ALA D  170  5                                   5    
HELIX   74 AI2 VAL D  175  ASN D  190  1                                  16    
HELIX   75 AI3 TRP D  191  LEU D  193  5                                   3    
HELIX   76 AI4 ASN D  194  ASN D  220  1                                  27    
HELIX   77 AI5 SER D  245  PHE D  257  1                                  13    
HELIX   78 AI6 ASN D  263  LEU D  291  1                                  29    
HELIX   79 AI7 PHE D  298  ASP D  308  1                                  11    
HELIX   80 AI8 THR D  313  GLN D  334  1                                  22    
HELIX   81 AI9 PRO D  335  ASN D  338  5                                   4    
HELIX   82 AJ1 PRO D  342  LEU D  346  5                                   5    
HELIX   83 AJ2 PRO E    9  SER E   16  1                                   8    
HELIX   84 AJ3 SER E   16  THR E   40  1                                  25    
HELIX   85 AJ4 GLY E   41  PHE E   47  1                                   7    
HELIX   86 AJ5 GLU E   71  GLN E   82  1                                  12    
HELIX   87 AJ6 THR F   17  GLN F   41  1                                  25    
HELIX   88 AJ7 THR H    5  LEU H   11  1                                   7    
HELIX   89 AJ8 THR H   27  ASN H   50  1                                  24    
HELIX   90 AJ9 GLU I    2  SER I   25  1                                  24    
HELIX   91 AK1 PRO J    9  ALA J   32  1                                  24    
HELIX   92 AK2 ALA K   14  ILE K   17  5                                   4    
HELIX   93 AK3 PHE K   18  ASP K   23  1                                   6    
HELIX   94 AK4 VAL K   24  PRO K   26  5                                   3    
HELIX   95 AK5 VAL K   27  VAL K   43  1                                  17    
HELIX   96 AK6 ASN L   13  ASN L   37  1                                  25    
HELIX   97 AK7 LEU M    6  SER M   31  1                                  26    
HELIX   98 AK8 GLY O   40  LYS O   44  5                                   5    
HELIX   99 AK9 LEU O  208  VAL O  213  1                                   6    
HELIX  100 AL1 GLU T    2  PHE T   23  1                                  22    
HELIX  101 AL2 ASN U   41  LEU U   47  1                                   7    
HELIX  102 AL3 ASN U   61  TYR U   68  5                                   8    
HELIX  103 AL4 PRO U   73  ASN U   82  1                                  10    
HELIX  104 AL5 SER U   87  ILE U   94  5                                   8    
HELIX  105 AL6 THR U   98  LEU U  109  1                                  12    
HELIX  106 AL7 GLU U  118  GLU U  123  1                                   6    
HELIX  107 AL8 GLY U  124  ASP U  126  5                                   3    
HELIX  108 AL9 THR V   48  CYS V   63  1                                  16    
HELIX  109 AM1 CYS V   63  VAL V   68  1                                   6    
HELIX  110 AM2 GLY V   69  ILE V   71  5                                   3    
HELIX  111 AM3 ARG V   81  LEU V   87  1                                   7    
HELIX  112 AM4 ASN V   94  MET V  102  1                                   9    
HELIX  113 AM5 SER V  120  ALA V  124  5                                   5    
HELIX  114 AM6 PRO V  128  LEU V  133  1                                   6    
HELIX  115 AM7 THR V  134  GLY V  153  1                                  20    
HELIX  116 AM8 GLY V  153  GLY V  158  1                                   6    
HELIX  117 AM9 GLY V  159  TYR V  163  5                                   5    
HELIX  118 AN1 GLN y   21  ARG y   42  1                                  22    
HELIX  119 AN2 THR X   13  GLN X   42  1                                  30    
HELIX  120 AN3 UNK Y    2  UNK Y   13  1                                  12    
HELIX  121 AN4 UNK Y   14  UNK Y   25  1                                  12    
HELIX  122 AN5 THR Z    2  SER Z   29  1                                  28    
HELIX  123 AN6 ARG Z   35  VAL Z   62  1                                  28    
HELIX  124 AN7 ASN a   12  THR a   22  1                                  11    
HELIX  125 AN8 PHE a   33  ALA a   55  1                                  23    
HELIX  126 AN9 SER a   70  GLY a   74  5                                   5    
HELIX  127 AO1 PRO a   95  ALA a   99  5                                   5    
HELIX  128 AO2 SER a  101  ASN a  108  1                                   8    
HELIX  129 AO3 GLY a  109  LEU a  137  1                                  29    
HELIX  130 AO4 TRP a  142  TYR a  147  1                                   6    
HELIX  131 AO5 TYR a  147  LEU a  159  1                                  13    
HELIX  132 AO6 LEU a  159  GLY a  166  1                                   8    
HELIX  133 AO7 SER a  167  GLY a  171  5                                   5    
HELIX  134 AO8 ILE a  176  ASN a  191  1                                  16    
HELIX  135 AO9 ILE a  192  MET a  194  5                                   3    
HELIX  136 AP1 HIS a  195  SER a  222  1                                  28    
HELIX  137 AP2 SER a  232  TYR a  237  5                                   6    
HELIX  138 AP3 ASN a  247  ILE a  259  1                                  13    
HELIX  139 AP4 PHE a  260  SER a  264  5                                   5    
HELIX  140 AP5 ASN a  267  MET a  293  1                                  27    
HELIX  141 AP6 THR a  316  HIS a  332  1                                  17    
HELIX  142 AP7 GLU a  333  HIS a  337  5                                   5    
HELIX  143 AP8 PRO b    4  ILE b   13  5                                  10    
HELIX  144 AP9 ASP b   15  ALA b   43  1                                  29    
HELIX  145 AQ1 PRO b   54  GLN b   58  5                                   5    
HELIX  146 AQ2 VAL b   62  ARG b   68  1                                   7    
HELIX  147 AQ3 SER b   92  TYR b  117  1                                  26    
HELIX  148 AQ4 LEU b  120  ARG b  124  5                                   5    
HELIX  149 AQ5 ASP b  134  PHE b  156  1                                  23    
HELIX  150 AQ6 GLY b  186  ASN b  191  5                                   6    
HELIX  151 AQ7 ASN b  194  VAL b  219  1                                  26    
HELIX  152 AQ8 PRO b  222  LEU b  229  1                                   8    
HELIX  153 AQ9 ASN b  233  GLU b  235  5                                   3    
HELIX  154 AR1 THR b  236  TYR b  258  1                                  23    
HELIX  155 AR2 PRO b  264  GLY b  269  1                                   6    
HELIX  156 AR3 THR b  271  SER b  277  1                                   7    
HELIX  157 AR4 SER b  278  SER b  294  1                                  17    
HELIX  158 AR5 THR b  297  ILE b  305  1                                   9    
HELIX  159 AR6 PRO b  306  TYR b  312  1                                   7    
HELIX  160 AR7 ASP b  313  ASN b  318  5                                   6    
HELIX  161 AR8 PRO b  329  GLY b  333  5                                   5    
HELIX  162 AR9 ARG b  384  SER b  388  5                                   5    
HELIX  163 AS1 SER b  391  GLY b  396  1                                   6    
HELIX  164 AS2 ASP b  413  ILE b  425  1                                  13    
HELIX  165 AS3 SER b  446  PHE b  475  1                                  30    
HELIX  166 AS4 ALA c   34  ILE c   43  5                                  10    
HELIX  167 AS5 LEU c   45  PHE c   75  1                                  31    
HELIX  168 AS6 PRO c   80  GLN c   84  5                                   5    
HELIX  169 AS7 LEU c   88  LEU c   95  1                                   8    
HELIX  170 AS8 GLY c  100  GLU c  104  5                                   5    
HELIX  171 AS9 THR c  108  ARG c  135  1                                  28    
HELIX  172 AT1 ASP c  153  PHE c  181  1                                  29    
HELIX  173 AT2 ASP c  205  PHE c  210  1                                   6    
HELIX  174 AT3 GLY c  211  LYS c  215  5                                   5    
HELIX  175 AT4 GLY c  222  VAL c  227  5                                   6    
HELIX  176 AT5 ASN c  229  LEU c  253  1                                  25    
HELIX  177 AT6 GLY c  258  PHE c  264  1                                   7    
