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Database: PDB
Entry: 5E79
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Original site: 5E79 
HEADER    PHOTOSYNTHESIS                          12-OCT-15   5E79              
TITLE     MACROMOLECULAR DIFFRACTIVE IMAGING USING IMPERFECT CRYSTALS           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM II PROTEIN D1 1;                               
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 SYNONYM: PSII D1 PROTEIN 1,PHOTOSYSTEM II Q(B) PROTEIN 1;            
COMPND   5 EC: 1.10.3.9;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PHOTOSYSTEM II CP47 REACTION CENTER PROTEIN;               
COMPND   8 CHAIN: B, b;                                                         
COMPND   9 SYNONYM: PSII 47 KDA PROTEIN,PROTEIN CP-47;                          
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;               
COMPND  12 CHAIN: C, c;                                                         
COMPND  13 SYNONYM: PSII 43 KDA PROTEIN,PROTEIN CP-43;                          
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  16 CHAIN: D, d;                                                         
COMPND  17 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM II 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;                                                     
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, y;                                                         
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 Z;                  
COMPND  75 CHAIN: Z, z;                                                         
COMPND  76 SYNONYM: PSII-Z                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE   6 ORGANISM_TAXID: 197221;                                              
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE   9 ORGANISM_TAXID: 197221;                                              
SOURCE  10 MOL_ID: 4;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  12 ORGANISM_TAXID: 197221;                                              
SOURCE  13 MOL_ID: 5;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  15 ORGANISM_TAXID: 197221;                                              
SOURCE  16 MOL_ID: 6;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  18 ORGANISM_TAXID: 197221;                                              
SOURCE  19 MOL_ID: 7;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  21 ORGANISM_TAXID: 197221;                                              
SOURCE  22 MOL_ID: 8;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  24 ORGANISM_TAXID: 197221;                                              
SOURCE  25 MOL_ID: 9;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  27 ORGANISM_TAXID: 197221;                                              
SOURCE  28 MOL_ID: 10;                                                          
SOURCE  29 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  30 ORGANISM_TAXID: 197221;                                              
SOURCE  31 MOL_ID: 11;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  33 ORGANISM_TAXID: 197221;                                              
SOURCE  34 MOL_ID: 12;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  36 ORGANISM_TAXID: 197221;                                              
SOURCE  37 MOL_ID: 13;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  39 ORGANISM_TAXID: 197221;                                              
SOURCE  40 MOL_ID: 14;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  42 ORGANISM_TAXID: 197221;                                              
SOURCE  43 MOL_ID: 15;                                                          
SOURCE  44 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  45 ORGANISM_TAXID: 197221;                                              
SOURCE  46 MOL_ID: 16;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  48 ORGANISM_TAXID: 197221;                                              
SOURCE  49 MOL_ID: 17;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  51 ORGANISM_TAXID: 197221;                                              
SOURCE  52 MOL_ID: 18;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  54 ORGANISM_TAXID: 197221;                                              
SOURCE  55 MOL_ID: 19;                                                          
SOURCE  56 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  57 ORGANISM_TAXID: 197221                                               
KEYWDS    PHOTOSYSTEM II, CONTINUOUS DIFFUSED SCATTERING, MOLECULAR TRANSFORM,  
KEYWDS   2 RESOLUTION INCREASE, PHOTOSYNTHESIS                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.AYYER,O.YEFANOV,D.OBERTHUR,S.ROY-CHOWDHURY,L.GALLI,V.MARIANI,       
AUTHOR   2 S.BASU,J.COE,C.E.CONRAD,R.FROMME,A.SCHAFFER,K.DORNER,D.JAMES,        
AUTHOR   3 C.KUPITZ,M.METZ,G.NELSON,P.L.XAVIER,K.R.BEYERLEIN,M.SCHMIDT,         
AUTHOR   4 I.SARROU,J.C.H.SPENCE,U.WEIERSTALL,T.A.WHITE,J.-H.YANG,Y.ZHAO,       
AUTHOR   5 M.LIANG,A.AQUILA,M.S.HUNTER,J.E.KOGLIN,S.BOUTET,P.FROMME,A.BARTY,    
AUTHOR   6 H.N.CHAPMAN                                                          
REVDAT   4   14-NOV-18 5E79    1       REMARK                                   
REVDAT   3   08-AUG-18 5E79    1       REMARK                                   
REVDAT   2   24-JAN-18 5E79    1       REMARK                                   
REVDAT   1   08-FEB-17 5E79    0                                                
JRNL        AUTH   K.AYYER,O.M.YEFANOV,D.OBERTHUR,S.ROY-CHOWDHURY,L.GALLI,      
JRNL        AUTH 2 V.MARIANI,S.BASU,J.COE,C.E.CONRAD,R.FROMME,A.SCHAFFER,       
JRNL        AUTH 3 K.DORNER,D.JAMES,C.KUPITZ,M.METZ,G.NELSON,P.L.XAVIER,        
JRNL        AUTH 4 K.R.BEYERLEIN,M.SCHMIDT,I.SARROU,J.C.SPENCE,U.WEIERSTALL,    
JRNL        AUTH 5 T.A.WHITE,J.H.YANG,Y.ZHAO,M.LIANG,A.AQUILA,M.S.HUNTER,       
JRNL        AUTH 6 J.S.ROBINSON,J.E.KOGLIN,S.BOUTET,P.FROMME,A.BARTY,           
JRNL        AUTH 7 H.N.CHAPMAN                                                  
JRNL        TITL   MACROMOLECULAR DIFFRACTIVE IMAGING USING IMPERFECT CRYSTALS. 
JRNL        REF    NATURE                        V. 530   202 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26863980                                                     
JRNL        DOI    10.1038/NATURE16949                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 769254                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.325                           
REMARK   3   R VALUE            (WORKING SET) : 0.324                           
REMARK   3   FREE R VALUE                     : 0.331                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 37657                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.9774 - 10.7137    0.99    23890  1428  0.2033 0.2194        
REMARK   3     2 10.7137 -  8.5692    1.00    24627   959  0.1574 0.1721        
REMARK   3     3  8.5692 -  7.5054    1.00    24246  1344  0.1689 0.1807        
REMARK   3     4  7.5054 -  6.8280    1.00    23894  1848  0.2009 0.2181        
REMARK   3     5  6.8280 -  6.3436    1.00    24308  1344  0.2106 0.2226        
REMARK   3     6  6.3436 -  5.9727    1.00    24314  1140  0.2333 0.2484        
REMARK   3     7  5.9727 -  5.6757    1.00    24475  1266  0.2382 0.2551        
REMARK   3     8  5.6757 -  5.4301    1.00    24520  1284  0.2536 0.2786        
REMARK   3     9  5.4301 -  5.2222    1.00    24351  1067  0.2606 0.2718        
REMARK   3    10  5.2222 -  5.0429    1.00    24005  1512  0.2685 0.2834        
REMARK   3    11  5.0429 -  4.8859    1.00    24550  1266  0.2779 0.2868        
REMARK   3    12  4.8859 -  4.7468    1.00    24505  1236  0.2775 0.2862        
REMARK   3    13  4.7468 -  4.6223    1.00    24033  1410  0.2976 0.3012        
REMARK   3    14  4.6223 -  4.5099    1.00    24540  1296  0.3388 0.3572        
REMARK   3    15  4.5099 -  4.4077    1.00    24477  1188  0.4817 0.5024        
REMARK   3    16  4.4077 -  4.3142    1.00    24376  1164  0.5389 0.5493        
REMARK   3    17  4.3142 -  4.2281    1.00    24475  1308  0.5187 0.5202        
REMARK   3    18  4.2281 -  4.1485    1.00    24486  1287  0.5169 0.5329        
REMARK   3    19  4.1485 -  4.0746    1.00    24277  1032  0.5188 0.5502        
REMARK   3    20  4.0746 -  4.0057    1.00    24397  1248  0.5242 0.5262        
REMARK   3    21  4.0057 -  3.9413    1.00    24434  1284  0.5230 0.5326        
REMARK   3    22  3.9413 -  3.8807    1.00    24169  1320  0.5223 0.5284        
REMARK   3    23  3.8807 -  3.8238    1.00    24795  1266  0.5210 0.5070        
REMARK   3    24  3.8238 -  3.7700    1.00    24205  1080  0.5174 0.5120        
REMARK   3    25  3.7700 -  3.7192    1.00    24567  1068  0.5212 0.5278        
REMARK   3    26  3.7192 -  3.6710    1.00    24589  1368  0.5248 0.5438        
REMARK   3    27  3.6710 -  3.6252    1.00    24314  1200  0.5300 0.5184        
REMARK   3    28  3.6252 -  3.5815    1.00    24061  1140  0.5251 0.5292        
REMARK   3    29  3.5815 -  3.5400    1.00    24870  1128  0.5254 0.5122        
REMARK   3    30  3.5400 -  3.5003    1.00    24847  1176  0.5308 0.5337        
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)     : 1.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 48.580           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.013          51966                                  
REMARK   3   ANGLE     :  1.718          71528                                  
REMARK   3   CHIRALITY :  0.651           7202                                  
REMARK   3   PLANARITY :  0.011           7760                                  
REMARK   3   DIHEDRAL  : 22.991          21482                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5E79 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214431.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.15                             
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER                
REMARK 200  BEAMLINE                       : CXI                                
REMARK 200  X-RAY GENERATOR MODEL          : SLAC LCLS BEAMLINE CXI             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.308                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : CS-PAD CXI-1                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL                           
REMARK 200  DATA SCALING SOFTWARE          : CRYSTFEL                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 769253                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 1.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.0100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.490                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3ARC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM PIPES PH 7.0, 5 MM CACL2, 10 MM   
REMARK 280  TOCOPHEROL, AND 10-17% PEG 2000, LIQUID DIFFUSION, TEMPERATURE      
REMARK 280  283.18K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 38-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,         
REMARK 350                    AND CHAINS: L, M, O, T, U, V, Y, X, Z,            
REMARK 350                    AND CHAINS: a, b, c, d, e, f, h, i, j, k,         
REMARK 350                    AND CHAINS: l, m, o, t, u, v, y, x, z             
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ILE L   24   CA   CB   CG1  CG2  CD1                             
REMARK 480     SER a  221   CA   CB   OG                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   C20  SQD L   102     C20  SQD b   601              0.29            
REMARK 500   C44  SQD L   102     C44  SQD b   601              0.37            
REMARK 500   C11  SQD B   622     C10  SQD l   101              0.39            
REMARK 500   C33  SQD L   102     C33  SQD b   601              0.44            
REMARK 500   O9   SQD B   622     O9   SQD l   101              0.47            
REMARK 500   C33  SQD B   622     C33  SQD l   101              0.47            
REMARK 500   C10  SQD L   102     C11  SQD b   601              0.51            
REMARK 500   O6   SQD B   622     C1   SQD l   101              0.54            
REMARK 500   C20  SQD B   622     C20  SQD l   101              0.54            
REMARK 500   C26  SQD L   102     C26  SQD b   601              0.54            
REMARK 500   C28  SQD L   102     C28  SQD b   601              0.59            
REMARK 500   C37  SQD L   102     C37  SQD b   601              0.59            
REMARK 500   C3   SQD B   622     C4   SQD l   101              0.59            
REMARK 500   C4   SQD L   102     C3   SQD b   601              0.60            
REMARK 500   C16  SQD B   622     C15  SQD l   101              0.61            
REMARK 500   C26  SQD B   622     C26  SQD l   101              0.61            
REMARK 500   C19  SQD B   622     C19  SQD l   101              0.66            
REMARK 500   C35  SQD B   622     C35  SQD l   101              0.67            
REMARK 500   C25  SQD L   102     C25  SQD b   601              0.68            
REMARK 500   C29  SQD L   102     C29  SQD b   601              0.68            
REMARK 500   C14  SQD L   102     C14  SQD b   601              0.69            
REMARK 500   O9   SQD L   102     O9   SQD b   601              0.70            
REMARK 500   C28  SQD B   622     C28  SQD l   101              0.70            
REMARK 500   C36  SQD B   622     C36  SQD l   101              0.71            
REMARK 500   C1   SQD L   102     C1   SQD b   601              0.72            
REMARK 500   C21  SQD L   102     C21  SQD b   601              0.74            
REMARK 500   C29  SQD B   622     C29  SQD l   101              0.74            
REMARK 500   S    SQD B   622     O8   SQD l   101              0.75            
REMARK 500   S    SQD L   102     S    SQD b   601              0.75            
REMARK 500   C15  SQD L   102     C16  SQD b   601              0.75            
REMARK 500   S    SQD B   622     S    SQD l   101              0.75            
REMARK 500   C5   SQD B   622     C6   SQD l   101              0.75            
REMARK 500   C31  SQD L   102     C31  SQD b   601              0.76            
REMARK 500   O8   SQD L   102     O8   SQD b   601              0.77            
REMARK 500   C2   SQD L   102     O2   SQD b   601              0.79            
REMARK 500   C44  SQD B   622     C44  SQD l   101              0.79            
REMARK 500   O6   SQD L   102     O6   SQD b   601              0.80            
REMARK 500   C25  SQD B   622     C25  SQD l   101              0.81            
REMARK 500   C37  SQD B   622     C37  SQD l   101              0.81            
REMARK 500   O8   SQD B   622     O8   SQD l   101              0.82            
REMARK 500   C30  SQD B   622     C29  SQD l   101              0.83            
REMARK 500   O5   SQD L   102     O5   SQD b   601              0.83            
REMARK 500   C6   SQD L   102     C6   SQD b   601              0.84            
REMARK 500   C31  SQD B   622     C31  SQD l   101              0.85            
REMARK 500   C23  SQD L   102     O10  SQD b   601              0.85            
REMARK 500   C9   SQD L   102     C9   SQD b   601              0.86            
REMARK 500   O5   SQD B   622     O5   SQD l   101              0.86            
REMARK 500   O7   SQD L   102     O7   SQD b   601              0.87            
REMARK 500   O5   SQD B   622     C5   SQD l   101              0.87            
REMARK 500   C12  SQD L   102     C12  SQD b   601              0.88            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     361 CLOSE CONTACTS                                
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 k  12   C   -  N   -  CA  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  30      -83.13    -93.95                                   
REMARK 500    LEU A 159      -53.86   -124.85                                   
REMARK 500    ILE A 259      -93.79   -101.74                                   
REMARK 500    TYR B 117       57.10    -91.91                                   
REMARK 500    ASP B 313       45.54    -92.84                                   
REMARK 500    PHE B 383      -78.54    -87.06                                   
REMARK 500    ASP C 107      112.53   -160.34                                   
REMARK 500    GLU C 221      -64.47   -124.72                                   
REMARK 500    TRP C 223     -137.94     46.94                                   
REMARK 500    SER C 416      -45.12    174.70                                   
REMARK 500    SER C 416      -47.30    175.60                                   
REMARK 500    ARG D  12       43.43   -156.21                                   
REMARK 500    VAL D  30      -70.66   -106.72                                   
REMARK 500    SER D  65       15.24   -147.94                                   
REMARK 500    PRO D 140       44.17    -91.62                                   
REMARK 500    ALA D 234       32.45    -77.82                                   
REMARK 500    PRO D 309        1.76    -65.87                                   
REMARK 500    ALA D 351      -52.22     71.97                                   
REMARK 500    LYS H  63       31.85    -82.42                                   
REMARK 500    LYS H  63       32.32    -82.85                                   
REMARK 500    LEU H  65      -88.09   -150.72                                   
REMARK 500    LYS I  33     -120.04   -109.89                                   
REMARK 500    SER J  39       -3.83     73.28                                   
REMARK 500    ASN O  58       -2.89    149.68                                   
REMARK 500    ARG O  73     -163.64     69.61                                   
REMARK 500    LEU O 164      -65.43    -90.27                                   
REMARK 500    ASN U  29      -36.80   -138.50                                   
REMARK 500    TYR U 103     -144.82   -113.47                                   
REMARK 500    ASN V  49       81.71   -159.42                                   
REMARK 500    ASP V  67       36.27    -89.66                                   
REMARK 500    ASP X  35       68.65   -116.48                                   
REMARK 500    VAL a  30      -82.37    -93.00                                   
REMARK 500    LEU a 159      -54.39   -124.56                                   
REMARK 500    ILE a 259      -93.64   -101.05                                   
REMARK 500    TYR b 117       56.57    -91.75                                   
REMARK 500    ASP b 313       45.73    -93.55                                   
REMARK 500    PHE b 383      -78.33    -87.23                                   
REMARK 500    ASP c 107      113.42   -160.15                                   
REMARK 500    GLU c 221      -65.39   -125.42                                   
REMARK 500    TRP c 223     -137.85     46.54                                   
REMARK 500    SER c 416      -45.52    174.29                                   
REMARK 500    SER c 416      -48.23    175.45                                   
REMARK 500    ARG d  12       43.16   -156.56                                   
REMARK 500    VAL d  30      -69.50   -106.70                                   
REMARK 500    SER d  65       14.36   -148.02                                   
REMARK 500    PRO d 140       44.44    -91.70                                   
REMARK 500    ALA d 234       32.55    -78.01                                   
REMARK 500    PRO d 309        1.32    -66.75                                   
REMARK 500    ALA d 351      -53.08     71.10                                   
REMARK 500    LYS h  63       32.40    -82.18                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      66 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     LMG A  613                                                       
REMARK 610     LMG B  621                                                       
REMARK 610     DGD C  515                                                       
REMARK 610     DGD C  516                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     LMG C  518                                                       
REMARK 610     LMG C  519                                                       
REMARK 610     LMG D  408                                                       
REMARK 610     DGD E  101                                                       
REMARK 610     LHG E  102                                                       
REMARK 610     DGD H  102                                                       
REMARK 610     SQD X  101                                                       
REMARK 610     LMG Z  101                                                       
REMARK 610     LMG a  613                                                       
REMARK 610     LMG b  622                                                       
REMARK 610     DGD c  516                                                       
REMARK 610     DGD c  517                                                       
REMARK 610     DGD c  518                                                       
REMARK 610     LMG c  519                                                       
REMARK 610     LMG c  520                                                       
REMARK 610     DGD d  405                                                       
REMARK 610     LHG e  101                                                       
REMARK 610     DGD h  102                                                       
REMARK 610     LMG j  101                                                       
REMARK 610     SQD x  101                                                       
REMARK 610     LMG z  101                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD1                                                    
REMARK 620 2 OEX A 601   O1  153.4                                              
REMARK 620 3 OEX A 601   O2   87.3  75.2                                        
REMARK 620 4 OEX A 601   O5  118.9  76.8  76.7                                  
REMARK 620 5 ALA A 344   O    87.4  71.0  83.1 145.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD2                                                    
REMARK 620 2 OEX A 601   O5   97.3                                              
REMARK 620 3 OEX A 601   O4   82.5  92.5                                        
REMARK 620 4 GLU A 333   OE2 172.0  77.8 103.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 OEX A 601   O1   77.4                                              
REMARK 620 3 OEX A 601   O5   68.9  82.5                                        
REMARK 620 4 OEX A 601   O3  149.7  92.0  81.7                                  
REMARK 620 5 HIS A 332   NE2 111.0 170.2  95.9  78.3                            
REMARK 620 6 ASP A 342   OD2 126.2  86.9 159.0  80.7  91.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2 102.0                                              
REMARK 620 3 HIS D 214   NE2  85.3  72.8                                        
REMARK 620 4 HIS D 268   NE2  77.9 160.0  87.2                                  
REMARK 620 5 BCT A 605   O1  173.9  80.9  90.5  97.6                            
REMARK 620 6 BCT A 605   O2  129.5  92.5 144.9 103.1  55.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 OEX A 601   O2  169.7                                              
REMARK 620 3 OEX A 601   O3   80.5  93.2                                        
REMARK 620 4 OEX A 601   O4  102.8  83.2 175.9                                  
REMARK 620 5 OEX A 601   O5   78.7  92.4  81.5  96.6                            
REMARK 620 6 GLU C 354   OE2  92.3  96.9 100.6  81.9 170.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 OEX A 601   O1   97.1                                              
REMARK 620 3 OEX A 601   O2  171.1  89.0                                        
REMARK 620 4 OEX A 601   O3  100.6  78.9  86.9                                  
REMARK 620 5 ALA A 344   OXT  75.3  91.3  98.3 168.9                            
REMARK 620 6 GLU C 354   OE1  97.2 151.9  80.0  74.8 115.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  39   OD1                                                    
REMARK 620 2 CLA C 511   NA  106.3                                              
REMARK 620 3 CLA C 511   NB   86.2  93.9                                        
REMARK 620 4 CLA C 511   NC   83.5 170.1  88.5                                  
REMARK 620 5 CLA C 511   ND   89.3  91.4 173.8  86.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 103  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM E 103   NA   94.2                                              
REMARK 620 3 HEM E 103   NB  109.3  87.2                                        
REMARK 620 4 HEM E 103   NC   88.6 175.9  94.6                                  
REMARK 620 5 HEM E 103   ND   64.5  89.1 172.5  89.5                            
REMARK 620 6 HIS F  24   NE2 152.5  77.8  96.7  98.4  88.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA J  34   O                                                      
REMARK 620 2 LEU J  36   O    99.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA O 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR O 138   O                                                      
REMARK 620 2 ASN O 200   OD1 116.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM V 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  41   NE2                                                    
REMARK 620 2 HEM V 201   NA   91.2                                              
REMARK 620 3 HEM V 201   NB   82.5  93.0                                        
REMARK 620 4 HEM V 201   NC   74.5 165.7  86.1                                  
REMARK 620 5 HEM V 201   ND   80.9  87.8 163.4  89.0                            
REMARK 620 6 HIS V  92   NE2 157.1 111.4  92.1  82.9 103.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD1                                                    
REMARK 620 2 OEX a 601   O1  153.9                                              
REMARK 620 3 OEX a 601   O2   91.4  75.2                                        
REMARK 620 4 OEX a 601   O5  122.4  76.8  76.6                                  
REMARK 620 5 ASP a 170   OD2  42.4 154.2  87.8  80.6                            
REMARK 620 6 ALA a 344   O    86.1  70.5  83.9 145.2 127.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD2                                                    
REMARK 620 2 OEX a 601   O5   93.2                                              
REMARK 620 3 OEX a 601   O4   86.7  92.5                                        
REMARK 620 4 GLU a 333   OE2 162.9  82.8 110.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 OEX a 601   O1   90.7                                              
REMARK 620 3 OEX a 601   O5   88.2  82.4                                        
REMARK 620 4 OEX a 601   O3  169.1  92.0  81.7                                  
REMARK 620 5 HIS a 332   NE2  87.3 173.3 103.9  91.1                            
REMARK 620 6 ASP a 342   OD2  94.3  87.0 169.1  96.5  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS a 272   NE2  75.3                                              
REMARK 620 3 HIS d 214   NE2 117.9  78.6                                        
REMARK 620 4 HIS d 268   NE2 107.0 168.0 109.6                                  
REMARK 620 5 BCT a 605   O1  146.9  82.0  79.8  90.7                            
REMARK 620 6 BCT a 605   O2  102.7  83.3 128.8  84.7  50.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 OEX a 601   O2  166.4                                              
REMARK 620 3 OEX a 601   O3   85.9  93.2                                        
REMARK 620 4 OEX a 601   O4   97.2  83.2 175.9                                  
REMARK 620 5 OEX a 601   O5   74.1  92.4  81.5  96.6                            
REMARK 620 6 GLU c 354   OE2  96.6  96.9  86.5  95.9 165.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 342   OD1                                                    
REMARK 620 2 OEX a 601   O1   82.1                                              
REMARK 620 3 OEX a 601   O2  169.1  89.0                                        
REMARK 620 4 OEX a 601   O3   97.5  78.9  86.8                                  
REMARK 620 5 ALA a 344   OXT  70.7  85.9 102.6 162.1                            
REMARK 620 6 GLU c 354   OE1  97.8 155.4  92.9  76.6 117.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c  39   OD1                                                    
REMARK 620 2 CLA c 511   NA   87.8                                              
REMARK 620 3 CLA c 511   NB   86.4  91.3                                        
REMARK 620 4 CLA c 511   NC   83.1 170.8  89.7                                  
REMARK 620 5 CLA c 511   ND   81.5  89.9 167.8  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM e 102  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e  23   NE2                                                    
REMARK 620 2 HEM e 102   NA  113.2                                              
REMARK 620 3 HEM e 102   NB  109.4  87.6                                        
REMARK 620 4 HEM e 102   NC   79.2 166.9  92.4                                  
REMARK 620 5 HEM e 102   ND   73.1  90.2 177.2  89.3                            
REMARK 620 6 HIS f  24   NE2 160.5  74.0  88.6  92.9  89.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA f 102  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG f  45   O                                                      
REMARK 620 2 ARG f  45   OXT  46.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG j 102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY j  31   O                                                      
REMARK 620 2 ALA j  34   O    92.2                                              
REMARK 620 3 LEU j  36   O   103.0  99.9                                        
REMARK 620 4 LMG j 101   O4   68.7 158.7  76.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA o 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR o 138   O                                                      
REMARK 620 2 ASN o 200   OD1 143.9                                              
REMARK 620 3 VAL o 201   O    73.0  70.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM v 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS v  41   NE2                                                    
REMARK 620 2 HEM v 201   NA   85.9                                              
REMARK 620 3 HEM v 201   NB   74.8  91.6                                        
REMARK 620 4 HEM v 201   NC   81.8 167.2  88.9                                  
REMARK 620 5 HEM v 201   ND   89.3  87.6 164.1  88.4                            
REMARK 620 6 HIS v  92   NE2 171.5  96.4  97.0  96.3  98.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG E 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR F 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR I 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG L 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD L 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL U 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD X 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG Z 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA b 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA f 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG j 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG j 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD l 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG l 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA o 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR t 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM v 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD x 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG z 101                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ARC   RELATED DB: PDB                                   
DBREF  5E79 A   11   344  UNP    P0A444   PSBA1_THEEB     11    344             
DBREF  5E79 B    2   505  UNP    Q8DIQ1   PSBB_THEEB       2    505             
DBREF  5E79 C   23   473  UNP    Q8DIF8   PSBC_THEEB      11    461             
DBREF  5E79 D   11   352  UNP    Q8CM25   PSBD_THEEB      11    352             
DBREF  5E79 E    4    84  UNP    Q8DIP0   PSBE_THEEB       4     84             
DBREF  5E79 F   12    45  UNP    Q8DIN9   PSBF_THEEB      12     45             