HELIX  178 AT7 SER c  267  ASN c  293  1                                  27    
HELIX  179 AT8 THR c  305  LEU c  324  1                                  20    
HELIX  180 AT9 ASN c  327  ALA c  331  5                                   5    
HELIX  181 AU1 GLY c  353  TRP c  359  5                                   7    
HELIX  182 AU2 LEU c  366  PRO c  368  5                                   3    
HELIX  183 AU3 ASP c  376  ASP c  383  1                                   8    
HELIX  184 AU4 GLN c  385  THR c  397  1                                  13    
HELIX  185 AU5 SER c  421  GLY c  454  1                                  34    
HELIX  186 AU6 GLU c  464  MET c  469  5                                   6    
HELIX  187 AU7 TRP d   14  LYS d   23  1                                  10    
HELIX  188 AU8 VAL d   30  PHE d   54  1                                  25    
HELIX  189 AU9 SER d   57  GLY d   62  1                                   6    
HELIX  190 AV1 SER d   66  GLY d   70  5                                   5    
HELIX  191 AV2 ASP d  100  LEU d  107  1                                   8    
HELIX  192 AV3 GLY d  108  GLY d  137  1                                  30    
HELIX  193 AV4 PRO d  140  PHE d  146  1                                   7    
HELIX  194 AV5 PHE d  146  LEU d  158  1                                  13    
HELIX  195 AV6 LEU d  158  GLN d  164  1                                   7    
HELIX  196 AV7 SER d  166  ALA d  170  5                                   5    
HELIX  197 AV8 VAL d  175  ASN d  190  1                                  16    
HELIX  198 AV9 TRP d  191  LEU d  193  5                                   3    
HELIX  199 AW1 ASN d  194  ASN d  220  1                                  27    
HELIX  200 AW2 SER d  245  PHE d  257  1                                  13    
HELIX  201 AW3 ASN d  263  LEU d  291  1                                  29    
HELIX  202 AW4 PHE d  298  ASP d  308  1                                  11    
HELIX  203 AW5 THR d  313  GLN d  334  1                                  22    
HELIX  204 AW6 PRO d  335  ASN d  338  5                                   4    
HELIX  205 AW7 PRO d  342  LEU d  346  5                                   5    
HELIX  206 AW8 PRO e    9  SER e   16  1                                   8    
HELIX  207 AW9 SER e   16  THR e   40  1                                  25    
HELIX  208 AX1 GLY e   41  PHE e   47  1                                   7    
HELIX  209 AX2 GLU e   71  GLN e   82  1                                  12    
HELIX  210 AX3 THR f   17  GLN f   41  1                                  25    
HELIX  211 AX4 THR h    5  LEU h   11  1                                   7    
HELIX  212 AX5 THR h   27  ASN h   50  1                                  24    
HELIX  213 AX6 GLU i    2  SER i   25  1                                  24    
HELIX  214 AX7 PRO j    9  ALA j   32  1                                  24    
HELIX  215 AX8 ALA k   14  ILE k   17  5                                   4    
HELIX  216 AX9 PHE k   18  ASP k   23  1                                   6    
HELIX  217 AY1 VAL k   24  PRO k   26  5                                   3    
HELIX  218 AY2 VAL k   27  VAL k   43  1                                  17    
HELIX  219 AY3 ASN l   13  ASN l   37  1                                  25    
HELIX  220 AY4 LEU m    6  SER m   31  1                                  26    
HELIX  221 AY5 GLY o   40  LYS o   44  5                                   5    
HELIX  222 AY6 LEU o  208  VAL o  213  1                                   6    
HELIX  223 AY7 GLU t    2  PHE t   23  1                                  22    
HELIX  224 AY8 ASN u   41  LEU u   47  1                                   7    
HELIX  225 AY9 ASN u   61  TYR u   68  5                                   8    
HELIX  226 AZ1 PRO u   73  ASN u   82  1                                  10    
HELIX  227 AZ2 SER u   87  ILE u   94  5                                   8    
HELIX  228 AZ3 THR u   98  LEU u  109  1                                  12    
HELIX  229 AZ4 GLU u  118  GLU u  123  1                                   6    
HELIX  230 AZ5 GLY u  124  ASP u  126  5                                   3    
HELIX  231 AZ6 THR v   48  CYS v   63  1                                  16    
HELIX  232 AZ7 CYS v   63  VAL v   68  1                                   6    
HELIX  233 AZ8 GLY v   69  ILE v   71  5                                   3    
HELIX  234 AZ9 ARG v   81  LEU v   87  1                                   7    
HELIX  235 BA1 ASN v   94  MET v  102  1                                   9    
HELIX  236 BA2 SER v  120  ALA v  124  5                                   5    
HELIX  237 BA3 PRO v  128  LEU v  133  1                                   6    
HELIX  238 BA4 THR v  134  GLY v  153  1                                  20    
HELIX  239 BA5 GLY v  153  GLY v  158  1                                   6    
HELIX  240 BA6 GLY v  159  TYR v  163  5                                   5    
HELIX  241 BA7 GLN g   21  ARG g   42  1                                  22    
HELIX  242 BA8 THR x   13  GLN x   42  1                                  30    
HELIX  243 BA9 UNK G    2  UNK G   12  1                                  11    
HELIX  244 BB1 UNK G   14  UNK G   25  1                                  12    
HELIX  245 BB2 THR z    2  SER z   29  1                                  28    
HELIX  246 BB3 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  LYS O 260   N  LEU O  77           
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  THR b 398   N  ARG b 347           
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  ALA o 228   O  ALA o 238           
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  3.20  
LINK         OD2 ASP A 170                MN4  OEX A 412     1555   1555  2.75  
LINK         OE1 GLU A 189                CA1  OEX A 412     1555   1555  3.08  
LINK         OE2 GLU A 189                MN1  OEX A 412     1555   1555  2.48  
LINK         NE2 HIS A 215                FE   FE2 A 401     1555   1555  2.53  
LINK         NE2 HIS A 272                FE   FE2 A 401     1555   1555  2.54  
LINK         NE2 HIS A 332                MN1  OEX A 412     1555   1555  2.54  
LINK         OE1 GLU A 333                MN3  OEX A 412     1555   1555  2.51  
LINK         OE2 GLU A 333                MN4  OEX A 412     1555   1555  2.73  
LINK         OD1 ASP A 342                MN2  OEX A 412     1555   1555  2.60  
LINK         OD2 ASP A 342                MN1  OEX A 412     1555   1555  2.78  
LINK         OXT ALA A 344                MN2  OEX A 412     1555   1555  2.58  
LINK         OD1 ASN C  39                MG   CLA C 510     1555   1555  2.88  
LINK         OE2 GLU C 354                MN3  OEX A 412     1555   1555  2.70  
LINK         NE2 HIS D 214                FE   FE2 A 401     1555   1555  2.51  
LINK         NE2 HIS D 268                FE   FE2 A 401     1555   1555  2.67  
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  2.59  
LINK         OD1 ASP K  23                CA    CA K 101     1555   1555  2.88  
LINK         OD2 ASP K  23                CA    CA K 101     1555   1555  2.67  
LINK         OE1 GLU O 140                CA    CA O 301     1555   1555  2.60  
LINK         NE2 HIS V  67                FE   HEM V 201     1555   1555  2.50  
LINK         NE2 HIS V 118                FE   HEM V 201     1555   1555  2.58  
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 414     1555   1555  3.00  
LINK         OD2 ASP a 170                MN4  OEX a 414     1555   1555  2.74  
LINK         OE1 GLU a 189                CA1  OEX a 414     1555   1555  3.06  
LINK         OE2 GLU a 189                MN1  OEX a 414     1555   1555  2.52  
LINK         NE2 HIS a 215                FE   FE2 a 403     1555   1555  2.58  
LINK         NE2 HIS a 272                FE   FE2 a 403     1555   1555  2.57  
LINK         NE2 HIS a 332                MN1  OEX a 414     1555   1555  2.53  
LINK         OE1 GLU a 333                MN3  OEX a 414     1555   1555  2.53  
LINK         OE2 GLU a 333                MN4  OEX a 414     1555   1555  2.79  
LINK         OD1 ASP a 342                MN2  OEX a 414     1555   1555  2.59  
LINK         OD2 ASP a 342                MN1  OEX a 414     1555   1555  2.79  
LINK         OXT ALA a 344                MN2  OEX a 414     1555   1555  2.59  