DBREF  5E79 H    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  5E79 I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  5E79 J    3    40  UNP    P59087   PSBJ_THEEB       3     40             
DBREF  5E79 K   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  5E79 L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5E79 M    1    34  UNP    Q8DHA7   PSBM_THEEB       1     34             
DBREF  5E79 O    4   246  UNP    P0A431   PSBO_THEEB      30    272             
DBREF  5E79 T    1    30  UNP    Q8DIQ0   PSBT_THEEB       1     30             
DBREF  5E79 U    8   104  UNP    Q9F1L5   PSBU_THEEB      38    134             
DBREF  5E79 V    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  5E79 Y   18    46  UNP    Q8DJI1   YCF12_THEEB     18     46             
DBREF  5E79 X    2    40  UNP    Q9F1R6   PSBX_THEEB       2     40             
DBREF  5E79 Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  5E79 a   11   344  UNP    P0A444   PSBA1_THEEB     11    344             
DBREF  5E79 b    2   505  UNP    Q8DIQ1   PSBB_THEEB       2    505             
DBREF  5E79 c   23   473  UNP    Q8DIF8   PSBC_THEEB      11    461             
DBREF  5E79 d   11   352  UNP    Q8CM25   PSBD_THEEB      11    352             
DBREF  5E79 e    4    84  UNP    Q8DIP0   PSBE_THEEB       4     84             
DBREF  5E79 f   12    45  UNP    Q8DIN9   PSBF_THEEB      12     45             
DBREF  5E79 h    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  5E79 i    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  5E79 j    3    40  UNP    P59087   PSBJ_THEEB       3     40             
DBREF  5E79 k   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  5E79 l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5E79 m    1    34  UNP    Q8DHA7   PSBM_THEEB       1     34             
DBREF  5E79 o    4   246  UNP    P0A431   PSBO_THEEB      30    272             
DBREF  5E79 t    1    30  UNP    Q8DIQ0   PSBT_THEEB       1     30             
DBREF  5E79 u    8   104  UNP    Q9F1L5   PSBU_THEEB      38    134             
DBREF  5E79 v    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  5E79 y   18    46  UNP    Q8DJI1   YCF12_THEEB     18     46             
DBREF  5E79 x    2    40  UNP    Q9F1R6   PSBX_THEEB       2     40             
DBREF  5E79 z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
SEQADV 5E79 ALA A  286  UNP  P0A444    THR   286 CONFLICT                       
SEQADV 5E79 ALA a  286  UNP  P0A444    THR   286 CONFLICT                       
SEQRES   1 A  334  ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER          
SEQRES   2 A  334  THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE          
SEQRES   3 A  334  MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL          
SEQRES   4 A  334  ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY          
SEQRES   5 A  334  ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN          
SEQRES   6 A  334  ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA          
SEQRES   7 A  334  ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER          
SEQRES   8 A  334  LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU          
SEQRES   9 A  334  ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET          
SEQRES  10 A  334  GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG          
SEQRES  11 A  334  PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER          
SEQRES  12 A  334  ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY          
SEQRES  13 A  334  SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR          
SEQRES  14 A  334  PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE          
SEQRES  15 A  334  LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL          
SEQRES  16 A  334  PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU          
SEQRES  17 A  334  VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU          
SEQRES  18 A  334  SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU          
SEQRES  19 A  334  THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG          
SEQRES  20 A  334  LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER          
SEQRES  21 A  334  LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL          
SEQRES  22 A  334  TRP PHE ALA ALA LEU GLY ILE SER THR MET ALA PHE ASN          
SEQRES  23 A  334  LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA          
SEQRES  24 A  334  LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN          
SEQRES  25 A  334  ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN          
SEQRES  26 A  334  ALA HIS ASN PHE PRO LEU ASP LEU ALA                          
SEQRES   1 B  504  GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN          
SEQRES   2 B  504  ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR          
SEQRES   3 B  504  ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR          
SEQRES   4 B  504  GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN          
SEQRES   5 B  504  PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET          
SEQRES   6 B  504  ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER          
SEQRES   7 B  504  ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER          
SEQRES   8 B  504  PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY          
SEQRES   9 B  504  LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP          
SEQRES  10 B  504  ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO          
SEQRES  11 B  504  ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE          
SEQRES  12 B  504  LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS          
SEQRES  13 B  504  LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP          
SEQRES  14 B  504  PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO          
SEQRES  15 B  504  GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY          
SEQRES  16 B  504  GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY          
SEQRES  17 B  504  ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO          
SEQRES  18 B  504  GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU          
SEQRES  19 B  504  THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA          
SEQRES  20 B  504  ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA          
SEQRES  21 B  504  THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN          
SEQRES  22 B  504  TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG          
SEQRES  23 B  504  VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU          
SEQRES  24 B  504  ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP          
SEQRES  25 B  504  TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG          
SEQRES  26 B  504  THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA          
SEQRES  27 B  504  TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU          
SEQRES  28 B  504  GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER          
SEQRES  29 B  504  PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS          
SEQRES  30 B  504  ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER          
SEQRES  31 B  504  PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY          
SEQRES  32 B  504  GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL          
SEQRES  33 B  504  LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE          
SEQRES  34 B  504  GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE          
SEQRES  35 B  504  ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA          
SEQRES  36 B  504  VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS          
SEQRES  37 B  504  GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE          
SEQRES  38 B  504  ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE          
SEQRES  39 B  504  TYR GLN LYS VAL GLY ASP VAL THR THR ARG                      
SEQRES   1 C  451  ALA THR ASN ARG ASP GLN GLU SER SER GLY PHE ALA TRP          
SEQRES   2 C  451  TRP ALA GLY ASN ALA ARG LEU ILE ASN LEU SER GLY LYS          
SEQRES   3 C  451  LEU LEU GLY ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL          
SEQRES   4 C  451  PHE TRP ALA GLY ALA MET THR LEU PHE GLU LEU ALA HIS          
SEQRES   5 C  451  PHE ILE PRO GLU LYS PRO MET TYR GLU GLN GLY LEU ILE          
SEQRES   6 C  451  LEU ILE PRO HIS ILE ALA THR LEU GLY TRP GLY VAL GLY          
SEQRES   7 C  451  PRO GLY GLY GLU VAL VAL ASP THR PHE PRO PHE PHE VAL          
SEQRES   8 C  451  VAL GLY VAL VAL HIS LEU ILE SER SER ALA VAL LEU GLY          
SEQRES   9 C  451  PHE GLY GLY VAL TYR HIS ALA ILE ARG GLY PRO GLU THR          
SEQRES  10 C  451  LEU GLU GLU TYR SER SER PHE PHE GLY TYR ASP TRP LYS          
SEQRES  11 C  451  ASP LYS ASN LYS MET THR THR ILE LEU GLY PHE HIS LEU          
SEQRES  12 C  451  ILE VAL LEU GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS          
SEQRES  13 C  451  ALA MET PHE PHE GLY GLY LEU TYR ASP THR TRP ALA PRO          
SEQRES  14 C  451  GLY GLY GLY ASP VAL ARG VAL ILE THR ASN PRO THR LEU          
SEQRES  15 C  451  ASP PRO ARG VAL ILE PHE GLY TYR LEU LEU LYS SER PRO          
SEQRES  16 C  451  PHE GLY GLY GLU GLY TRP ILE VAL SER VAL ASN ASN LEU          
SEQRES  17 C  451  GLU ASP VAL VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE          
SEQRES  18 C  451  CYS ILE ALA GLY GLY ILE TRP HIS ILE LEU THR THR PRO          
SEQRES  19 C  451  PHE GLY TRP ALA ARG ARG ALA PHE ILE TRP SER GLY GLU          
SEQRES  20 C  451  ALA TYR LEU SER TYR SER LEU GLY ALA LEU SER MET MET          
SEQRES  21 C  451  GLY PHE ILE ALA THR CYS PHE VAL TRP PHE ASN ASN THR          
SEQRES  22 C  451  VAL TYR PRO SER GLU PHE TYR GLY PRO THR GLY PRO GLU          
SEQRES  23 C  451  ALA SER GLN ALA GLN ALA MET THR PHE LEU ILE ARG ASP          
SEQRES  24 C  451  GLN LYS LEU GLY ALA ASN VAL GLY SER ALA GLN GLY PRO          
SEQRES  25 C  451  THR GLY LEU GLY LYS TYR LEU MET ARG SER PRO THR GLY          
SEQRES  26 C  451  GLU ILE ILE PHE GLY GLY GLU THR MET ARG PHE TRP ASP          
SEQRES  27 C  451  PHE ARG GLY PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN          
SEQRES  28 C  451  GLY LEU ASP LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO          
SEQRES  29 C  451  TRP GLN GLU ARG ARG ALA ALA GLU TYR MET THR HIS ALA          
SEQRES  30 C  451  PRO LEU GLY SER LEU ASN SER VAL GLY GLY VAL ALA THR          
SEQRES  31 C  451  GLU ILE ASN SER VAL ASN PHE VAL SER PRO ARG SER TRP          
SEQRES  32 C  451  LEU ALA THR SER HIS PHE VAL LEU ALA PHE PHE PHE LEU          
SEQRES  33 C  451  VAL GLY HIS LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA          
SEQRES  34 C  451  ALA ALA GLY PHE GLU LYS GLY ILE ASP ARG GLU SER GLU          
SEQRES  35 C  451  PRO VAL LEU SER MET PRO SER LEU ASP                          
SEQRES   1 D  342  GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS          
SEQRES   2 D  342  ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU          
SEQRES   3 D  342  LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU          
SEQRES   4 D  342  THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY          
SEQRES   5 D  342  LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR          
SEQRES   6 D  342  VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER          
SEQRES   7 D  342  LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE          
SEQRES   8 D  342  THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE          
SEQRES   9 D  342  ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU          
SEQRES  10 D  342  ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO          
SEQRES  11 D  342  TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE          
SEQRES  12 D  342  VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER          
SEQRES  13 D  342  TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE          
SEQRES  14 D  342  ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR          
SEQRES  15 D  342  LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU          
SEQRES  16 D  342  GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL          
SEQRES  17 D  342  GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR          
SEQRES  18 D  342  PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR          
SEQRES  19 D  342  SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE          
SEQRES  20 D  342  GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE          
SEQRES  21 D  342  MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA          
SEQRES  22 D  342  ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR          
SEQRES  23 D  342  ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO          
SEQRES  24 D  342  GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN          
SEQRES  25 D  342  GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO          
SEQRES  26 D  342  HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG          
SEQRES  27 D  342  GLY ASN ALA LEU                                              
SEQRES   1 E   81  THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER          
SEQRES   2 E   81  VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA          
SEQRES   3 E   81  LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU          
SEQRES   4 E   81  ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR          
SEQRES   5 E   81  TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP          
SEQRES   6 E   81  ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU          
SEQRES   7 E   81  GLN LEU LYS                                                  
SEQRES   1 F   34  SER TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS          
SEQRES   2 F   34  THR LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE          
SEQRES   3 F   34  ALA ALA MET GLN PHE ILE GLN ARG                              
SEQRES   1 H   65  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 H   65  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 H   65  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 H   65  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 H   65  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY          
SEQRES   1 I   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 I   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 I   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 J   38  SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL ALA THR          
SEQRES   2 J   38  VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY LEU PHE          
SEQRES   3 J   38  PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER LEU              
SEQRES   1 K   37  LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL          
SEQRES   2 K   37  ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU          
SEQRES   3 K   37  ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG                  
SEQRES   1 L   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 L   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 L   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 M   34  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 M   34  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 M   34  VAL GLN THR GLU SER GLN GLN LYS                              
SEQRES   1 O  243  THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA          
SEQRES   2 O  243  ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA          
SEQRES   3 O  243  TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG          
SEQRES   4 O  243  LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU          
SEQRES   5 O  243  PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR          
SEQRES   6 O  243  LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE          
SEQRES   7 O  243  GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR          
SEQRES   8 O  243  PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR          
SEQRES   9 O  243  VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE          
SEQRES  10 O  243  THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL          
SEQRES  11 O  243  THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE          
SEQRES  12 O  243  ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO          
SEQRES  13 O  243  LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE          
SEQRES  14 O  243  ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA          
SEQRES  15 O  243  ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER          
SEQRES  16 O  243  LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE          
SEQRES  17 O  243  ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP          
SEQRES  18 O  243  MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY          
SEQRES  19 O  243  VAL PHE TYR ALA SER ILE GLU PRO ALA                          
SEQRES   1 T   30  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 T   30  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 T   30  PRO ARG ILE THR                                              
SEQRES   1 U   97  GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA          
SEQRES   2 U   97  TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA          
SEQRES   3 U   97  ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA          
SEQRES   4 U   97  LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU          
SEQRES   5 U   97  ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS          
SEQRES   6 U   97  GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR          
SEQRES   7 U   97  GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR          
SEQRES   8 U   97  ASN ASN GLY LEU TYR LYS                                      
SEQRES   1 V  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 V  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 V  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 V  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 V  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 V  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 V  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 V  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 V  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 V  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 V  137  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 Y   29  VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE          
SEQRES   2 Y   29  ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG          
SEQRES   3 Y   29  GLY ASN LEU                                                  
SEQRES   1 X   39  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 X   39  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 X   39  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER          
SEQRES   1 Z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 Z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 Z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 Z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 Z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
SEQRES   1 a  334  ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER          
SEQRES   2 a  334  THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE          
SEQRES   3 a  334  MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL          
SEQRES   4 a  334  ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY          
SEQRES   5 a  334  ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN          
SEQRES   6 a  334  ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA          
SEQRES   7 a  334  ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER          
SEQRES   8 a  334  LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU          
SEQRES   9 a  334  ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET          
SEQRES  10 a  334  GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG          
SEQRES  11 a  334  PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER          
SEQRES  12 a  334  ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY          
SEQRES  13 a  334  SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR          
SEQRES  14 a  334  PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE          
SEQRES  15 a  334  LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL          
SEQRES  16 a  334  PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU          
SEQRES  17 a  334  VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU          
SEQRES  18 a  334  SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU          
SEQRES  19 a  334  THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG          
SEQRES  20 a  334  LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER          
SEQRES  21 a  334  LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL          
SEQRES  22 a  334  TRP PHE ALA ALA LEU GLY ILE SER THR MET ALA PHE ASN          
SEQRES  23 a  334  LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA          
SEQRES  24 a  334  LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN          
SEQRES  25 a  334  ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN          
SEQRES  26 a  334  ALA HIS ASN PHE PRO LEU ASP LEU ALA                          
SEQRES   1 b  504  GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN          
SEQRES   2 b  504  ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR          
SEQRES   3 b  504  ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR          
SEQRES   4 b  504  GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN          
SEQRES   5 b  504  PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET          
SEQRES   6 b  504  ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER          
SEQRES   7 b  504  ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER          
SEQRES   8 b  504  PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY          
SEQRES   9 b  504  LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP          
SEQRES  10 b  504  ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO          
SEQRES  11 b  504  ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE          
SEQRES  12 b  504  LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS          
SEQRES  13 b  504  LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP          
SEQRES  14 b  504  PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO          
SEQRES  15 b  504  GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY          
SEQRES  16 b  504  GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY          
SEQRES  17 b  504  ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO          
SEQRES  18 b  504  GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU          
SEQRES  19 b  504  THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA          
SEQRES  20 b  504  ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA          
SEQRES  21 b  504  THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN          
SEQRES  22 b  504  TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG          
SEQRES  23 b  504  VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU          
SEQRES  24 b  504  ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP          
SEQRES  25 b  504  TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG          
SEQRES  26 b  504  THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA          
SEQRES  27 b  504  TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU          
SEQRES  28 b  504  GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER          
SEQRES  29 b  504  PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS          
SEQRES  30 b  504  ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER          
SEQRES  31 b  504  PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY          
SEQRES  32 b  504  GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL          
SEQRES  33 b  504  LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE          
SEQRES  34 b  504  GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE          
SEQRES  35 b  504  ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA          
SEQRES  36 b  504  VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS          
SEQRES  37 b  504  GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE          
SEQRES  38 b  504  ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE          
SEQRES  39 b  504  TYR GLN LYS VAL GLY ASP VAL THR THR ARG                      
SEQRES   1 c  451  ALA THR ASN ARG ASP GLN GLU SER SER GLY PHE ALA TRP          
SEQRES   2 c  451  TRP ALA GLY ASN ALA ARG LEU ILE ASN LEU SER GLY LYS          
SEQRES   3 c  451  LEU LEU GLY ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL          
SEQRES   4 c  451  PHE TRP ALA GLY ALA MET THR LEU PHE GLU LEU ALA HIS          
SEQRES   5 c  451  PHE ILE PRO GLU LYS PRO MET TYR GLU GLN GLY LEU ILE          
SEQRES   6 c  451  LEU ILE PRO HIS ILE ALA THR LEU GLY TRP GLY VAL GLY          
SEQRES   7 c  451  PRO GLY GLY GLU VAL VAL ASP THR PHE PRO PHE PHE VAL          
SEQRES   8 c  451  VAL GLY VAL VAL HIS LEU ILE SER SER ALA VAL LEU GLY          
SEQRES   9 c  451  PHE GLY GLY VAL TYR HIS ALA ILE ARG GLY PRO GLU THR          
SEQRES  10 c  451  LEU GLU GLU TYR SER SER PHE PHE GLY TYR ASP TRP LYS          
SEQRES  11 c  451  ASP LYS ASN LYS MET THR THR ILE LEU GLY PHE HIS LEU          
SEQRES  12 c  451  ILE VAL LEU GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS          
SEQRES  13 c  451  ALA MET PHE PHE GLY GLY LEU TYR ASP THR TRP ALA PRO          
SEQRES  14 c  451  GLY GLY GLY ASP VAL ARG VAL ILE THR ASN PRO THR LEU          
SEQRES  15 c  451  ASP PRO ARG VAL ILE PHE GLY TYR LEU LEU LYS SER PRO          
SEQRES  16 c  451  PHE GLY GLY GLU GLY TRP ILE VAL SER VAL ASN ASN LEU          
SEQRES  17 c  451  GLU ASP VAL VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE          
SEQRES  18 c  451  CYS ILE ALA GLY GLY ILE TRP HIS ILE LEU THR THR PRO          
SEQRES  19 c  451  PHE GLY TRP ALA ARG ARG ALA PHE ILE TRP SER GLY GLU          
SEQRES  20 c  451  ALA TYR LEU SER TYR SER LEU GLY ALA LEU SER MET MET          
SEQRES  21 c  451  GLY PHE ILE ALA THR CYS PHE VAL TRP PHE ASN ASN THR          
SEQRES  22 c  451  VAL TYR PRO SER GLU PHE TYR GLY PRO THR GLY PRO GLU          
SEQRES  23 c  451  ALA SER GLN ALA GLN ALA MET THR PHE LEU ILE ARG ASP          
SEQRES  24 c  451  GLN LYS LEU GLY ALA ASN VAL GLY SER ALA GLN GLY PRO          
SEQRES  25 c  451  THR GLY LEU GLY LYS TYR LEU MET ARG SER PRO THR GLY          
SEQRES  26 c  451  GLU ILE ILE PHE GLY GLY GLU THR MET ARG PHE TRP ASP          
SEQRES  27 c  451  PHE ARG GLY PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN          
SEQRES  28 c  451  GLY LEU ASP LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO          
SEQRES  29 c  451  TRP GLN GLU ARG ARG ALA ALA GLU TYR MET THR HIS ALA          
SEQRES  30 c  451  PRO LEU GLY SER LEU ASN SER VAL GLY GLY VAL ALA THR          
SEQRES  31 c  451  GLU ILE ASN SER VAL ASN PHE VAL SER PRO ARG SER TRP          
SEQRES  32 c  451  LEU ALA THR SER HIS PHE VAL LEU ALA PHE PHE PHE LEU          
SEQRES  33 c  451  VAL GLY HIS LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA          
SEQRES  34 c  451  ALA ALA GLY PHE GLU LYS GLY ILE ASP ARG GLU SER GLU          
SEQRES  35 c  451  PRO VAL LEU SER MET PRO SER LEU ASP                          
SEQRES   1 d  342  GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS          
SEQRES   2 d  342  ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU          
SEQRES   3 d  342  LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU          
SEQRES   4 d  342  THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY          
SEQRES   5 d  342  LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR          
SEQRES   6 d  342  VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER          
SEQRES   7 d  342  LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE          
SEQRES   8 d  342  THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE          
SEQRES   9 d  342  ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU          
SEQRES  10 d  342  ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO          
SEQRES  11 d  342  TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE          
SEQRES  12 d  342  VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER          
SEQRES  13 d  342  TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE          
SEQRES  14 d  342  ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR          
SEQRES  15 d  342  LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU          
SEQRES  16 d  342  GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL          
SEQRES  17 d  342  GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR          
SEQRES  18 d  342  PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR          
SEQRES  19 d  342  SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE          
SEQRES  20 d  342  GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE          
SEQRES  21 d  342  MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA          
SEQRES  22 d  342  ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR          
SEQRES  23 d  342  ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO          
SEQRES  24 d  342  GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN          
SEQRES  25 d  342  GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO          
SEQRES  26 d  342  HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG          
SEQRES  27 d  342  GLY ASN ALA LEU                                              
SEQRES   1 e   81  THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER          
SEQRES   2 e   81  VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA          
SEQRES   3 e   81  LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU          
SEQRES   4 e   81  ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR          
SEQRES   5 e   81  TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP          
SEQRES   6 e   81  ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU          
SEQRES   7 e   81  GLN LEU LYS                                                  
SEQRES   1 f   34  SER TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS          
SEQRES   2 f   34  THR LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE          
SEQRES   3 f   34  ALA ALA MET GLN PHE ILE GLN ARG                              
SEQRES   1 h   65  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 h   65  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 h   65  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 h   65  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 h   65  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY          
SEQRES   1 i   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 i   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 i   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 j   38  SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL ALA THR          
SEQRES   2 j   38  VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY LEU PHE          
SEQRES   3 j   38  PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER LEU              
SEQRES   1 k   37  LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL          
SEQRES   2 k   37  ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU          
SEQRES   3 k   37  ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG                  
SEQRES   1 l   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 l   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 l   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 m   34  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 m   34  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 m   34  VAL GLN THR GLU SER GLN GLN LYS                              
SEQRES   1 o  243  THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA          
SEQRES   2 o  243  ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA          
SEQRES   3 o  243  TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG          
SEQRES   4 o  243  LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU          
SEQRES   5 o  243  PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR          
SEQRES   6 o  243  LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE          
SEQRES   7 o  243  GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR          
SEQRES   8 o  243  PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR          