LINK         OD1 ASN c  39                MG   CLA c 510     1555   1555  2.94  
LINK         OE1 GLU c 354                MN2  OEX a 414     1555   1555  2.72  
LINK         OE2 GLU c 354                MN3  OEX a 414     1555   1555  2.65  
LINK         NE2 HIS d 214                FE   FE2 a 403     1555   1555  2.55  
LINK         NE2 HIS d 268                FE   FE2 a 403     1555   1555  2.68  
LINK         NE2 HIS e  23                FE   HEM f 101     1555   1555  2.60  
LINK         NE2 HIS f  24                FE   HEM f 101     1555   1555  2.64  
LINK         OD2 ASP k  19                CA    CA k 101     1555   1555  2.56  
LINK         OD1 ASP k  23                CA    CA k 101     1555   1555  3.17  
LINK         OD2 ASP k  23                CA    CA k 101     1555   1555  2.99  
LINK         OE1 GLU o 140                CA    CA o 301     1555   1555  2.57  
LINK         NE2 HIS v  67                FE   HEM v 201     1555   1555  2.53  
LINK         NE2 HIS v 118                FE   HEM v 201     1555   1555  2.62  
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                 O3  BCT D 404     1555   1555  2.67  
LINK        FE   FE2 A 401                 O2  BCT D 404     1555   1555  2.68  
LINK        FE   FE2 a 403                 O2  BCT d 403     1555   1555  2.65  
LINK        FE   FE2 a 403                 O3  BCT d 403     1555   1555  2.67  
CISPEP   1 THR V   89    PRO V   90          0        -0.74                     
CISPEP   2 THR v   89    PRO v   90          0        -0.81                     
SITE     1 AC1  5 HIS A 215  HIS A 272  HIS D 214  HIS D 268                    
SITE     2 AC1  5 BCT D 404                                                     
SITE     1 AC2 23 PHE A 119  TYR A 147  PRO A 150  SER A 153                    
SITE     2 AC2 23 VAL A 157  MET A 183  PHE A 186  GLN A 187                    
SITE     3 AC2 23 LEU A 193  HIS A 198  GLY A 201  VAL A 205                    
SITE     4 AC2 23 PHE A 206  VAL A 283  THR A 286  ILE A 290                    
SITE     5 AC2 23 CLA A 403  CLA A 404  LEU D 182  LEU D 205                    
SITE     6 AC2 23 PHO D 401  CLA D 405  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 MET D 198  VAL D 201  ALA D 202  PHO D 401                    
SITE     4 AC3 14 CLA D 405  PL9 D 407                                          
SITE     1 AC4 15 GLN A 199  VAL A 202  ALA A 203  LEU A 210                    
SITE     2 AC4 15 TRP A 278  CLA A 402  PL9 A 406  PHE D 157                    
SITE     3 AC4 15 VAL D 175  ILE D 178  PHE D 179  PHE D 181                    
SITE     4 AC4 15 LEU D 182  PHO D 402  CLA D 405                               
SITE     1 AC5 14 ILE A  36  PRO A  39  THR A  40  PHE A  93                    
SITE     2 AC5 14 PRO A  95  ILE A  96  TRP A  97  LEU A 114                    
SITE     3 AC5 14 HIS A 118  LEU A 121  BCR A 407  DGD A 408                    
SITE     4 AC5 14 TYR I   9  PHE I  15                                          
SITE     1 AC6 15 HIS A 215  LEU A 218  HIS A 252  PHE A 255                    
SITE     2 AC6 15 SER A 264  PHE A 265  LEU A 271  PHE A 274                    
SITE     3 AC6 15 CLA A 404  PHE D  38  ALA D  41  TYR D  42                    
SITE     4 AC6 15 ALA F  22  THR F  25  PL9 J 101                               
SITE     1 AC7  8 ILE A  38  LEU A  42  ALA A  43  TRP A 105                    
SITE     2 AC7  8 CLA A 405  SQD A 414  PHE I  15  LMT b 603                    
SITE     1 AC8 13 PHE A  93  TRP A  97  GLU A  98  CLA A 405                    
SITE     2 AC8 13 LEU C 214  LYS C 215  SER C 216  PRO C 217                    
SITE     3 AC8 13 TRP C 223  PHE C 284  LYS I   5  TYR I   9                    
SITE     4 AC8 13 GLY O  38                                                     
SITE     1 AC9 14 ARG A 140  TRP A 142  PHE A 273  SQD A 413                    
SITE     2 AC9 14 TRP C  36  TRP C 443  ARG C 447  CLA C 507                    
SITE     3 AC9 14 CLA C 520  ASN D 220  ALA D 229  SER D 230                    
SITE     4 AC9 14 THR D 231  PHE D 232                                          
SITE     1 AD1 12 SER A 232  ASN A 234  TRP B   5  TYR B   6                    
SITE     2 AD1 12 LMG B 624  TRP D 266  PHE D 269  PHE D 273                    
SITE     3 AD1 12 PL9 D 407  GLU L  11  ASN L  13  SER L  16                    
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 14 ASN A 267  SER A 270  PHE A 273  PHE A 274                    
SITE     2 AD4 14 TRP A 278  LHG A 409  TRP C  36  DGD C 516                    
SITE     3 AD4 14 DGD C 517  LHG C 519  PHE D 232  ARG D 233                    
SITE     4 AD4 14 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 VAL A  30  THR A  45  BCR A 407  PHO D 401                    
SITE     3 AD5 13 TRP b 113  TYR b 117  CLA b 609  CLA b 619                    
SITE     4 AD5 13 BCR b 623                                                     
SITE     1 AD6  9 LEU A  72  LEU A 102  ASP A 103  ARG D 304                    
SITE     2 AD6  9 GLY O 138  ALA b  43  TRP b  75  SER b  76                    
SITE     3 AD6  9 LEU b  98                                                     
SITE     1 AD7  9 TRP B 185  PRO B 187  PHE B 190  ILE B 207                    
SITE     2 AD7  9 VAL B 208  PHE H  41  ILE H  44  CLA H 101                    
SITE     3 AD7  9 BCR H 102                                                     
SITE     1 AD8 20 ARG B  68  LEU B  69  ALA B 146  LEU B 149                    
SITE     2 AD8 20 CYS B 150  PHE B 153  VAL B 198  HIS B 201                    
SITE     3 AD8 20 HIS B 202  PHE B 247  ALA B 248  VAL B 252                    
SITE     4 AD8 20 THR B 262  CLA B 603  CLA B 604  CLA B 605                    
SITE     5 AD8 20 CLA B 608  PHE H  38  LEU H  42  CLA H 101                    
SITE     1 AD9 20 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 AD9 20 VAL B 245  ALA B 248  ALA B 249  VAL B 252                    
SITE     3 AD9 20 PHE B 451  HIS B 455  PHE B 458  ALA B 459                    
SITE     4 AD9 20 PHE B 462  CLA B 602  CLA B 604  CLA B 606                    
SITE     5 AD9 20 CLA B 610  CLA B 611  CLA B 612  CLA B 614                    
SITE     1 AE1 18 THR B  27  VAL B  30  ALA B  31  TRP B  33                    
SITE     2 AE1 18 ALA B  34  VAL B  62  PHE B  65  MET B  66                    
SITE     3 AE1 18 ARG B  68  LEU B  69  HIS B 100  LEU B 103                    
SITE     4 AE1 18 ALA B 205  CLA B 602  CLA B 603  CLA B 605                    
SITE     5 AE1 18 CLA B 609  CLA B 611                                          
SITE     1 AE2 17 LEU B  69  TRP B  91  ALA B  99  LEU B 103                    
SITE     2 AE2 17 LEU B 106  GLY B 152  PHE B 153  PHE B 156                    
SITE     3 AE2 17 HIS B 157  PHE B 162  PRO B 164  CLA B 602                    
SITE     4 AE2 17 CLA B 604  CLA B 615  BCR B 619  LMT B 622                    
SITE     5 AE2 17 SQD a 401                                                     
SITE     1 AE3 20 TRP B  33  MET B  37  TYR B  40  GLN B  58                    
SITE     2 AE3 20 GLY B  59  PHE B  61  THR B 327  GLY B 328                    
SITE     3 AE3 20 PRO B 329  TRP B 450  ALA B 454  CLA B 603                    
SITE     4 AE3 20 BCR B 616  BCR B 617  BCR B 618  LMG B 621                    
SITE     5 AE3 20 LMG B 624  MET D 281  LEU L  27  PHE M  14                    
SITE     1 AE4 17 THR B 236  SER B 239  ALA B 243  PHE B 246                    
SITE     2 AE4 17 PHE B 247  PHE B 463  HIS B 466  LEU B 474                    
SITE     3 AE4 17 CLA B 608  CLA B 609  PHE D 120  ILE D 123                    
SITE     4 AE4 17 MET D 126  LEU D 127  PHE D 130  SQD D 403                    
SITE     5 AE4 17 LEU H  43                                                     
SITE     1 AE5 16 PHE B 139  ALA B 212  PHE B 215  HIS B 216                    
SITE     2 AE5 16 PRO B 221  PRO B 222  LEU B 229  CLA B 602                    
SITE     3 AE5 16 CLA B 607  CLA B 609  THR H  27  THR H  28                    
SITE     4 AE5 16 MET H  31  PHE H  34  MET H  35  BCR H 102                    
SITE     1 AE6 12 PHE B 139  HIS B 142  LEU B 143  ALA B 146                    
SITE     2 AE6 12 VAL B 237  SER B 240  CLA B 604  CLA B 607                    
SITE     3 AE6 12 CLA B 608  CLA B 611  CLA B 614  BCR H 102                    