SEQRES   9 o  243  VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE          
SEQRES  10 o  243  THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL          
SEQRES  11 o  243  THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE          
SEQRES  12 o  243  ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO          
SEQRES  13 o  243  LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE          
SEQRES  14 o  243  ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA          
SEQRES  15 o  243  ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER          
SEQRES  16 o  243  LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE          
SEQRES  17 o  243  ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP          
SEQRES  18 o  243  MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY          
SEQRES  19 o  243  VAL PHE TYR ALA SER ILE GLU PRO ALA                          
SEQRES   1 t   30  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 t   30  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 t   30  PRO ARG ILE THR                                              
SEQRES   1 u   97  GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA          
SEQRES   2 u   97  TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA          
SEQRES   3 u   97  ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA          
SEQRES   4 u   97  LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU          
SEQRES   5 u   97  ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS          
SEQRES   6 u   97  GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR          
SEQRES   7 u   97  GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR          
SEQRES   8 u   97  ASN ASN GLY LEU TYR LYS                                      
SEQRES   1 v  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 v  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 v  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 v  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 v  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 v  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 v  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 v  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 v  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 v  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 v  137  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 y   29  VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE          
SEQRES   2 y   29  ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG          
SEQRES   3 y   29  GLY ASN LEU                                                  
SEQRES   1 x   39  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 x   39  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 x   39  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER          
SEQRES   1 z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
HET    OEX  A 601      10                                                       
HET    FE2  A 602       1                                                       
HET     CL  A 603       1                                                       
HET     CL  A 604       1                                                       
HET    BCT  A 605       4                                                       
HET    CLA  A 606      65                                                       
HET    CLA  A 607      65                                                       
HET    PHO  A 608      64                                                       
HET    CLA  A 609      65                                                       
HET    BCR  A 610      40                                                       
HET    PL9  A 611      55                                                       
HET    SQD  A 612      54                                                       
HET    LMG  A 613      51                                                       
HET    SQD  A 614      54                                                       
HET    LHG  A 615      49                                                       
HET     CA  B 601       1                                                       
HET    CLA  B 602      65                                                       
HET    CLA  B 603      65                                                       
HET    CLA  B 604      65                                                       
HET    CLA  B 605      65                                                       
HET    CLA  B 606      65                                                       
HET    CLA  B 607     130                                                       
HET    CLA  B 608      65                                                       
HET    CLA  B 609      65                                                       
HET    CLA  B 610      65                                                       
HET    CLA  B 611      65                                                       
HET    CLA  B 612      65                                                       
HET    CLA  B 613      65                                                       
HET    CLA  B 614      65                                                       
HET    CLA  B 615      65                                                       
HET    CLA  B 616      65                                                       
HET    CLA  B 617      65                                                       
HET    BCR  B 618      40                                                       
HET    BCR  B 619      40                                                       
HET    BCR  B 620      40                                                       
HET    LMG  B 621      51                                                       
HET    SQD  B 622      54                                                       
HET    CLA  C 501      65                                                       
HET    CLA  C 502      65                                                       
HET    CLA  C 503      65                                                       
HET    CLA  C 504      65                                                       
HET    CLA  C 505      65                                                       
HET    CLA  C 506      65                                                       
HET    CLA  C 507      65                                                       
HET    CLA  C 508      65                                                       
HET    CLA  C 509      65                                                       
HET    CLA  C 510      65                                                       
HET    CLA  C 511      65                                                       
HET    CLA  C 512      65                                                       
HET    CLA  C 513      65                                                       
HET    BCR  C 514      40                                                       
HET    DGD  C 515      62                                                       
HET    DGD  C 516      62                                                       
HET    DGD  C 517      62                                                       
HET    LMG  C 518      51                                                       
HET    LMG  C 519      51                                                       
HET    PHO  D 401      64                                                       
HET    CLA  D 402      65                                                       
HET    CLA  D 403      65                                                       
HET    CLA  D 404      65                                                       
HET    PL9  D 405      55                                                       
HET    LHG  D 406      49                                                       
HET    LHG  D 407      49                                                       
HET    LMG  D 408      51                                                       
HET    DGD  E 101      62                                                       
HET    LHG  E 102      42                                                       
HET    HEM  E 103      43                                                       
HET    BCR  F 101      40                                                       
HET     CA  F 102       1                                                       
HET    BCR  H 101      40                                                       
HET    DGD  H 102      62                                                       
HET    BCR  I 101      40                                                       
HET     MG  J 101       1                                                       
HET    BCR  K 101      40                                                       
HET    BCR  K 102      40                                                       
HET    LHG  L 101      49                                                       
HET    SQD  L 102      54                                                       
HET     CA  O 301       1                                                       
HET    BCR  T 101      40                                                       
HET     CL  U 201       1                                                       
HET    HEM  V 201      43                                                       
HET    SQD  X 101      43                                                       
HET    LMG  Z 101      37                                                       
HET    OEX  a 601      10                                                       
HET    FE2  a 602       1                                                       
HET     CL  a 603       1                                                       
HET     CL  a 604       1                                                       
HET    BCT  a 605       4                                                       
HET    CLA  a 606      65                                                       
HET    CLA  a 607      65                                                       
HET    PHO  a 608      64                                                       
HET    CLA  a 609      65                                                       
HET    BCR  a 610      40                                                       
HET    PL9  a 611      55                                                       
HET    SQD  a 612      54                                                       
HET    LMG  a 613      51                                                       
HET    SQD  a 614      54                                                       
HET    CLA  a 615      65                                                       
HET    LHG  a 616      49                                                       
HET    SQD  b 601      54                                                       
HET     CA  b 602       1                                                       
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     130                                                       
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    BCR  b 619      40                                                       
HET    BCR  b 620      40                                                       
HET    BCR  b 621      40                                                       
HET    LMG  b 622      51                                                       
HET    CLA  c 501      65                                                       
HET    CLA  c 502      65                                                       
HET    CLA  c 503      65                                                       
HET    CLA  c 504      65                                                       
HET    CLA  c 505      65                                                       
HET    CLA  c 506      65                                                       
HET    CLA  c 507      65                                                       
HET    CLA  c 508      65                                                       
HET    CLA  c 509      65                                                       
HET    CLA  c 510      65                                                       
HET    CLA  c 511      65                                                       
HET    CLA  c 512      65                                                       
HET    CLA  c 513      65                                                       
HET    BCR  c 514      40                                                       
HET    BCR  c 515      40                                                       
HET    DGD  c 516      62                                                       
HET    DGD  c 517      62                                                       
HET    DGD  c 518      62                                                       
HET    LMG  c 519      51                                                       
HET    LMG  c 520      51                                                       
HET    BCR  c 521      40                                                       
HET    PHO  d 401      64                                                       
HET    CLA  d 402      65                                                       
HET    CLA  d 403      65                                                       
HET    PL9  d 404      55                                                       
HET    DGD  d 405      62                                                       
HET    LHG  d 406      49                                                       
HET    LHG  d 407      49                                                       
HET    LHG  e 101      42                                                       
HET    HEM  e 102      43                                                       
HET    BCR  f 101      40                                                       
HET     CA  f 102       1                                                       
HET    BCR  h 101      40                                                       
HET    DGD  h 102      62                                                       
HET    LMG  j 101      51                                                       
HET     MG  j 102       1                                                       
HET    BCR  k 101      40                                                       
HET    SQD  l 101      54                                                       
HET    LHG  l 102      49                                                       
HET     CA  o 301       1                                                       
HET    BCR  t 101      40                                                       
HET     CL  u 201       1                                                       
HET    HEM  v 201      43                                                       
HET    SQD  x 101      43                                                       
HET    LMG  z 101      37                                                       
HETNAM     OEX CA-MN4-O5 CLUSTER                                                
HETNAM     FE2 FE (II) ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN A                                                     
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,           
HETNAM   2 PL9  6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-               
HETNAM   3 PL9  CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-          
HETNAM   4 PL9  BENZOQUINONE                                                    
HETNAM     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM      CA CALCIUM ION                                                      
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     HEM HEME                                                             
FORMUL  39  OEX    2(CA MN4 O5)                                                 
FORMUL  40  FE2    2(FE 2+)                                                     
FORMUL  41   CL    6(CL 1-)                                                     
FORMUL  43  BCT    2(C H O3 1-)                                                 
FORMUL  44  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  46  PHO    4(C55 H74 N4 O5)                                             
FORMUL  48  BCR    22(C40 H56)                                                  
FORMUL  49  PL9    4(C53 H80 O2)                                                
FORMUL  50  SQD    10(C41 H78 O12 S)                                            
FORMUL  51  LMG    12(C45 H86 O10)                                              
FORMUL  53  LHG    10(C38 H75 O10 P)                                            
FORMUL  54   CA    6(CA 2+)                                                     
FORMUL  90  DGD    10(C51 H96 O15)                                              
FORMUL  05  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  11   MG    2(MG 2+)                                                     
HELIX    1 AA1 ASN A   12  THR A   22  1                                  11    
HELIX    2 AA2 VAL A   30  ALA A   55  1                                  26    
HELIX    3 AA3 SER A   70  GLY A   74  5                                   5    
HELIX    4 AA4 PRO A   95  ALA A   99  5                                   5    
HELIX    5 AA5 SER A  101  ASN A  108  1                                   8    
HELIX    6 AA6 GLY A  109  LEU A  137  1                                  29    
HELIX    7 AA7 TRP A  142  LEU A  159  1                                  18    
HELIX    8 AA8 LEU A  159  GLY A  166  1                                   8    
HELIX    9 AA9 SER A  167  GLY A  171  5                                   5    
HELIX   10 AB1 ILE A  176  ASN A  191  1                                  16    
HELIX   11 AB2 ILE A  192  MET A  194  5                                   3    
HELIX   12 AB3 HIS A  195  SER A  222  1                                  28    
HELIX   13 AB4 SER A  232  TYR A  237  5                                   6    
HELIX   14 AB5 ASN A  247  ILE A  259  1                                  13    
HELIX   15 AB6 PHE A  260  SER A  264  5                                   5    
HELIX   16 AB7 ASN A  267  ALA A  294  1                                  28    
HELIX   17 AB8 THR A  316  HIS A  332  1                                  17    
HELIX   18 AB9 TYR B    6  ILE B   13  5                                   8    
HELIX   19 AC1 ASP B   15  PHE B   45  1                                  31    
HELIX   20 AC2 PRO B   54  GLN B   58  5                                   5    
HELIX   21 AC3 VAL B   62  LEU B   69  1                                   8    
HELIX   22 AC4 SER B   92  TYR B  117  1                                  26    
HELIX   23 AC5 LEU B  120  ARG B  124  5                                   5    
HELIX   24 AC6 ASP B  134  HIS B  157  1                                  24    
HELIX   25 AC7 GLY B  186  ASN B  191  5                                   6    
HELIX   26 AC8 ASN B  194  VAL B  219  1                                  26    
HELIX   27 AC9 PRO B  222  LEU B  229  1                                   8    
HELIX   28 AD1 ASN B  233  GLY B  259  1                                  27    
HELIX   29 AD2 PRO B  264  GLY B  269  1                                   6    
HELIX   30 AD3 THR B  271  SER B  277  1                                   7    
HELIX   31 AD4 SER B  278  SER B  294  1                                  17    
HELIX   32 AD5 THR B  297  ALA B  304  1                                   8    
HELIX   33 AD6 PRO B  306  ASP B  313  1                                   8    
HELIX   34 AD7 TYR B  314  GLY B  322  5                                   9    
HELIX   35 AD8 PRO B  329  GLY B  333  5                                   5    
HELIX   36 AD9 SER B  391  GLY B  396  1                                   6    
HELIX   37 AE1 ASP B  413  ILE B  425  1                                  13    
HELIX   38 AE2 SER B  446  PHE B  475  1                                  30    
HELIX   39 AE3 ARG B  476  PHE B  479  5                                   4    
HELIX   40 AE4 SER B  487  VAL B  491  5                                   5    
HELIX   41 AE5 ASP B  501  ARG B  505  5                                   5    
HELIX   42 AE6 ASP C   27  GLY C   32  1                                   6    
HELIX   43 AE7 ALA C   34  ILE C   43  5                                  10    
HELIX   44 AE8 LEU C   45  PHE C   75  1                                  31    
HELIX   45 AE9 PRO C   80  GLY C   85  5                                   6    
HELIX   46 AF1 ILE C   87  LEU C   95  1                                   9    
HELIX   47 AF2 GLY C  100  GLU C  104  5                                   5    
HELIX   48 AF3 THR C  108  ARG C  135  1                                  28    
HELIX   49 AF4 ASP C  153  PHE C  182  1                                  30    
HELIX   50 AF5 ASP C  205  LEU C  214  1                                  10    
HELIX   51 AF6 GLY C  222  VAL C  227  5                                   6    
HELIX   52 AF7 ASN C  229  THR C  254  1                                  26    
HELIX   53 AF8 PHE C  257  PHE C  264  1                                   8    
HELIX   54 AF9 SER C  267  ASN C  293  1                                  27    
HELIX   55 AG1 PRO C  298  GLY C  303  1                                   6    
HELIX   56 AG2 THR C  305  GLY C  325  1                                  21    
HELIX   57 AG3 GLY C  353  TRP C  359  5                                   7    
HELIX   58 AG4 LEU C  366  PRO C  368  5                                   3    
HELIX   59 AG5 ASP C  376  ASP C  383  1                                   8    
HELIX   60 AG6 GLN C  385  THR C  397  1                                  13    
HELIX   61 AG7 SER C  421  GLY C  454  1                                  34    
HELIX   62 AG8 ASP C  460  MET C  469  5                                  10    
HELIX   63 AG9 GLY D   13  LYS D   23  1                                  11    
HELIX   64 AH1 TRP D   32  VAL D   55  1                                  24    
HELIX   65 AH2 SER D   66  GLY D   70  5                                   5    
HELIX   66 AH3 ALA D   82  GLY D   86  5                                   5    
HELIX   67 AH4 ASP D  100  LEU D  107  1                                   8    
HELIX   68 AH5 GLY D  108  GLY D  137  1                                  30    
HELIX   69 AH6 PRO D  140  LEU D  158  1                                  19    
HELIX   70 AH7 LEU D  158  GLN D  164  1                                   7    
HELIX   71 AH8 SER D  166  ALA D  170  5                                   5    
HELIX   72 AH9 VAL D  175  ASN D  190  1                                  16    
HELIX   73 AI1 TRP D  191  LEU D  193  5                                   3    
HELIX   74 AI2 ASN D  194  ASN D  220  1                                  27    
HELIX   75 AI3 SER D  245  PHE D  257  1                                  13    
HELIX   76 AI4 ASN D  263  ALA D  290  1                                  28    
HELIX   77 AI5 PHE D  298  ASP D  308  1                                  11    
HELIX   78 AI6 THR D  313  GLN D  334  1                                  22    
HELIX   79 AI7 PRO D  335  ASN D  338  5                                   4    
HELIX   80 AI8 PRO D  342  LEU D  346  5                                   5    
HELIX   81 AI9 PRO E    9  THR E   15  1                                   7    
HELIX   82 AJ1 SER E   16  THR E   40  1                                  25    
HELIX   83 AJ2 GLY E   41  GLY E   48  1                                   8    
HELIX   84 AJ3 GLU E   71  GLN E   82  1                                  12    
HELIX   85 AJ4 THR F   17  GLN F   41  1                                  25    
HELIX   86 AJ5 THR H    5  ARG H   12  1                                   8    
HELIX   87 AJ6 PRO H   13  SER H   16  5                                   4    
HELIX   88 AJ7 THR H   27  ASN H   50  1                                  24    
HELIX   89 AJ8 SER H   61  LEU H   65  5                                   5    
HELIX   90 AJ9 GLU I    2  SER I   25  1                                  24    
HELIX   91 AK1 GLY I   26  ARG I   30  5                                   5    
HELIX   92 AK2 PRO J    9  TYR J   33  1                                  25    
HELIX   93 AK3 PRO K   12  ILE K   17  5                                   6    
HELIX   94 AK4 PHE K   18  LEU K   25  1                                   8    
HELIX   95 AK5 VAL K   27  VAL K   43  1                                  17    
HELIX   96 AK6 ASN L   13  ASN L   37  1                                  25    
HELIX   97 AK7 LEU M    6  SER M   31  1                                  26    
HELIX   98 AK8 THR O    6  VAL O   11  1                                   6    
HELIX   99 AK9 GLY O   14  LYS O   18  5                                   5    
HELIX  100 AL1 GLU O  179  GLU O  181  5                                   3    
HELIX  101 AL2 LEU O  182  VAL O  187  1                                   6    
HELIX  102 AL3 GLU T    2  PHE T   23  1                                  22    
HELIX  103 AL4 ASN U   11  GLY U   18  1                                   8    
HELIX  104 AL5 THR U   19  GLU U   23  5                                   5    
HELIX  105 AL6 ASN U   31  TYR U   38  5                                   8    
HELIX  106 AL7 PRO U   43  ASN U   52  1                                  10    
HELIX  107 AL8 SER U   57  ILE U   64  5                                   8    
HELIX  108 AL9 THR U   68  LEU U   79  1                                  12    
HELIX  109 AM1 GLU U   88  GLU U   93  1                                   6    
HELIX  110 AM2 GLY U   94  ASP U   96  5                                   3    
HELIX  111 AM3 THR V   22  CYS V   37  1                                  16    
HELIX  112 AM4 CYS V   37  VAL V   42  1                                   6    
HELIX  113 AM5 GLY V   43  ILE V   45  5                                   3    
HELIX  114 AM6 ARG V   55  ALA V   62  1                                   8    
HELIX  115 AM7 ASN V   68  ASN V   78  1                                  11    
HELIX  116 AM8 SER V   94  ALA V   98  5                                   5    
HELIX  117 AM9 PHE V  101  ARG V  105  5                                   5    
HELIX  118 AN1 THR V  108  GLY V  127  1                                  20    
HELIX  119 AN2 ASP V  128  TRP V  130  5                                   3    
HELIX  120 AN3 GLY V  132  TYR V  137  5                                   6    
HELIX  121 AN4 ILE Y   19  ARG Y   42  1                                  24    
HELIX  122 AN5 THR X    4  ASP X   35  1                                  32    
HELIX  123 AN6 THR Z    2  SER Z   29  1                                  28    
HELIX  124 AN7 ASP Z   32  ASN Z   58  1                                  27    
HELIX  125 AN8 PHE Z   59  VAL Z   61  5                                   3    
HELIX  126 AN9 ASN a   12  THR a   22  1                                  11    
HELIX  127 AO1 VAL a   30  ALA a   55  1                                  26    
HELIX  128 AO2 SER a   70  GLY a   74  5                                   5    
HELIX  129 AO3 PRO a   95  ALA a   99  5                                   5    
HELIX  130 AO4 SER a  101  ASN a  108  1                                   8    
HELIX  131 AO5 GLY a  109  LEU a  137  1                                  29    
HELIX  132 AO6 TRP a  142  LEU a  159  1                                  18    
HELIX  133 AO7 LEU a  159  GLY a  166  1                                   8    
HELIX  134 AO8 SER a  167  GLY a  171  5                                   5    
HELIX  135 AO9 ILE a  176  ASN a  191  1                                  16    
HELIX  136 AP1 ILE a  192  MET a  194  5                                   3    
HELIX  137 AP2 HIS a  195  SER a  222  1                                  28    
HELIX  138 AP3 SER a  232  TYR a  237  5                                   6    
HELIX  139 AP4 ASN a  247  ILE a  259  1                                  13    
HELIX  140 AP5 PHE a  260  SER a  264  5                                   5    
HELIX  141 AP6 ASN a  267  ALA a  294  1                                  28    
HELIX  142 AP7 THR a  316  HIS a  332  1                                  17    
HELIX  143 AP8 PRO b    4  ILE b   13  5                                  10    
HELIX  144 AP9 ASP b   15  PHE b   45  1                                  31    
HELIX  145 AQ1 PRO b   54  GLN b   58  5                                   5    
HELIX  146 AQ2 VAL b   62  LEU b   69  1                                   8    
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  HIS b  157  1                                  24    
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  GLY b  259  1                                  27    
HELIX  154 AR1 PRO b  264  GLY b  269  1                                   6    
HELIX  155 AR2 THR b  271  SER b  277  1                                   7    
HELIX  156 AR3 SER b  278  SER b  294  1                                  17    
HELIX  157 AR4 THR b  297  ALA b  304  1                                   8    
HELIX  158 AR5 PRO b  306  ASP b  313  1                                   8    
HELIX  159 AR6 TYR b  314  GLY b  322  5                                   9    
HELIX  160 AR7 MET b  330  GLY b  335  1                                   6    
HELIX  161 AR8 SER b  391  GLY b  396  1                                   6    
HELIX  162 AR9 ASP b  413  ILE b  425  1                                  13    
HELIX  163 AS1 SER b  446  PHE b  475  1                                  30    
HELIX  164 AS2 ARG b  476  PHE b  479  5                                   4    
HELIX  165 AS3 SER b  487  VAL b  491  5                                   5    
HELIX  166 AS4 ASP b  501  ARG b  505  5                                   5    
HELIX  167 AS5 ASP c   27  GLY c   32  1                                   6    
HELIX  168 AS6 ALA c   34  ILE c   43  5                                  10    
HELIX  169 AS7 LEU c   45  PHE c   75  1                                  31    
HELIX  170 AS8 PRO c   80  GLN c   84  5                                   5    
HELIX  171 AS9 ILE c   87  LEU c   95  1                                   9    
HELIX  172 AT1 GLY c  100  GLU c  104  5                                   5    
HELIX  173 AT2 THR c  108  ARG c  135  1                                  28    
HELIX  174 AT3 ASP c  153  PHE c  182  1                                  30    
HELIX  175 AT4 ASP c  205  LYS c  215  1                                  11    
HELIX  176 AT5 GLY c  222  VAL c  227  5                                   6    
HELIX  177 AT6 ASN c  229  THR c  254  1                                  26    
HELIX  178 AT7 PHE c  257  PHE c  264  1                                   8    
HELIX  179 AT8 SER c  267  ASN c  293  1                                  27    
HELIX  180 AT9 PRO c  298  GLY c  303  1                                   6    
HELIX  181 AU1 THR c  305  GLY c  325  1                                  21    
HELIX  182 AU2 GLY c  353  TRP c  359  5                                   7    
HELIX  183 AU3 LEU c  366  PRO c  368  5                                   3    
HELIX  184 AU4 ASP c  376  ASP c  383  1                                   8    
HELIX  185 AU5 GLN c  385  THR c  397  1                                  13    
HELIX  186 AU6 SER c  421  GLY c  454  1                                  34    
HELIX  187 AU7 GLU c  464  MET c  469  5                                   6    
HELIX  188 AU8 GLY d   13  LYS d   23  1                                  11    
HELIX  189 AU9 VAL d   30  VAL d   55  1                                  26    
HELIX  190 AV1 SER d   66  GLY d   70  5                                   5    
HELIX  191 AV2 ALA d   82  GLY d   86  5                                   5    
HELIX  192 AV3 ASP d  100  LEU d  107  1                                   8    
HELIX  193 AV4 GLY d  108  GLY d  137  1                                  30    
HELIX  194 AV5 PRO d  140  LEU d  158  1                                  19    
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  ALA d  290  1                                  28    
HELIX  202 AW4 PHE d  298  ASP d  308  1                                  11    
HELIX  203 AW5 THR d  313  GLN d  334  1                                  22    
HELIX  204 AW6 PRO d  335  ASN d  338  5                                   4    