SITE     1 AE7 17 TRP B   5  TYR B   6  ARG B   7  VAL B   8                    
SITE     2 AE7 17 HIS B   9  ILE B 242  LEU B 461  PHE B 462                    
SITE     3 AE7 17 GLY B 465  TRP B 468  HIS B 469  ARG B 472                    
SITE     4 AE7 17 CLA B 603  CLA B 611  CLA B 612  CLA B 613                    
SITE     5 AE7 17 LMG B 624                                                     
SITE     1 AE8 17 HIS B   9  LEU B  19  HIS B  23  HIS B  26                    
SITE     2 AE8 17 THR B  27  ILE B 234  VAL B 237  LEU B 238                    
SITE     3 AE8 17 SER B 241  VAL B 245  CLA B 603  CLA B 604                    
SITE     4 AE8 17 CLA B 609  CLA B 610  CLA B 612  CLA B 613                    
SITE     5 AE8 17 CLA B 614                                                     
SITE     1 AE9 10 HIS B   9  HIS B  26  VAL B  30  PHE B 462                    
SITE     2 AE9 10 CLA B 603  CLA B 610  CLA B 611  CLA B 613                    
SITE     3 AE9 10 BCR B 618  LMG B 624                                          
SITE     1 AF1 14 VAL B   8  HIS B   9  VAL B  11  LEU B  12                    
SITE     2 AF1 14 LEU B  29  TRP B 115  CLA B 610  CLA B 611                    
SITE     3 AF1 14 CLA B 612  BCR B 616  SQD B 626  VAL L  10                    
SITE     4 AF1 14 LMG m 101  PHE t   8                                          
SITE     1 AF2 12 HIS B  23  MET B 138  ILE B 141  HIS B 142                    
SITE     2 AF2 12 LEU B 145  CLA B 603  CLA B 609  CLA B 611                    
SITE     3 AF2 12 CLA B 615  BCR B 619  LEU H  14  ASN H  15                    
SITE     1 AF3  9 LEU B  24  ALA B 110  TRP B 113  HIS B 114                    
SITE     2 AF3  9 CLA B 605  CLA B 614  THR H   5  LEU H   7                    
SITE     3 AF3  9 SQD a 401                                                     
SITE     1 AF4 10 MET B  25  LEU B  29  TRP B 115  CLA B 606                    
SITE     2 AF4 10 CLA B 613  BCR B 617  BCR B 618  SQD B 626                    
SITE     3 AF4 10 LEU M  13  PHE t  19                                          
SITE     1 AF5 12 TRP B  33  SER B  36  MET B  37  CLA B 606                    
SITE     2 AF5 12 BCR B 616  BCR B 618  LMT B 628  ILE t   4                    
SITE     3 AF5 12 PHE t   8  ALA t  11  PHE t  17  ILE t  21                    
SITE     1 AF6  9 LEU B  29  GLY B  32  TRP B  33  GLY B 105                    
SITE     2 AF6  9 CLA B 606  CLA B 612  BCR B 616  BCR B 617                    
SITE     3 AF6  9 DGD B 625                                                     
SITE     1 AF7  8 LEU B 109  CYS B 112  TYR B 117  CLA B 605                    
SITE     2 AF7  8 CLA B 614  SQD a 401  PHE t  18  PHE t  22                    
SITE     1 AF8 13 TYR B 193  PHE B 250  TYR B 258  TYR B 273                    
SITE     2 AF8 13 SER B 277  HIS D  87  LEU D 162  TYR H  49                    
SITE     3 AF8 13 ASN H  50  VAL H  60  SER H  61  TRP H  62                    
SITE     4 AF8 13 CLA H 101                                                     
SITE     1 AF9 10 THR B 327  GLY B 328  PRO B 329  LYS B 332                    
SITE     2 AF9 10 CLA B 606  ILE D 284  PHE L  35  ASN M   4                    
SITE     3 AF9 10 LEU M   6  LMT M 103                                          
SITE     1 AG1  4 TRP B  91  PHE B 162  CLA B 605  DGD B 625                    
SITE     1 AG2  7 ARG B 224  LYS B 227  ASP D  16  ASP D  19                    
SITE     2 AG2  7 SQD D 403  ALA H  32  MET H  35                               
SITE     1 AG3 14 ASN A 234  LMG A 410  TRP B   5  TYR B   6                    
SITE     2 AG3 14 ARG B   7  PHE B 464  TRP B 468  CLA B 606                    
SITE     3 AG3 14 CLA B 610  CLA B 612  ARG D 139  TYR D 141                    
SITE     4 AG3 14 PHE D 269  PHE D 273                                          
SITE     1 AG4  9 TRP B  75  ASP B  87  GLY B  89  PHE B  90                    
SITE     2 AG4  9 BCR B 618  LMT B 622  LMT B 627  ILE a  46                    
SITE     3 AG4  9 LMG i 101                                                     
SITE     1 AG5 13 ARG B  18  LEU B  29  SER B 104  PHE B 108                    
SITE     2 AG5 13 TRP B 115  CLA B 613  BCR B 616  ASN L   4                    
SITE     3 AG5 13 ARG l  14  TYR l  18  TYR m  26  PHE t  19                    
SITE     4 AG5 13 PHE t  23                                                     
SITE     1 AG6  8 GLY B  85  ASP B  87  DGD B 625  ALA a 100                    
SITE     2 AG6  8 BCR a 410  MET i   1  LMG i 101  LYS o  95                    
SITE     1 AG7  4 ALA B  43  LEU B 437  BCR B 617  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  PHE C 289  VAL C 296                    
SITE     4 AG8 17 TYR C 297  CLA C 502  CLA C 503  CLA C 506                    
SITE     5 AG8 17 BCR C 514                                                     
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 518                                          
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 514  PHE I  23                    
SITE     1 AH3 13 LEU C 165  LEU C 213  ILE C 243  GLY C 247                    
SITE     2 AH3 13 TRP C 250  HIS C 251  THR C 255  PRO C 256                    
SITE     3 AH3 13 PHE C 257  TRP C 259  ALA C 260  PHE C 264                    
SITE     4 AH3 13 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 514                               
SITE     1 AH5 18 LHG A 409  TRP C  36  ALA C  37  ASN C  39                    
SITE     2 AH5 18 ALA C  40  GLU C 269  LEU C 276  PHE C 436                    
SITE     3 AH5 18 PHE C 437  GLY C 440  TRP C 443  HIS C 444                    
SITE     4 AH5 18 ARG C 447  CLA C 508  CLA C 509  DGD C 516                    
SITE     5 AH5 18 CLA C 520  VAL K  30                                          
SITE     1 AH6 18 ASN C  39  LEU C  42  LEU C  49  ALA C  52                    
SITE     2 AH6 18 HIS C  53  HIS C  56  TYR C 149  GLY C 268                    
SITE     3 AH6 18 TYR C 271  LEU C 272  SER C 275  LEU C 279                    
SITE     4 AH6 18 CLA C 502  CLA C 506  CLA C 507  CLA C 509                    
SITE     5 AH6 18 CLA C 510  CLA C 511                                          
SITE     1 AH7 15 ASN C  39  HIS C  56  LEU C  59  LEU C 279                    
SITE     2 AH7 15 PHE C 436  PHE C 437  CLA C 502  CLA C 503                    
SITE     3 AH7 15 CLA C 507  CLA C 508  CLA C 510  CLA C 520                    
SITE     4 AH7 15 PRO K  29  VAL K  30  LEU K  33                               
SITE     1 AH8 21 GLN C  28  TRP C  35  GLY C  38  ASN C  39                    
SITE     2 AH8 21 ARG C  41  LEU C  42  LYS C  48  ALA C  52                    
SITE     3 AH8 21 PHE C 127  ILE C 134  CLA C 508  CLA C 509                    
SITE     4 AH8 21 BCR C 513  PHE K  32  TRP K  39  GLN K  40                    
SITE     5 AH8 21 MET Z  19  VAL Z  20  PRO Z  24  ILE y  35                    
SITE     6 AH8 21 LEU y  46                                                     
SITE     1 AH9 12 HIS C  53  ALA C  57  PHE C 147  PHE C 163                    
SITE     2 AH9 12 HIS C 164  VAL C 167  ILE C 170  LEU C 174                    
SITE     3 AH9 12 CLA C 503  CLA C 508  CLA C 512  BCR C 521                    
SITE     1 AI1  9 LEU C  50  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 521                                                     
SITE     1 AI2 11 ALA C  55  LEU C  59  VAL C 116  LEU C 119                    
SITE     2 AI2 11 SER C 122  ALA C 123  CLA C 510  BCR C 521                    
SITE     3 AI2 11 PHE K  32  VAL Z  13  BCR y 101                               
SITE     1 AI3 11 ILE C 209  TYR C 212  LEU C 213  VAL C 227                    
SITE     2 AI3 11 ASP C 232  VAL C 233  ILE C 240  PHE C 264                    
SITE     3 AI3 11 CLA C 501  CLA C 504  CLA C 506                               
SITE     1 AI4 16 LEU A  91  PHE A 155  ILE A 163  PRO C 217                    
SITE     2 AI4 16 PHE C 218  GLY C 219  GLY C 220  VAL C 225                    
SITE     3 AI4 16 SER C 226  PHE C 284  CYS C 288  PHE C 292                    
SITE     4 AI4 16 ASN C 294  PRO C 307  PHE C 361  ARG C 362                    
SITE     1 AI5 20 PHE A 197  SQD A 413  TYR C  82  GLU C  83                    
SITE     2 AI5 20 GLN C  84  GLY C  85  LEU C 404  SER C 406                    
SITE     3 AI5 20 ASN C 418  PHE C 419  VAL C 420  TRP C 425                    