HELIX  205 AW7 PRO d  342  LEU d  346  5                                   5    
HELIX  206 AW8 PRO e    9  THR e   15  1                                   7    
HELIX  207 AW9 SER e   16  THR e   40  1                                  25    
HELIX  208 AX1 GLY e   41  GLY e   48  1                                   8    
HELIX  209 AX2 GLU e   71  GLN e   82  1                                  12    
HELIX  210 AX3 THR f   17  GLN f   41  1                                  25    
HELIX  211 AX4 THR h    5  ARG h   12  1                                   8    
HELIX  212 AX5 PRO h   13  SER h   16  5                                   4    
HELIX  213 AX6 THR h   27  ASN h   50  1                                  24    
HELIX  214 AX7 SER h   61  LEU h   65  5                                   5    
HELIX  215 AX8 GLU i    2  SER i   25  1                                  24    
HELIX  216 AX9 PRO j    9  ALA j   32  1                                  24    
HELIX  217 AY1 PHE k   18  LEU k   25  1                                   8    
HELIX  218 AY2 VAL k   27  VAL k   43  1                                  17    
HELIX  219 AY3 ASN l   13  ASN l   37  1                                  25    
HELIX  220 AY4 LEU m    6  SER m   31  1                                  26    
HELIX  221 AY5 THR o    6  VAL o   11  1                                   6    
HELIX  222 AY6 GLY o   14  LYS o   18  5                                   5    
HELIX  223 AY7 LYS o  178  GLU o  181  5                                   4    
HELIX  224 AY8 LEU o  182  VAL o  187  1                                   6    
HELIX  225 AY9 GLU t    2  PHE t   23  1                                  22    
HELIX  226 AZ1 ASN u   11  GLY u   18  1                                   8    
HELIX  227 AZ2 THR u   19  GLU u   23  5                                   5    
HELIX  228 AZ3 ASN u   31  TYR u   38  5                                   8    
HELIX  229 AZ4 PRO u   43  ASN u   52  1                                  10    
HELIX  230 AZ5 SER u   57  ILE u   64  5                                   8    
HELIX  231 AZ6 THR u   68  LEU u   79  1                                  12    
HELIX  232 AZ7 GLU u   88  GLU u   93  1                                   6    
HELIX  233 AZ8 GLY u   94  ASP u   96  5                                   3    
HELIX  234 AZ9 THR v   22  CYS v   37  1                                  16    
HELIX  235 BA1 CYS v   37  VAL v   42  1                                   6    
HELIX  236 BA2 GLY v   43  ILE v   45  5                                   3    
HELIX  237 BA3 ARG v   55  ALA v   62  1                                   8    
HELIX  238 BA4 ASN v   68  ASN v   78  1                                  11    
HELIX  239 BA5 PHE v  101  ARG v  105  5                                   5    
HELIX  240 BA6 THR v  108  GLY v  127  1                                  20    
HELIX  241 BA7 ASP v  128  TRP v  130  5                                   3    
HELIX  242 BA8 GLY v  132  TYR v  137  5                                   6    
HELIX  243 BA9 ILE y   19  ARG y   42  1                                  24    
HELIX  244 BB1 THR x    4  ASP x   35  1                                  32    
HELIX  245 BB2 THR z    2  SER z   29  1                                  28    
HELIX  246 BB3 ASP z   32  ASN z   58  1                                  27    
HELIX  247 BB4 PHE z   59  VAL z   61  5                                   3    
SHEET    1 AA1 2 ALA A  81  VAL A  82  0                                        
SHEET    2 AA1 2 LEU A 174  GLY A 175 -1  O  LEU A 174   N  VAL A  82           
SHEET    1 AA2 2 LEU A 297  ASN A 298  0                                        
SHEET    2 AA2 2 GLY C 402  SER C 403  1  O  GLY C 402   N  ASN A 298           
SHEET    1 AA3 2 LEU B   3  PRO B   4  0                                        
SHEET    2 AA3 2 VAL L  10  GLU L  11  1  O  GLU L  11   N  LEU B   3           
SHEET    1 AA4 2 MET B 166  VAL B 168  0                                        
SHEET    2 AA4 2 SER B 177  GLN B 179 -1  O  GLN B 179   N  MET B 166           
SHEET    1 AA5 2 ILE B 336  TRP B 340  0                                        
SHEET    2 AA5 2 PHE B 430  ASP B 433 -1  O  GLU B 431   N  GLN B 338           
SHEET    1 AA6 6 VAL B 377  ASP B 380  0                                        
SHEET    2 AA6 6 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA6 6 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA6 6 HIS B 343  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA6 6 THR B 398  TYR B 402 -1  O  THR B 398   N  ARG B 347           
SHEET    6 AA6 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1 AA7 2 LEU C 185  ASP C 187  0                                        
SHEET    2 AA7 2 ASP C 195  ARG C 197 -1  O  ARG C 197   N  LEU C 185           
SHEET    1 AA8 2 LEU C 341  ARG C 343  0                                        
SHEET    2 AA8 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1 AA9 2 ARG C 370  GLY C 371  0                                        
SHEET    2 AA9 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1 AB1 2 ALA D  77  VAL D  78  0                                        
SHEET    2 AB1 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1 AB2 2 TYR O  30  PRO O  31  0                                        
SHEET    2 AB2 2 SER O 135  ILE O 136 -1  O  ILE O 136   N  TYR O  30           
SHEET    1 AB310 PHE O  65  PRO O  67  0                                        
SHEET    2 AB310 TYR O  38  LYS O  53 -1  N  VAL O  52   O  VAL O  66           
SHEET    3 AB310 GLU O 232  PRO O 245 -1  O  GLU O 244   N  ARG O  39           
SHEET    4 AB310 GLU O 210  LEU O 220 -1  N  SER O 217   O  ILE O 235           
SHEET    5 AB310 LEU O 192  ASP O 205 -1  N  ASN O 200   O  THR O 214           
SHEET    6 AB310 ASP O 141  PRO O 149 -1  N  PHE O 142   O  LEU O 199           
SHEET    7 AB310 VAL O 126  SER O 128 -1  N  SER O 128   O  LYS O 143           
SHEET    8 AB310 LEU O  93  ILE O 101 -1  N  PHE O  95   O  ALA O 127           
SHEET    9 AB310 LEU O  78  VAL O  87 -1  N  GLN O  82   O  ASP O  99           
SHEET   10 AB310 TYR O  38  LYS O  53 -1  N  LEU O  45   O  LEU O  78           
SHEET    1 AB4 3 LYS O  69  LEU O  70  0                                        
SHEET    2 AB4 3 PHE O 103  GLN O 109 -1  O  GLN O 109   N  LYS O  69           
SHEET    3 AB4 3 ARG O 115  THR O 121 -1  O  ILE O 116   N  VAL O 108           
SHEET    1 AB5 2 ILE U  25  ASP U  26  0                                        
SHEET    2 AB5 2 PHE U  82  THR U  83  1  O  THR U  83   N  ILE U  25           
SHEET    1 AB6 2 THR V   9  PRO V  11  0                                        
SHEET    2 AB6 2 THR V  18  THR V  20 -1  O  ILE V  19   N  VAL V  10           
SHEET    1 AB7 2 ALA a  81  VAL a  82  0                                        
SHEET    2 AB7 2 LEU a 174  GLY a 175 -1  O  LEU a 174   N  VAL a  82           
SHEET    1 AB8 2 LEU a 297  ASN a 298  0                                        
SHEET    2 AB8 2 GLY c 402  SER c 403  1  O  GLY c 402   N  ASN a 298           
SHEET    1 AB9 2 MET b 166  VAL b 168  0                                        
SHEET    2 AB9 2 SER b 177  GLN b 179 -1  O  GLN b 179   N  MET b 166           
SHEET    1 AC1 6 VAL b 377  ASP b 380  0                                        
SHEET    2 AC1 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC1 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC1 6 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC1 6 THR b 398  TYR b 402 -1  O  THR b 398   N  ARG b 347           
SHEET    6 AC1 6 THR b 410  PHE b 411 -1  O  PHE b 411   N  VAL b 399           
SHEET    1 AC2 5 VAL b 377  ASP b 380  0                                        
SHEET    2 AC2 5 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC2 5 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC2 5 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC2 5 ILE b 429  ASP b 433 -1  O  GLU b 431   N  GLN b 338           
SHEET    1 AC3 2 LEU c 185  ASP c 187  0                                        
SHEET    2 AC3 2 ASP c 195  ARG c 197 -1  O  ARG c 197   N  LEU c 185           
SHEET    1 AC4 2 LEU c 341  ARG c 343  0                                        
SHEET    2 AC4 2 ILE c 349  PHE c 351 -1  O  ILE c 350   N  MET c 342           
SHEET    1 AC5 2 ARG c 370  GLY c 371  0                                        
SHEET    2 AC5 2 GLY c 374  LEU c 375 -1  O  GLY c 374   N  GLY c 371           
SHEET    1 AC6 2 ALA d  77  VAL d  78  0                                        
SHEET    2 AC6 2 PHE d 173  GLY d 174 -1  O  PHE d 173   N  VAL d  78           
SHEET    1 AC7 2 TYR o  30  PRO o  31  0                                        
SHEET    2 AC7 2 SER o 135  ILE o 136 -1  O  ILE o 136   N  TYR o  30           
SHEET    1 AC810 PHE o  65  PRO o  67  0                                        
SHEET    2 AC810 TYR o  38  LYS o  53 -1  N  VAL o  52   O  VAL o  66           
SHEET    3 AC810 GLU o 232  PRO o 245 -1  O  GLN o 236   N  THR o  48           
SHEET    4 AC810 GLU o 210  LEU o 220 -1  N  ILE o 211   O  ALA o 241           
SHEET    5 AC810 LEU o 192  ASP o 205 -1  N  GLN o 196   O  GLU o 218           
SHEET    6 AC810 ASP o 141  PRO o 149 -1  N  PHE o 142   O  LEU o 199           
SHEET    7 AC810 VAL o 126  SER o 128 -1  N  SER o 128   O  LYS o 143           
SHEET    8 AC810 LEU o  93  ILE o 101 -1  N  PHE o  95   O  ALA o 127           
SHEET    9 AC810 LEU o  78  VAL o  87 -1  N  GLU o  84   O  VAL o  96           
SHEET   10 AC810 TYR o  38  LYS o  53 -1  N  LEU o  45   O  LEU o  78           
SHEET    1 AC9 3 LYS o  69  LEU o  70  0                                        
SHEET    2 AC9 3 PHE o 103  GLN o 109 -1  O  GLN o 109   N  LYS o  69           
SHEET    3 AC9 3 ARG o 115  THR o 121 -1  O  ILE o 116   N  VAL o 108           
SHEET    1 AD1 2 ILE u  25  ASP u  26  0                                        
SHEET    2 AD1 2 PHE u  82  THR u  83  1  O  THR u  83   N  ILE u  25           
SHEET    1 AD2 2 THR v   9  PRO v  11  0                                        
SHEET    2 AD2 2 THR v  18  THR v  20 -1  O  ILE v  19   N  VAL v  10           
SSBOND   1 CYS O   19    CYS O   44                          1555   1555  2.03  
SSBOND   2 CYS o   19    CYS o   44                          1555   1555  2.03  
LINK         OD1 ASP A 170                CA1  OEX A 601     1555   1555  2.89  
LINK         OD2 ASP A 170                MN4  OEX A 601     1555   1555  2.32  
LINK         OE2 GLU A 189                MN1  OEX A 601     1555   1555  2.21  
LINK         NE2 HIS A 215                FE   FE2 A 602     1555   1555  2.31  
LINK         NE2 HIS A 272                FE   FE2 A 602     1555   1555  2.42  
LINK         NE2 HIS A 332                MN1  OEX A 601     1555   1555  2.33  
LINK         OE1 GLU A 333                MN3  OEX A 601     1555   1555  2.15  
LINK         OE2 GLU A 333                MN4  OEX A 601     1555   1555  2.24  
LINK         OD1 ASP A 342                MN2  OEX A 601     1555   1555  2.26  
LINK         OD2 ASP A 342                MN1  OEX A 601     1555   1555  2.28  
LINK         O   ALA A 344                CA1  OEX A 601     1555   1555  2.90  
LINK         OXT ALA A 344                MN2  OEX A 601     1555   1555  2.29  
LINK         OD1 ASN C  39                MG   CLA C 511     1555   1555  2.61  
LINK         OE1 GLU C 354                MN2  OEX A 601     1555   1555  2.26  
LINK         OE2 GLU C 354                MN3  OEX A 601     1555   1555  2.26  
LINK         NE2 HIS D 214                FE   FE2 A 602     1555   1555  2.47  
LINK         NE2 HIS D 268                FE   FE2 A 602     1555   1555  2.45  
LINK         NE2 HIS E  23                FE   HEM E 103     1555   1555  2.42  
LINK         NE2 HIS F  24                FE   HEM E 103     1555   1555  2.15  
LINK         O   ALA J  34                MG    MG J 101     1555   1555  2.03  
LINK         O   LEU J  36                MG    MG J 101     1555   1555  2.68  
LINK         O   THR O 138                CA    CA O 301     1555   1555  2.78  
LINK         OD1 ASN O 200                CA    CA O 301     1555   1555  2.78  
LINK         NE2 HIS V  41                FE   HEM V 201     1555   1555  2.18  
LINK         NE2 HIS V  92                FE   HEM V 201     1555   1555  2.39  
LINK         OD1 ASP a 170                CA1  OEX a 601     1555   1555  2.98  
LINK         OD2 ASP a 170                CA1  OEX a 601     1555   1555  3.11  
LINK         OD2 ASP a 170                MN4  OEX a 601     1555   1555  2.53  
LINK         OE2 GLU a 189                MN1  OEX a 601     1555   1555  2.08  
LINK         NE2 HIS a 215                FE   FE2 a 602     1555   1555  2.28  
LINK         NE2 HIS a 272                FE   FE2 a 602     1555   1555  2.39  
LINK         NE2 HIS a 332                MN1  OEX a 601     1555   1555  2.43  
LINK         OE1 GLU a 333                MN3  OEX a 601     1555   1555  2.26  
LINK         OE2 GLU a 333                MN4  OEX a 601     1555   1555  2.53  
LINK         OD1 ASP a 342                MN2  OEX a 601     1555   1555  2.32  
LINK         OD2 ASP a 342                MN1  OEX a 601     1555   1555  2.26  
LINK         O   ALA a 344                CA1  OEX a 601     1555   1555  2.85  
LINK         OXT ALA a 344                MN2  OEX a 601     1555   1555  2.24  
LINK         OD1 ASN c  39                MG   CLA c 511     1555   1555  2.76  
LINK         OE1 GLU c 354                MN2  OEX a 601     1555   1555  2.15  
LINK         OE2 GLU c 354                MN3  OEX a 601     1555   1555  2.31  
LINK         NE2 HIS d 214                FE   FE2 a 602     1555   1555  2.41  
LINK         NE2 HIS d 268                FE   FE2 a 602     1555   1555  2.42  
LINK         NE2 HIS e  23                FE   HEM e 102     1555   1555  2.30  
LINK         NE2 HIS f  24                FE   HEM e 102     1555   1555  2.39  
LINK         O   ARG f  45                CA    CA f 102     1555   1555  2.65  
LINK         OXT ARG f  45                CA    CA f 102     1555   1555  2.67  
LINK         O   GLY j  31                MG    MG j 102     1555   1555  2.07  
LINK         O   ALA j  34                MG    MG j 102     1555   1555  1.90  
LINK         O   LEU j  36                MG    MG j 102     1555   1555  2.80  
LINK         O   THR o 138                CA    CA o 301     1555   1555  2.41  
LINK         OD1 ASN o 200                CA    CA o 301     1555   1555  2.63  
LINK         O   VAL o 201                CA    CA o 301     1555   1555  2.76  
LINK         NE2 HIS v  41                FE   HEM v 201     1555   1555  2.38  
LINK         NE2 HIS v  92                FE   HEM v 201     1555   1555  2.32  
LINK        FE   FE2 A 602                 O1  BCT A 605     1555   1555  2.55  
LINK        FE   FE2 A 602                 O2  BCT A 605     1555   1555  2.51  
LINK        FE   FE2 a 602                 O1  BCT a 605     1555   1555  2.75  
LINK        FE   FE2 a 602                 O2  BCT a 605     1555   1555  2.69  
LINK         O4  LMG j 101                MG    MG j 102     1555   1555  2.44  
CISPEP   1 TYR U   42    PRO U   43          0         2.44                     
CISPEP   2 ALA U   53    PRO U   54          0         1.78                     
CISPEP   3 THR V   63    PRO V   64          0        -9.77                     
CISPEP   4 TYR u   42    PRO u   43          0         4.11                     
CISPEP   5 ALA u   53    PRO u   54          0         1.79                     
CISPEP   6 THR v   63    PRO v   64          0        -8.88                     
SITE     1 AC1  9 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 AC1  9 HIS A 337  ASP A 342  ALA A 344  GLU C 354                    
SITE     3 AC1  9 ARG C 357                                                     
SITE     1 AC2  5 HIS A 215  HIS A 272  BCT A 605  HIS D 214                    
SITE     2 AC2  5 HIS D 268                                                     
SITE     1 AC3  2 HIS A 332  GLU A 333                                          
SITE     1 AC4  3 PHE A 339  GLU C 354  THR C 355                               
SITE     1 AC5  7 GLU A 244  TYR A 246  HIS A 272  FE2 A 602                    
SITE     2 AC5  7 HIS D 214  TYR D 244  HIS D 268                               