SITE     4 AI5 20 SER C 429  CLA C 507  DGD C 517  LHG C 519                    
SITE     5 AI5 20 CLA C 520  LMG C 522  TYR J  33  BCR J 102                    
SITE     1 AI6 20 LEU A 200  TRP A 278  PHE A 300  ASN A 301                    
SITE     2 AI6 20 SER A 305  SQD A 413  ASN C 405  VAL C 407                    
SITE     3 AI6 20 ASN C 415  SER C 416  ASN C 418  DGD C 516                    
SITE     4 AI6 20 CLA C 520  PHE J  29  ALA J  32  TYR J  33                    
SITE     5 AI6 20 GLY J  37  SER J  38  SER J  39  GLN V  60                    
SITE     1 AI7  7 TRP C  97  PHE C 109  VAL C 113  VAL C 117                    
SITE     2 AI7  7 HIS C 118  CLA C 503  PHE Z  59                               
SITE     1 AI8  8 TYR A 262  ASN A 266  SQD A 413  TRP C  35                    
SITE     2 AI8  8 DGD C 516  LMG E 101  BCR J 102  PHE K  45                    
SITE     1 AI9 17 PHE A 285  LHG A 409  TRP C  63  MET C  67                    
SITE     2 AI9 17 PHE C  70  GLN C  84  GLY C  85  ILE C  87                    
SITE     3 AI9 17 TRP C 425  SER C 429  CLA C 507  CLA C 509                    
SITE     4 AI9 17 DGD C 516  DGD C 517  LMG C 522  PRO K  26                    
SITE     5 AI9 17 VAL K  30                                                     
SITE     1 AJ1 11 PHE C 112  VAL C 116  SER C 121  VAL C 124                    
SITE     2 AJ1 11 CLA C 511  CLA C 512  BCR C 513  TYR K  15                    
SITE     3 AJ1 11 VAL Z  54  GLY Z  55  ASN Z  58                               
SITE     1 AJ2  7 HIS C  74  DGD C 516  CLA C 520  BCR J 102                    
SITE     2 AJ2  7 ASP K  23  VAL K  27  ILE y  25                               
SITE     1 AJ3 19 LEU A  41  ALA A  44  THR A  45  ILE A 115                    
SITE     2 AJ3 19 TYR A 126  GLN A 130  ALA A 146  TYR A 147                    
SITE     3 AJ3 19 VAL A 283  CLA A 402  CLA A 403  SQD A 414                    
SITE     4 AJ3 19 LEU D 205  ALA D 208  LEU D 209  ALA D 212                    
SITE     5 AJ3 19 ILE D 213  TRP D 253  PHE D 257                               
SITE     1 AJ4 20 PHE A 206  ALA A 209  LEU A 210  MET A 214                    
SITE     2 AJ4 20 LEU A 258  CLA A 404  ALA D  41  LEU D  45                    
SITE     3 AJ4 20 TRP D  48  GLY D 118  LEU D 122  PHE D 125                    
SITE     4 AJ4 20 GLN D 129  ASN D 142  PHE D 146  PHE D 153                    
SITE     5 AJ4 20 PHE D 173  PRO D 275  LEU D 279  CLA D 405                    
SITE     1 AJ5 10 LYS B 227  ALA B 228  ARG B 230  LEU B 474                    
SITE     2 AJ5 10 CLA B 607  LMT B 623  LYS D  23  TRP D  32                    
SITE     3 AJ5 10 ARG D 134  LEU D 135                                          
SITE     1 AJ6  8 HIS A 215  GLU A 244  TYR A 246  HIS A 272                    
SITE     2 AJ6  8 FE2 A 401  TYR D 244  LYS D 264  HIS D 268                    
SITE     1 AJ7 22 PHE A 206  CLA A 402  CLA A 403  CLA A 404                    
SITE     2 AJ7 22 LEU D 122  VAL D 152  PHE D 153  VAL D 156                    
SITE     3 AJ7 22 LEU D 182  PHE D 185  GLN D 186  TRP D 191                    
SITE     4 AJ7 22 THR D 192  HIS D 197  GLY D 200  VAL D 201                    
SITE     5 AJ7 22 VAL D 204  LEU D 279  SER D 282  ALA D 283                    
SITE     6 AJ7 22 VAL D 286  PHO D 402                                          
SITE     1 AJ8 14 LEU D  43  LEU D  89  LEU D  90  LEU D  91                    
SITE     2 AJ8 14 LEU D  92  TRP D  93  THR D 112  PHE D 113                    
SITE     3 AJ8 14 HIS D 117  PHE D 120  LMT D 410  GLY X  22                    
SITE     4 AJ8 14 LEU X  23  GLY X  26                                          
SITE     1 AJ9 18 PHE A  52  ILE A  77  CLA A 403  LMG A 410                    
SITE     2 AJ9 18 MET D 199  LEU D 209  HIS D 214  THR D 217                    
SITE     3 AJ9 18 TRP D 253  ALA D 260  PHE D 261  LEU D 267                    
SITE     4 AJ9 18 PHE D 270  PHE D 273  VAL D 274  LMG D 408                    
SITE     5 AJ9 18 VAL L  26  PHE T  10                                          
SITE     1 AK1 13 PHE D 257  ILE D 259  ALA D 260  PHE D 261                    
SITE     2 AK1 13 SER D 262  ASN D 263  TRP D 266  PL9 D 407                    
SITE     3 AK1 13 THR L  15  TYR L  18  LEU L  19  PHE T  17                    
SITE     4 AK1 13 ALA T  20                                                     
SITE     1 AK2  6 ASP D 100  PHE D 101  THR D 102  LMT D 410                    
SITE     2 AK2  6 ASP E  45  VAL E  46                                          
SITE     1 AK3  8 LEU D  92  TRP D  93  GLY D  99  CLA D 406                    
SITE     2 AK3  8 DGD D 409  ILE X  21  SER X  25  GLY X  26                    
SITE     1 AK4 11 TYR D  42  GLY D  47  LEU D  49  THR D  50                    
SITE     2 AK4 11 PHE D 101  LMG D 412  PRO F  29  PHE F  33                    
SITE     3 AK4 11 VAL J  21  VAL J  25  PL9 J 101                               
SITE     1 AK5 13 TYR D  67  GLY D  70  CYS D  71  ASN D  72                    
SITE     2 AK5 13 PHE D  73  BCR D 411  ILE F  37  MET F  40                    
SITE     3 AK5 13 GLN F  41  PHE J  28  GLY J  31  ALA J  32                    
SITE     4 AK5 13 GLY J  37                                                     
SITE     1 AK6  7 TYR A 262  LHG C 519  PHE D  27  PRO E   9                    
SITE     2 AK6  7 PHE E  10  SER E  11  PL9 J 101                               
SITE     1 AK7 15 ARG E   8  PHE E  10  ILE E  13  ARG E  18                    
SITE     2 AK7 15 TYR E  19  HIS E  23  THR E  26  LEU E  30                    
SITE     3 AK7 15 ILE F  15  ARG F  19  TRP F  20  VAL F  23                    
SITE     4 AK7 15 HIS F  24  ALA F  27  ILE F  31                               
SITE     1 AK8  9 TRP D  21  ARG D  24  ARG D  26  GLU E   7                    
SITE     2 AK8  9 PHE F  16  THR F  17  VAL F  18  THR X  33                    
SITE     3 AK8  9 ASP X  44                                                     
SITE     1 AK9 16 GLU B 184  GLY B 189  GLY B 197  HIS B 201                    
SITE     2 AK9 16 ALA B 204  ALA B 205  VAL B 208  PHE B 247                    
SITE     3 AK9 16 CLA B 601  CLA B 602  DGD B 620  VAL D 154                    
SITE     4 AK9 16 PHE H  38  PHE H  41  ILE H  45  TYR H  49                    
SITE     1 AL1 10 CLA B 601  CLA B 608  CLA B 609  PHE H  34                    
SITE     2 AL1 10 MET H  35  LEU H  37  PHE H  38  PHE H  41                    
SITE     3 AL1 10 THR X  11  LEU X  16                                          
SITE     1 AL2  6 MET I   1  THR I   3  LEU I   4  LMT I 102                    
SITE     2 AL2  6 DGD b 601  LMT b 603                                          
SITE     1 AL3  4 THR I   3  ILE I   6  ILE I  10  LMG I 101                    
SITE     1 AL4  4 PL9 A 406  BCR D 411  LMG E 101  VAL J  16                    
SITE     1 AL5  6 SQD A 413  DGD C 516  LHG C 519  LMG C 522                    
SITE     2 AL5  6 PHE J  29  TYR J  33                                          
SITE     1 AL6  2 ASP K  19  ASP K  23                                          
SITE     1 AL7  9 GLU M  30  SER M  31  SQD b 602  CLA b 617                    
SITE     2 AL7  9 PRO l   9  VAL l  10  ILE m  24  GLN m  28                    
SITE     3 AL7  9 GLN m  32                                                     
SITE     1 AL8  7 MET M   1  GLU M   2  MET T   1  ILE T   4                    
SITE     2 AL8  7 TYR b  40  LMG b 625  GLN m   5                               
SITE     1 AL9  6 TYR B  40  LMG B 621  GLN M   5  MET m   1                    
SITE     2 AL9  6 GLU m   2  MET t   1                                          
SITE     1 AM1  2 GLU O 140  HIS O 257                                          
SITE     1 AM2 14 ALA V  62  CYS V  63  CYS V  66  HIS V  67                    
SITE     2 AM2 14 THR V  74  LEU V  78  ASP V  79  THR V  84                    
SITE     3 AM2 14 LEU V  85  TYR V 101  MET V 102  TYR V 108                    
SITE     4 AM2 14 HIS V 118  PRO V 119                                          
SITE     1 AM3 14 BCR C 513  ALA J  14  THR J  15  MET J  19                    
SITE     2 AM3 14 ILE K  28  LEU K  31  ALA K  34  PHE K  37                    
SITE     3 AM3 14 VAL K  38  VAL Z  13  PHE Z  17  ILE y  28                    
SITE     4 AM3 14 GLY y  29  GLY y  32                                          
SITE     1 AM4 13 TRP B 113  TYR B 117  CLA B 605  CLA B 615                    
SITE     2 AM4 13 BCR B 619  TRP a  20  ASN a  26  ARG a  27                    
SITE     3 AM4 13 LEU a  28  VAL a  30  THR a  45  BCR a 410                    
SITE     4 AM4 13 PHO d 401                                                     
SITE     1 AM5  8 ALA B  43  TRP B  75  SER B  76  LEU B  98                    
SITE     2 AM5  8 LEU a  72  ASP a 103  ARG d 304  GLY o 138                    
SITE     1 AM6  5 HIS a 215  HIS a 272  HIS d 214  HIS d 268                    
SITE     2 AM6  5 BCT d 403                                                     
SITE     1 AM7 24 PHE a 119  TYR a 147  PRO a 150  SER a 153                    
SITE     2 AM7 24 VAL a 157  MET a 183  PHE a 186  GLN a 187                    
SITE     3 AM7 24 LEU a 193  HIS a 198  GLY a 201  VAL a 205                    
SITE     4 AM7 24 PHE a 206  VAL a 283  THR a 286  ILE a 290                    
SITE     5 AM7 24 CLA a 405  CLA a 406  LEU d 182  LEU d 205                    
SITE     6 AM7 24 PHO d 401  CLA d 404  LMG d 407  PHE t  17                    
SITE     1 AM8 14 THR a  45  VAL a 157  PHE a 158  MET a 172                    
SITE     2 AM8 14 ILE a 176  THR a 179  PHE a 180  MET a 183                    
SITE     3 AM8 14 CLA a 404  MET d 198  VAL d 201  PHO d 401                    
SITE     4 AM8 14 CLA d 404  PL9 d 406                                          
SITE     1 AM9 13 GLN a 199  VAL a 202  ALA a 203  TRP a 278                    
SITE     2 AM9 13 CLA a 404  PHO a 407  PHE d 157  VAL d 175                    
SITE     3 AM9 13 ILE d 178  PHE d 179  PHE d 181  LEU d 182                    
SITE     4 AM9 13 CLA d 404                                                     
SITE     1 AN1 21 PHE a 206  ALA a 209  LEU a 210  MET a 214                    
SITE     2 AN1 21 LEU a 258  CLA a 406  ALA d  41  TRP d  48                    
SITE     3 AN1 21 GLY d 118  LEU d 122  PHE d 125  GLN d 129                    
SITE     4 AN1 21 ASN d 142  ALA d 145  PHE d 146  ALA d 148                    
SITE     5 AN1 21 PHE d 153  PHE d 173  PRO d 275  LEU d 279                    
SITE     6 AN1 21 CLA d 404                                                     
SITE     1 AN2 14 ILE a  36  PRO a  39  THR a  40  PHE a  93                    
SITE     2 AN2 14 PRO a  95  ILE a  96  TRP a  97  LEU a 114                    
SITE     3 AN2 14 HIS a 118  LEU a 121  BCR a 410  DGD a 411                    
SITE     4 AN2 14 TYR i   9  PHE i  15                                          
SITE     1 AN3 13 HIS a 215  LEU a 218  HIS a 252  PHE a 255                    
SITE     2 AN3 13 SER a 264  PHE a 265  LEU a 271  PHE a 274                    
SITE     3 AN3 13 PHE d  38  ALA d  41  TYR d  42  THR f  25                    
SITE     4 AN3 13 PL9 j 101                                                     
SITE     1 AN4  8 LMT B 627  LEU a  42  ALA a  43  TRP a 105                    
SITE     2 AN4  8 LEU a 106  SQD a 401  CLA a 408  PHE i  15                    
SITE     1 AN5 13 PHE a  93  TRP a  97  GLU a  98  CLA a 408                    
SITE     2 AN5 13 LEU c 214  LYS c 215  SER c 216  PRO c 217                    
SITE     3 AN5 13 TRP c 223  PHE c 284  LYS i   5  TYR i   9                    
SITE     4 AN5 13 GLY o  38                                                     
SITE     1 AN6 15 ARG a 140  TRP a 142  PHE a 273  SQD a 415                    
SITE     2 AN6 15 TRP c  36  PHE c 436  TRP c 443  ARG c 447                    
SITE     3 AN6 15 CLA c 507  CLA c 520  ASN d 220  ALA d 229                    
SITE     4 AN6 15 SER d 230  THR d 231  PHE d 232                               
SITE     1 AN7 13 SER a 232  ASN a 234  TRP b   5  TYR b   6                    
SITE     2 AN7 13 LMG b 628  TRP d 266  PHE d 269  PHE d 273                    
SITE     3 AN7 13 PL9 d 406  GLU l  11  ASN l  13  SER l  16                    
SITE     4 AN7 13 VAL l  26                                                     
SITE     1 AN8  9 ASP a 170  GLU a 189  HIS a 332  GLU a 333                    
SITE     2 AN8  9 HIS a 337  ASP a 342  ALA a 344  GLU c 354                    
SITE     3 AN8  9 ARG c 357                                                     
SITE     1 AN9 14 ASN a 267  SER a 270  PHE a 273  PHE a 274                    
SITE     2 AN9 14 TRP a 278  LHG a 412  TRP c  36  DGD c 516                    
SITE     3 AN9 14 DGD c 517  LHG c 519  PHE d 232  ARG d 233                    
SITE     4 AN9 14 BCR j 102  PHE k  37                                          
SITE     1 AO1  3 ASN a 181  GLU a 333  LYS d 317                               
SITE     1 AO2  8 ILE A  46  LMG I 101  TRP b  75  ASP b  87                    
SITE     2 AO2  8 GLY b  89  PHE b  90  LMT b 603  LMT b 626                    
SITE     1 AO3 13 ARG L  14  TYR L  18  TYR M  26  LMG M 101                    
SITE     2 AO3 13 PHE T  19  PHE T  23  ARG b  18  LEU b  29                    
SITE     3 AO3 13 SER b 104  TRP b 115  CLA b 617  BCR b 620                    
SITE     4 AO3 13 ASN l   4                                                     
SITE     1 AO4  7 BCR A 407  MET I   1  LMG I 101  LYS O  95                    
SITE     2 AO4  7 GLY b  85  ASP b  87  DGD b 601                               
SITE     1 AO5  4 VAL T   7  ALA b  43  LEU b 437  BCR b 621                    
SITE     1 AO6  8 TRP b 185  PRO b 187  PHE b 190  ILE b 207                    
SITE     2 AO6  8 PHE h  41  ILE h  44  CLA h 101  BCR x 101                    
SITE     1 AO7 19 ARG b  68  LEU b  69  ALA b 146  LEU b 149                    
SITE     2 AO7 19 CYS b 150  PHE b 153  VAL b 198  HIS b 201                    
SITE     3 AO7 19 HIS b 202  PHE b 247  ALA b 248  VAL b 252                    
SITE     4 AO7 19 THR b 262  CLA b 607  CLA b 608  CLA b 609                    
SITE     5 AO7 19 CLA b 612  PHE h  38  CLA h 101                               
SITE     1 AO8 20 TRP b  33  PHE b  61  PHE b  65  ARG b  68                    
SITE     2 AO8 20 VAL b 245  ALA b 248  ALA b 249  VAL b 252                    
SITE     3 AO8 20 PHE b 451  HIS b 455  PHE b 458  ALA b 459                    
SITE     4 AO8 20 PHE b 462  CLA b 606  CLA b 608  CLA b 610                    
SITE     5 AO8 20 CLA b 614  CLA b 615  CLA b 616  CLA b 618                    
SITE     1 AO9 20 THR b  27  VAL b  30  ALA b  31  TRP b  33                    
SITE     2 AO9 20 ALA b  34  VAL b  62  PHE b  65  MET b  66                    
SITE     3 AO9 20 ARG b  68  LEU b  69  VAL b  96  HIS b 100                    
SITE     4 AO9 20 LEU b 103  ALA b 205  CLA b 606  CLA b 607                    
SITE     5 AO9 20 CLA b 609  CLA b 612  CLA b 613  CLA b 615                    
SITE     1 AP1 16 SQD A 414  LEU b  69  TRP b  91  ALA b  99                    
SITE     2 AP1 16 LEU b 103  LEU b 106  GLY b 152  PHE b 153                    
SITE     3 AP1 16 PHE b 156  HIS b 157  PHE b 162  PRO b 164                    
SITE     4 AP1 16 CLA b 606  CLA b 608  BCR b 623  LMT b 626                    
SITE     1 AP2 18 TRP b  33  TYR b  40  GLN b  58  GLY b  59                    
SITE     2 AP2 18 PHE b  61  THR b 327  GLY b 328  PRO b 329                    
SITE     3 AP2 18 TRP b 450  ALA b 454  CLA b 607  BCR b 620                    
SITE     4 AP2 18 BCR b 621  BCR b 622  LMG b 625  LMG b 628                    
SITE     5 AP2 18 MET d 281  LEU l  27                                          
SITE     1 AP3 15 THR b 236  SER b 239  ALA b 243  PHE b 246                    
SITE     2 AP3 15 PHE b 247  HIS b 466  LEU b 474  CLA b 612                    
SITE     3 AP3 15 CLA b 613  PHE d 120  ILE d 123  MET d 126                    
SITE     4 AP3 15 LEU d 127  PHE d 130  SQD d 402                               
SITE     1 AP4 17 PHE b 139  ALA b 212  PHE b 215  HIS b 216                    
SITE     2 AP4 17 PRO b 221  PRO b 222  LEU b 229  CLA b 606                    
SITE     3 AP4 17 CLA b 608  CLA b 611  CLA b 613  THR h  27                    
SITE     4 AP4 17 THR h  28  MET h  31  PHE h  34  MET h  35                    
SITE     5 AP4 17 BCR x 101                                                     
SITE     1 AP5 13 LEU b 135  PHE b 139  HIS b 142  LEU b 143                    
SITE     2 AP5 13 THR b 236  VAL b 237  SER b 240  CLA b 608                    
SITE     3 AP5 13 CLA b 611  CLA b 612  CLA b 615  CLA b 618                    
SITE     4 AP5 13 BCR x 101                                                     
SITE     1 AP6 18 TRP b   5  TYR b   6  ARG b   7  VAL b   8                    
SITE     2 AP6 18 HIS b   9  THR b  10  ILE b 242  LEU b 461                    
SITE     3 AP6 18 PHE b 462  GLY b 465  TRP b 468  HIS b 469                    
SITE     4 AP6 18 ARG b 472  CLA b 607  CLA b 615  CLA b 616                    
SITE     5 AP6 18 CLA b 617  LMG b 628                                          
SITE     1 AP7 17 HIS b   9  LEU b  19  HIS b  23  HIS b  26                    
SITE     2 AP7 17 THR b  27  ILE b 234  VAL b 237  LEU b 238                    
SITE     3 AP7 17 SER b 241  VAL b 245  CLA b 607  CLA b 608                    
SITE     4 AP7 17 CLA b 613  CLA b 614  CLA b 616  CLA b 617                    
SITE     5 AP7 17 CLA b 618                                                     
SITE     1 AP8  8 HIS b   9  HIS b  26  PHE b 462  CLA b 607                    
SITE     2 AP8  8 CLA b 614  CLA b 615  CLA b 617  LMG b 628                    
SITE     1 AP9 12 LMG M 101  PHE T   8  VAL b   8  HIS b   9                    
SITE     2 AP9 12 VAL b  11  TRP b 115  SQD b 602  CLA b 614                    
SITE     3 AP9 12 CLA b 615  CLA b 616  BCR b 620  VAL l  10                    
SITE     1 AQ1 11 HIS b  23  MET b 138  ILE b 141  HIS b 142                    
SITE     2 AQ1 11 LEU b 145  CLA b 607  CLA b 613  CLA b 615                    
SITE     3 AQ1 11 CLA b 619  BCR b 623  LEU h  14                               
SITE     1 AQ2  8 SQD A 414  LEU b  24  ALA b 110  TRP b 113                    
SITE     2 AQ2  8 HIS b 114  CLA b 618  THR h   5  LEU h   7                    
SITE     1 AQ3 11 PHE T  19  MET b  25  LEU b  29  TRP b 115                    
SITE     2 AQ3 11 SQD b 602  CLA b 610  CLA b 617  BCR b 621                    
SITE     3 AQ3 11 BCR b 622  ALA m  10  LEU m  13                               
SITE     1 AQ4 14 ILE T   4  PHE T   8  ALA T  11  PHE T  17                    
SITE     2 AQ4 14 PHE T  18  ILE T  21  PHE T  22  TRP b  33                    
SITE     3 AQ4 14 SER b  36  MET b  37  LMT b 604  CLA b 610                    
SITE     4 AQ4 14 BCR b 620  BCR b 622                                          
SITE     1 AQ5  6 GLY b  32  TRP b  33  GLY b 105  CLA b 610                    
SITE     2 AQ5  6 BCR b 620  BCR b 621                                          
SITE     1 AQ6  9 SQD A 414  PHE T  22  LEU b 106  LEU b 109                    
SITE     2 AQ6  9 ALA b 110  CYS b 112  TYR b 117  CLA b 609                    
SITE     3 AQ6  9 CLA b 618                                                     
SITE     1 AQ7 13 TYR b 193  PHE b 250  TYR b 258  TYR b 273                    
SITE     2 AQ7 13 SER b 277  HIS d  87  LEU d 162  TYR h  49                    
SITE     3 AQ7 13 ASN h  50  VAL h  60  SER h  61  TRP h  62                    
SITE     4 AQ7 13 CLA h 101                                                     
SITE     1 AQ8 11 LMT M 102  THR b 327  GLY b 328  PRO b 329                    
SITE     2 AQ8 11 LYS b 332  PHE b 453  CLA b 610  ILE d 284                    
SITE     3 AQ8 11 PHE l  35  ASN m   4  LEU m   6                               
SITE     1 AQ9  4 TRP b  91  PHE b 162  DGD b 601  CLA b 609                    
SITE     1 AR1  7 ARG b 224  LYS b 227  ASP d  16  ASP d  19                    
SITE     2 AR1  7 SQD d 402  ALA h  32  MET h  35                               
SITE     1 AR2 13 ASN a 234  LMG a 413  TRP b   5  TYR b   6                    
SITE     2 AR2 13 ARG b   7  PHE b 464  TRP b 468  CLA b 610                    
SITE     3 AR2 13 CLA b 614  CLA b 616  ARG d 139  TYR d 141                    
SITE     4 AR2 13 PHE d 269                                                     
SITE     1 AR3 16 LEU c  95  LEU c 168  GLY c 171  ALA c 172                    
SITE     2 AR3 16 ILE c 224  VAL c 233  HIS c 237  ILE c 240                    
SITE     3 AR3 16 MET c 282  PHE c 289  VAL c 296  TYR c 297                    
SITE     4 AR3 16 CLA c 502  CLA c 503  CLA c 506  BCR c 514                    
SITE     1 AR4 15 TRP c  63  HIS c  91  TRP c  97  LYS c 178                    
SITE     2 AR4 15 PHE c 182  LEU c 279  MET c 282  ALA c 286                    
SITE     3 AR4 15 TYR c 297  HIS c 430  LEU c 433  PHE c 437                    
SITE     4 AR4 15 CLA c 501  CLA c 503  CLA c 508                               
SITE     1 AR5 14 ILE c  60  VAL c  61  ALA c  64  THR c  68                    
SITE     2 AR5 14 LEU c  88  HIS c  91  ILE c  92  VAL c 114                    
SITE     3 AR5 14 HIS c 118  CLA c 501  CLA c 502  CLA c 509                    
SITE     4 AR5 14 CLA c 511  LMG c 518                                          
SITE     1 AR6 17 PHE a  33  MET a 127  TRP a 131  PHE c 264                    
SITE     2 AR6 17 ILE c 265  TYR c 274  GLY c 277  ALA c 278                    
SITE     3 AR6 17 MET c 281  HIS c 441  LEU c 442  ALA c 445                    
SITE     4 AR6 17 ARG c 449  CLA c 506  BCR c 514  VAL i  12                    
SITE     5 AR6 17 PHE i  23                                                     
SITE     1 AR7 13 LEU c 165  LEU c 213  ILE c 243  GLY c 247                    
SITE     2 AR7 13 TRP c 250  HIS c 251  THR c 255  PRO c 256                    
SITE     3 AR7 13 PHE c 257  TRP c 259  ALA c 260  PHE c 264                    
SITE     4 AR7 13 CLA c 506                                                     
SITE     1 AR8 13 MET c 157  LEU c 161  HIS c 164  PHE c 264                    
SITE     2 AR8 13 TRP c 266  TYR c 271  TYR c 274  SER c 275                    
SITE     3 AR8 13 LEU c 279  CLA c 501  CLA c 504  CLA c 505                    
SITE     4 AR8 13 CLA c 508                                                     
SITE     1 AR9 16 LHG a 412  TRP c  36  ALA c  37  ASN c  39                    
SITE     2 AR9 16 ALA c  40  GLU c 269  LEU c 276  PHE c 436                    
SITE     3 AR9 16 PHE c 437  GLY c 440  TRP c 443  HIS c 444                    
SITE     4 AR9 16 ARG c 447  CLA c 508  CLA c 509  DGD c 516                    
SITE     1 AS1 19 ASN c  39  LEU c  42  LEU c  49  ALA c  52                    
SITE     2 AS1 19 HIS c  53  HIS c  56  TYR c 149  TRP c 151                    
SITE     3 AS1 19 GLY c 268  TYR c 271  LEU c 272  SER c 275                    
SITE     4 AS1 19 LEU c 279  CLA c 502  CLA c 506  CLA c 507                    
SITE     5 AS1 19 CLA c 509  CLA c 510  CLA c 511                               
SITE     1 AS2 14 ASN c  39  HIS c  56  LEU c  59  LEU c 279                    
SITE     2 AS2 14 PHE c 436  PHE c 437  CLA c 503  CLA c 507                    
SITE     3 AS2 14 CLA c 508  CLA c 510  CLA c 520  PRO k  29                    
SITE     4 AS2 14 VAL k  30  LEU k  33                                          
SITE     1 AS3 21 GLN c  28  TRP c  35  GLY c  38  ASN c  39                    
SITE     2 AS3 21 ARG c  41  LEU c  42  LYS c  48  ALA c  52                    
SITE     3 AS3 21 PHE c 127  ILE c 134  CLA c 508  CLA c 509                    
SITE     4 AS3 21 BCR c 513  ILE g  35  LEU g  46  PHE k  32                    
SITE     5 AS3 21 TRP k  39  GLN k  40  MET z  19  VAL z  20                    
SITE     6 AS3 21 PRO z  24                                                     
SITE     1 AS4 12 HIS c  53  ALA c  57  PHE c 147  PHE c 163                    
SITE     2 AS4 12 HIS c 164  VAL c 167  ILE c 170  LEU c 174                    
SITE     3 AS4 12 CLA c 503  CLA c 508  CLA c 512  BCR c 521                    
SITE     1 AS5  9 LEU c  50  VAL c 124  GLY c 128  TYR c 131                    
SITE     2 AS5  9 HIS c 132  PRO c 137  PHE c 147  CLA c 511                    
SITE     3 AS5  9 BCR c 521                                                     
SITE     1 AS6 10 ALA c  55  VAL c 116  LEU c 119  SER c 122                    
SITE     2 AS6 10 ALA c 123  CLA c 510  BCR c 521  BCR g 101                    
SITE     3 AS6 10 PHE k  32  VAL z  13                                          
SITE     1 AS7 11 ILE c 209  TYR c 212  LEU c 213  VAL c 227                    
SITE     2 AS7 11 ASP c 232  VAL c 233  GLY c 236  ILE c 240                    
SITE     3 AS7 11 PHE c 264  CLA c 501  CLA c 504                               
SITE     1 AS8 16 LEU a  91  PHE a 155  ILE a 163  PRO c 217                    
SITE     2 AS8 16 PHE c 218  GLY c 219  GLY c 220  VAL c 225                    
SITE     3 AS8 16 SER c 226  PHE c 284  CYS c 288  PHE c 292                    
SITE     4 AS8 16 ASN c 294  PRO c 307  PHE c 361  ARG c 362                    
SITE     1 AS9 19 PHE a 197  SQD a 415  TYR c  82  GLU c  83                    
SITE     2 AS9 19 GLN c  84  GLY c  85  SER c 406  ASN c 418                    
SITE     3 AS9 19 PHE c 419  VAL c 420  TRP c 425  SER c 429                    
SITE     4 AS9 19 CLA c 507  DGD c 517  LHG c 519  CLA c 520                    
SITE     5 AS9 19 LMG c 522  TYR j  33  BCR j 102                               
SITE     1 AT1 22 LEU a 200  TRP a 278  PHE a 300  ASN a 301                    
SITE     2 AT1 22 SER a 305  SQD a 415  ASN c 405  SER c 406                    
SITE     3 AT1 22 VAL c 407  ASN c 415  SER c 416  ASN c 418                    
SITE     4 AT1 22 DGD c 516  CLA c 520  LMG d 410  PHE j  29                    
SITE     5 AT1 22 ALA j  32  TYR j  33  GLY j  37  SER j  38                    
SITE     6 AT1 22 SER j  39  GLN v  60                                          
SITE     1 AT2  7 TRP c  97  PHE c 109  VAL c 113  VAL c 117                    
SITE     2 AT2  7 HIS c 118  CLA c 503  PHE z  59                               
SITE     1 AT3  8 TYR a 262  ASN a 266  SQD a 415  TRP c  35                    
SITE     2 AT3  8 DGD c 516  LMG e 101  BCR j 102  PHE k  45                    
SITE     1 AT4 16 PHE a 285  LHG a 412  TRP c  63  MET c  67                    
SITE     2 AT4 16 PHE c  70  GLN c  84  GLY c  85  ILE c  87                    
SITE     3 AT4 16 TRP c 425  SER c 429  CLA c 509  DGD c 516                    
SITE     4 AT4 16 DGD c 517  LMG c 522  PRO k  26  VAL k  30                    
SITE     1 AT5 10 VAL c 116  SER c 121  VAL c 124  CLA c 511                    
SITE     2 AT5 10 CLA c 512  BCR c 513  TYR k  15  VAL z  54                    
SITE     3 AT5 10 GLY z  55  ASN z  58                                          
SITE     1 AT6  8 PHE c  70  HIS c  74  DGD c 516  CLA c 520                    
SITE     2 AT6  8 ILE g  25  BCR j 102  ASP k  23  VAL k  27                    
SITE     1 AT7 19 ALA a  44  THR a  45  ILE a 115  TYR a 126                    
SITE     2 AT7 19 GLN a 130  TYR a 147  PRO a 150  LEU a 174                    
SITE     3 AT7 19 GLY a 175  VAL a 283  SQD a 401  CLA a 404                    
SITE     4 AT7 19 CLA a 405  LEU d 205  ALA d 208  LEU d 209                    
SITE     5 AT7 19 ILE d 213  TRP d 253  PHE d 257                               
SITE     1 AT8 10 LYS b 227  ALA b 228  ARG b 230  LEU b 474                    
SITE     2 AT8 10 CLA b 611  LMT b 627  LYS d  23  TRP d  32                    
SITE     3 AT8 10 ARG d 134  LEU d 135                                          
SITE     1 AT9  8 HIS a 215  GLU a 244  TYR a 246  HIS a 272                    
SITE     2 AT9  8 FE2 a 403  TYR d 244  LYS d 264  HIS d 268                    
SITE     1 AU1 22 PHE a 206  CLA a 404  CLA a 405  CLA a 406                    
SITE     2 AU1 22 PHO a 407  TRP d  48  VAL d 152  PHE d 153                    
SITE     3 AU1 22 VAL d 156  LEU d 182  PHE d 185  GLN d 186                    
SITE     4 AU1 22 TRP d 191  THR d 192  HIS d 197  GLY d 200                    
SITE     5 AU1 22 VAL d 201  VAL d 204  LEU d 279  SER d 282                    
SITE     6 AU1 22 ALA d 283  VAL d 286                                          
SITE     1 AU2 14 LEU d  43  LEU d  89  LEU d  90  LEU d  91                    
SITE     2 AU2 14 LEU d  92  TRP d  93  THR d 112  PHE d 113                    
SITE     3 AU2 14 HIS d 117  PHE d 120  LMT d 409  GLY x  22                    
SITE     4 AU2 14 LEU x  23  GLY x  26                                          
SITE     1 AU3 14 CLA a 405  LMG a 413  MET d 199  HIS d 214                    
SITE     2 AU3 14 THR d 217  TRP d 253  ILE d 259  ALA d 260                    
SITE     3 AU3 14 PHE d 261  LEU d 267  PHE d 273  VAL d 274                    
SITE     4 AU3 14 VAL l  26  PHE t  10                                          
SITE     1 AU4 13 CLA a 404  PHE d 257  ILE d 259  ALA d 260                    
SITE     2 AU4 13 PHE d 261  SER d 262  ASN d 263  TRP d 266                    
SITE     3 AU4 13 THR l  15  TYR l  18  LEU l  19  PHE t  17                    
SITE     4 AU4 13 ALA t  20                                                     
SITE     1 AU5  6 ASP d 100  PHE d 101  THR d 102  LMT d 409                    
SITE     2 AU5  6 ASP e  45  VAL e  46                                          
SITE     1 AU6  8 LEU d  92  TRP d  93  GLY d  99  CLA d 405                    
SITE     2 AU6  8 DGD d 408  ILE x  21  SER x  25  GLY x  26                    
SITE     1 AU7 13 DGD c 517  TYR d  67  GLY d  70  ASN d  72                    
SITE     2 AU7 13 PHE d  73  ILE f  37  MET f  40  GLN f  41                    
SITE     3 AU7 13 BCR f 102  PHE j  28  GLY j  31  ALA j  32                    
SITE     4 AU7 13 GLY j  37                                                     
SITE     1 AU8  7 TYR a 262  LHG c 519  PHE d  27  PRO e   9                    
SITE     2 AU8  7 PHE e  10  SER e  11  PL9 j 101                               
SITE     1 AU9 14 ARG e   8  PHE e  10  ILE e  13  ARG e  18                    
SITE     2 AU9 14 TYR e  19  HIS e  23  THR e  26  LEU e  30                    
SITE     3 AU9 14 ILE f  15  ARG f  19  TRP f  20  HIS f  24                    
SITE     4 AU9 14 ALA f  27  ILE f  31                                          
SITE     1 AV1 12 TYR d  42  GLY d  46  GLY d  47  LEU d  49                    
SITE     2 AV1 12 THR d  50  PHE d 101  LMG d 410  PRO f  29                    
SITE     3 AV1 12 PHE f  33  VAL j  21  VAL j  25  PL9 j 101                    
SITE     1 AV2  9 TRP d  21  ARG d  24  ARG d  26  GLU e   7                    
SITE     2 AV2  9 PHE f  16  THR f  17  VAL f  18  THR x  33                    
SITE     3 AV2  9 VAL x  36                                                     
SITE     1 AV3 15 GLU b 184  GLY b 189  GLY b 197  HIS b 201                    
SITE     2 AV3 15 ALA b 204  VAL b 208  PHE b 247  CLA b 605                    
SITE     3 AV3 15 CLA b 606  DGD b 624  VAL d 154  PHE h  38                    
SITE     4 AV3 15 PHE h  41  ILE h  45  TYR h  49                               
SITE     1 AV4  6 DGD B 625  LMT B 627  MET i   1  THR i   3                    
SITE     2 AV4  6 LEU i   4  LMT i 102                                          
SITE     1 AV5  5 THR i   3  ILE i   6  THR i   7  ILE i  10                    
SITE     2 AV5  5 LMG i 101                                                     
SITE     1 AV6  3 PL9 a 409  LMG e 101  BCR f 102                               
SITE     1 AV7  8 SQD a 415  DGD c 516  LHG c 519  LMG c 522                    
SITE     2 AV7  8 BCR g 101  PHE j  29  TYR j  30  TYR j  33                    
SITE     1 AV8  2 ASP k  19  ASP k  23                                          
SITE     1 AV9  7 CLA B 613  VAL L  10  GLN M  28  GLN M  32                    
SITE     2 AV9  7 VAL m  27  GLU m  30  SER m  31                               
SITE     1 AW1  2 GLU o 140  HIS o 257                                          
SITE     1 AW2 14 ALA v  62  CYS v  63  CYS v  66  HIS v  67                    
SITE     2 AW2 14 THR v  74  LEU v  78  ASP v  79  THR v  84                    
SITE     3 AW2 14 LEU v  85  TYR v 101  MET v 102  TYR v 108                    
SITE     4 AW2 14 HIS v 118  PRO v 119                                          
SITE     1 AW3 13 BCR c 513  ILE g  28  GLY g  29  GLY g  32                    
SITE     2 AW3 13 ALA j  14  THR j  15  BCR j 102  ILE k  28                    
SITE     3 AW3 13 LEU k  31  ALA k  34  PHE k  37  VAL k  38                    
SITE     4 AW3 13 VAL z  13                                                     
SITE     1 AW4 10 CLA b 605  CLA b 612  CLA b 613  PHE h  34                    
SITE     2 AW4 10 MET h  35  LEU h  37  PHE h  38  PHE h  41                    
SITE     3 AW4 10 THR x  11  LEU x  16                                          
CRYST1  132.298  228.713  307.976  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      0.007559  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004372  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003247        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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