SITE     1 AC6 20 PHE A 119  TYR A 147  PRO A 150  SER A 153                    
SITE     2 AC6 20 VAL A 157  MET A 183  PHE A 186  GLN A 187                    
SITE     3 AC6 20 LEU A 193  HIS A 198  PHE A 206  ALA A 286                    
SITE     4 AC6 20 ALA A 287  ILE A 290  CLA A 607  PHO A 608                    
SITE     5 AC6 20 LEU D 205  CLA D 402  CLA D 403  PHE T  17                    
SITE     1 AC7 17 GLN A 199  VAL A 202  ALA A 203  GLY A 207                    
SITE     2 AC7 17 LEU A 210  TRP A 278  CLA A 606  PL9 A 611                    
SITE     3 AC7 17 DGD C 517  PHE D 157  VAL D 175  ILE D 178                    
SITE     4 AC7 17 PHE D 179  LEU D 182  PHO D 401  CLA D 403                    
SITE     5 AC7 17 LMG D 408                                                     
SITE     1 AC8 16 LEU A  41  ALA A  44  THR A  45  TYR A 126                    
SITE     2 AC8 16 GLN A 130  ALA A 146  TYR A 147  PRO A 150                    
SITE     3 AC8 16 VAL A 283  CLA A 606  LEU D 205  LEU D 209                    
SITE     4 AC8 16 ILE D 213  TRP D 253  PHE D 257  CLA D 402                    
SITE     1 AC9 17 ILE A  36  PRO A  39  THR A  40  PHE A  93                    
SITE     2 AC9 17 PRO A  95  ILE A  96  TRP A  97  LEU A 114                    
SITE     3 AC9 17 HIS A 118  LEU A 121  BCR A 610  LMG A 613                    
SITE     4 AC9 17 VAL I   8  TYR I   9  VAL I  12  PHE I  15                    
SITE     5 AC9 17 BCR I 101                                                     
SITE     1 AD1  8 TRP A  20  LEU A  42  ALA A  43  ILE A  50                    
SITE     2 AD1  8 ILE A  96  TRP A 105  LEU A 106  CLA A 609                    
SITE     1 AD2 22 PHE A 211  MET A 214  HIS A 215  LEU A 218                    
SITE     2 AD2 22 HIS A 252  PHE A 255  SER A 264  PHE A 265                    
SITE     3 AD2 22 LEU A 271  PHE A 274  CLA A 607  VAL D  30                    
SITE     4 AD2 22 PRO D  39  ALA D  41  TYR D  42  LEU D  45                    
SITE     5 AD2 22 PHO D 401  LHG E 102  ALA F  22  THR F  25                    
SITE     6 AD2 22 THR X  24  SQD X 101                                          
SITE     1 AD3 13 ASN A 267  SER A 270  PHE A 273  TRP A 278                    
SITE     2 AD3 13 GLY A 282  LHG A 615  GLN C  28  ALA C  34                    
SITE     3 AD3 13 TRP C  36  CLA C 508  PHE D 232  ARG D 233                    
SITE     4 AD3 13 PHE K  37                                                     
SITE     1 AD4 13 PHE A  93  TRP A  97  GLU A  98  LEU A 121                    
SITE     2 AD4 13 CLA A 609  LEU C 214  PHE C 218  GLU C 221                    
SITE     3 AD4 13 TRP C 223  CLA C 505  DGD C 515  LYS I   5                    
SITE     4 AD4 13 TYR I   9                                                     
SITE     1 AD5 10 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 AD5 10 CLA D 402  BCR T 101  TRP b 113  TYR b 117                    
SITE     3 AD5 10 CLA b 608  BCR b 621                                          
SITE     1 AD6 17 ARG A 140  TRP A 142  PHE A 273  ALA A 276                    
SITE     2 AD6 17 SQD A 612  TRP C  36  TRP C 443  ARG C 447                    
SITE     3 AD6 17 CLA C 504  CLA C 508  CLA C 510  GLU D 219                    
SITE     4 AD6 17 ASN D 220  ALA D 229  SER D 230  THR D 231                    
SITE     5 AD6 17 PHE D 232                                                     
SITE     1 AD7  1 GLU O 181                                                     
SITE     1 AD8  5 TRP B 185  PRO B 187  PHE B 190  PHE H  41                    
SITE     2 AD8  5 BCR H 101                                                     
SITE     1 AD9 20 TRP B 185  GLY B 189  PHE B 190  PRO B 192                    
SITE     2 AD9 20 GLY B 197  ALA B 200  HIS B 201  ALA B 204                    
SITE     3 AD9 20 ALA B 205  VAL B 208  PHE B 246  PHE B 247                    
SITE     4 AD9 20 PHE B 250  CLA B 604  PHE H  38  PHE H  41                    
SITE     5 AD9 20 ILE H  45  LEU H  46  TYR H  49  DGD H 102                    
SITE     1 AE1 18 ARG B  68  LEU B  69  ALA B 146  LEU B 149                    
SITE     2 AE1 18 CYS B 150  PHE B 153  HIS B 201  HIS B 202                    
SITE     3 AE1 18 VAL B 252  THR B 262  CLA B 603  CLA B 605                    
SITE     4 AE1 18 CLA B 606  CLA B 607  CLA B 610  CLA B 611                    
SITE     5 AE1 18 MET H  35  LEU H  39                                          
SITE     1 AE2 18 TRP B  33  PHE B  65  ARG B  68  LEU B 148                    
SITE     2 AE2 18 LEU B 149  VAL B 245  ALA B 249  VAL B 252                    
SITE     3 AE2 18 PHE B 451  HIS B 455  PHE B 458  ALA B 459                    
SITE     4 AE2 18 CLA B 604  CLA B 606  CLA B 608  CLA B 613                    
SITE     5 AE2 18 CLA B 614  CLA B 616                                          
SITE     1 AE3 20 THR B  27  VAL B  30  ALA B  34  VAL B  62                    
SITE     2 AE3 20 PHE B  65  MET B  66  ARG B  68  LEU B  69                    
SITE     3 AE3 20 HIS B 100  LEU B 103  LEU B 143  ALA B 146                    
SITE     4 AE3 20 CYS B 150  ALA B 205  GLY B 209  CLA B 604                    
SITE     5 AE3 20 CLA B 605  CLA B 607  CLA B 611  BCR B 620                    
SITE     1 AE4 16 GLY B  70  VAL B  71  PHE B  90  TRP B  91                    
SITE     2 AE4 16 VAL B  96  VAL B 102  GLY B 152  PHE B 153                    
SITE     3 AE4 16 PHE B 156  HIS B 157  PHE B 162  PRO B 164                    
SITE     4 AE4 16 CLA B 604  CLA B 606  BCR B 620  SQD a 614                    
SITE     1 AE5 19 TRP B  33  TYR B  40  GLN B  58  GLY B  59                    
SITE     2 AE5 19 MET B  60  PHE B  61  LEU B 324  THR B 327                    
SITE     3 AE5 19 GLY B 328  PRO B 329  TRP B 450  PHE B 451                    
SITE     4 AE5 19 CLA B 605  BCR B 618  BCR B 619  LMG B 621                    
SITE     5 AE5 19 LHG D 406  PHE M  14  BCR t 101                               
SITE     1 AE6 13 THR B 236  SER B 239  SER B 240  ALA B 243                    
SITE     2 AE6 13 PHE B 246  PHE B 463  HIS B 466  ILE B 467                    
SITE     3 AE6 13 CLA B 611  ILE D 123  LEU H  39  LEU H  43                    
SITE     4 AE6 13 DGD H 102                                                     
SITE     1 AE7 16 PHE B 139  VAL B 208  ALA B 212  PHE B 215                    
SITE     2 AE7 16 HIS B 216  VAL B 219  ARG B 220  PRO B 221                    
SITE     3 AE7 16 LEU B 229  CLA B 604  CLA B 611  THR H  27                    
SITE     4 AE7 16 MET H  31  PHE H  34  LEU H  43  BCR H 101                    
SITE     1 AE8 20 LEU B 135  MET B 138  PHE B 139  HIS B 142                    
SITE     2 AE8 20 LEU B 143  LEU B 145  ALA B 146  LEU B 229                    
SITE     3 AE8 20 MET B 231  THR B 236  VAL B 237  SER B 240                    
SITE     4 AE8 20 SER B 241  CLA B 604  CLA B 606  CLA B 609                    
SITE     5 AE8 20 CLA B 610  CLA B 613  CLA B 616  BCR H 101                    
SITE     1 AE9 19 TRP B   5  TYR B   6  ARG B   7  VAL B   8                    
SITE     2 AE9 19 HIS B   9  THR B  10  LEU B 238  ILE B 242                    
SITE     3 AE9 19 LEU B 461  PHE B 462  PHE B 464  GLY B 465                    
SITE     4 AE9 19 TRP B 468  HIS B 469  CLA B 613  CLA B 614                    
SITE     5 AE9 19 CLA B 615  BCR B 619  LHG D 406                               
SITE     1 AF1 16 HIS B   9  LEU B  19  ALA B  22  HIS B  23                    
SITE     2 AF1 16 HIS B  26  THR B  27  ILE B 234  LEU B 238                    
SITE     3 AF1 16 SER B 241  VAL B 245  CLA B 605  CLA B 611                    
SITE     4 AF1 16 CLA B 612  CLA B 614  CLA B 615  CLA B 616                    
SITE     1 AF2 12 HIS B   9  HIS B  26  VAL B  30  TRP B  33                    
SITE     2 AF2 12 PHE B 462  CLA B 605  CLA B 612  CLA B 613                    
SITE     3 AF2 12 CLA B 615  BCR B 619  LMG B 621  PHE M  14                    
SITE     1 AF3 14 VAL B   8  HIS B   9  ALA B  22  TRP B 115                    
SITE     2 AF3 14 CLA B 612  CLA B 613  CLA B 614  BCR B 618                    
SITE     3 AF3 14 LMG B 621  SQD B 622  VAL L  10  PHE M  21                    
SITE     4 AF3 14 SQD l 101  PHE t   8                                          
SITE     1 AF4 15 ILE B  20  HIS B  23  LEU B  24  LEU B 133                    
SITE     2 AF4 15 MET B 138  ILE B 141  HIS B 142  LEU B 145                    
SITE     3 AF4 15 CLA B 605  CLA B 611  CLA B 613  CLA B 617                    
SITE     4 AF4 15 BCR B 620  LEU H  14  ASN H  15                               
SITE     1 AF5 10 LEU B  24  ALA B 110  TRP B 113  HIS B 114                    
SITE     2 AF5 10 LEU B 120  CLA B 616  BCR B 620  THR H   5                    
SITE     3 AF5 10 LEU H   7  GLY H   8                                          
SITE     1 AF6 12 MET B  25  LEU B  29  PHE B 108  TRP B 115                    
SITE     2 AF6 12 CLA B 608  CLA B 615  BCR B 619  LMG B 621                    
SITE     3 AF6 12 SQD B 622  SQD l 101  PHE t  19  BCR t 101                    
SITE     1 AF7 15 LEU B  29  GLY B  32  TRP B  33  SER B  36                    
SITE     2 AF7 15 ILE B 101  VAL B 102  SER B 104  GLY B 105                    
SITE     3 AF7 15 CLA B 608  CLA B 612  CLA B 614  BCR B 618                    
SITE     4 AF7 15 LMG B 621  SQD l 101  BCR t 101                               
SITE     1 AF8  8 LEU B 106  TRP B 113  CLA B 606  CLA B 607                    
SITE     2 AF8  8 CLA B 616  CLA B 617  SQD a 614  PHE t  23                    
SITE     1 AF9 13 TYR B  40  THR B 327  GLY B 328  PRO B 329                    
SITE     2 AF9 13 ALA B 454  VAL B 457  CLA B 608  CLA B 614                    
SITE     3 AF9 13 CLA B 615  BCR B 618  BCR B 619  LHG L 101                    
SITE     4 AF9 13 ASN M   4                                                     
SITE     1 AG1 15 ARG B  18  ALA B  28  LEU B  29  SER B 104                    
SITE     2 AG1 15 PHE B 108  TRP B 115  CLA B 615  BCR B 618                    
SITE     3 AG1 15 ASN L   4  ARG L   7  ARG l  14  SQD l 101                    
SITE     4 AG1 15 LEU m  16  PHE t  19  PHE t  23                               
SITE     1 AG2 16 LEU C 168  GLY C 171  ALA C 172  LEU C 175                    
SITE     2 AG2 16 LEU C 185  VAL C 233  HIS C 237  ILE C 240                    
SITE     3 AG2 16 MET C 282  VAL C 296  TYR C 297  CLA C 502                    
SITE     4 AG2 16 CLA C 503  CLA C 506  CLA C 507  BCR I 101                    
SITE     1 AG3 16 HIS C  91  LYS C 178  PHE C 182  LEU C 279                    
SITE     2 AG3 16 MET C 282  ALA C 286  VAL C 290  TYR C 297                    
SITE     3 AG3 16 LEU C 426  HIS C 430  LEU C 433  PHE C 437                    
SITE     4 AG3 16 CLA C 501  CLA C 503  CLA C 504  CLA C 510                    
SITE     1 AG4 11 ILE C  60  VAL C  61  THR C  68  LEU C  88                    
SITE     2 AG4 11 HIS C  91  LEU C  95  HIS C 118  CLA C 501                    
SITE     3 AG4 11 CLA C 502  CLA C 512  LMG C 519                               
SITE     1 AG5 15 LHG A 615  TRP C  63  MET C  67  PHE C  70                    
SITE     2 AG5 15 GLN C  84  GLY C  85  TRP C 425  SER C 429                    
SITE     3 AG5 15 CLA C 502  CLA C 510  DGD C 516  DGD C 517                    
SITE     4 AG5 15 LMG C 518  PRO K  26  VAL K  30                               
SITE     1 AG6 16 PHE A  33  MET A 127  TRP A 131  LMG A 613                    
SITE     2 AG6 16 PHE C 264  SER C 273  TYR C 274  MET C 281                    
SITE     3 AG6 16 HIS C 441  LEU C 442  ALA C 445  ARG C 449                    
SITE     4 AG6 16 CLA C 507  DGD C 515  VAL I  16  BCR I 101                    
SITE     1 AG7 15 LEU C 161  LEU C 165  LEU C 213  ILE C 243                    
SITE     2 AG7 15 TRP C 250  HIS C 251  THR C 254  THR C 255                    
SITE     3 AG7 15 PRO C 256  PHE C 257  TRP C 259  PHE C 264                    
SITE     4 AG7 15 CLA C 501  CLA C 507  BCR I 101                               
SITE     1 AG8 18 MET C 157  THR C 158  LEU C 161  HIS C 164                    
SITE     2 AG8 18 LEU C 168  CYS C 244  TRP C 259  TRP C 266                    
SITE     3 AG8 18 TYR C 271  TYR C 274  SER C 275  LEU C 279                    
SITE     4 AG8 18 MET C 282  CLA C 501  CLA C 505  CLA C 506                    
SITE     5 AG8 18 CLA C 509  BCR I 101                                          
SITE     1 AG9 21 SQD A 612  LHG A 615  TRP C  36  ALA C  37                    
SITE     2 AG9 21 GLY C  38  ASN C  39  ALA C  40  GLU C 269                    
SITE     3 AG9 21 LEU C 276  PHE C 436  PHE C 437  GLY C 440                    
SITE     4 AG9 21 TRP C 443  HIS C 444  ARG C 447  CLA C 509                    
SITE     5 AG9 21 CLA C 510  CLA C 511  DGD C 517  LMG C 518                    
SITE     6 AG9 21 VAL K  30                                                     
SITE     1 AH1 16 ASN C  39  LEU C  49  HIS C  53  HIS C  56                    
SITE     2 AH1 16 TYR C 149  MET C 157  ILE C 160  HIS C 164                    
SITE     3 AH1 16 TYR C 271  LEU C 272  SER C 275  CLA C 507                    
SITE     4 AH1 16 CLA C 508  CLA C 510  CLA C 511  CLA C 512                    
SITE     1 AH2 13 LHG A 615  ASN C  39  HIS C  56  PHE C 436                    
SITE     2 AH2 13 PHE C 437  CLA C 502  CLA C 504  CLA C 508                    
SITE     3 AH2 13 CLA C 509  CLA C 511  PRO K  29  VAL K  30                    
SITE     4 AH2 13 LEU K  33                                                     
SITE     1 AH3 26 ARG C  26  TRP C  35  GLY C  38  ASN C  39                    
SITE     2 AH3 26 ARG C  41  LEU C  42  LEU C  45  LYS C  48                    
SITE     3 AH3 26 ALA C  52  ALA C 123  PHE C 127  ILE C 134                    
SITE     4 AH3 26 CLA C 508  CLA C 509  CLA C 510  PHE K  37                    
SITE     5 AH3 26 TRP K  39  GLN K  40  BCR K 102  LEU Y  39                    
SITE     6 AH3 26 ASN Y  45  LEU Y  46  MET Z  19  VAL Z  20                    
SITE     7 AH3 26 VAL Z  23  ALA Z  28                                          
SITE     1 AH4 12 LEU C  50  HIS C  53  PHE C 146  PHE C 147                    
SITE     2 AH4 12 PHE C 163  HIS C 164  VAL C 167  ILE C 170                    
SITE     3 AH4 12 GLY C 171  CLA C 503  CLA C 509  CLA C 513                    
SITE     1 AH5 10 LEU C  50  VAL C 124  GLY C 128  TYR C 131                    
SITE     2 AH5 10 HIS C 132  LEU C 140  TYR C 143  CLA C 512                    
SITE     3 AH5 10 BCR C 514  LMG Z 101                                          
SITE     1 AH6  9 PHE C 112  VAL C 116  ILE C 120  SER C 121                    
SITE     2 AH6  9 VAL C 124  CLA C 513  LMG C 519  TYR K  15                    
SITE     3 AH6  9 ASN Z  58                                                     
SITE     1 AH7 20 LEU A  91  PHE A 155  ILE A 163  LMG A 613                    
SITE     2 AH7 20 PRO C 217  GLY C 219  GLY C 220  GLY C 222                    
SITE     3 AH7 20 TRP C 223  VAL C 227  CYS C 288  PHE C 292                    
SITE     4 AH7 20 ASN C 293  ASN C 294  THR C 295  ASP C 360                    
SITE     5 AH7 20 PHE C 361  ARG C 362  LEU C 438  CLA C 505                    
SITE     1 AH8 14 PHE A 197  LEU A 297  GLU C  83  GLN C  84                    
SITE     2 AH8 14 GLY C  85  SER C 406  ASN C 418  VAL C 420                    
SITE     3 AH8 14 TRP C 425  CLA C 504  DGD C 517  LMG C 518                    
SITE     4 AH8 14 PHE J  29  TYR J  33                                          
SITE     1 AH9 25 GLN A 199  LEU A 200  ALA A 203  TRP A 278                    
SITE     2 AH9 25 ASN A 301  PHE A 302  SER A 305  CLA A 607                    
SITE     3 AH9 25 ASN C 405  VAL C 407  ASN C 415  SER C 416                    
SITE     4 AH9 25 VAL C 417  ASN C 418  CLA C 504  CLA C 508                    
SITE     5 AH9 25 DGD C 516  LMG D 408  PHE J  29  ALA J  32                    
SITE     6 AH9 25 TYR J  33  GLY J  37  SER J  38  SER J  39                    
SITE     7 AH9 25 LEU J  40                                                     
SITE     1 AI1  7 HIS C  74  GLN C  84  CLA C 504  CLA C 508                    
SITE     2 AI1  7 DGD C 516  ASP K  23  VAL K  27                               
SITE     1 AI2  9 TRP C  97  ASP C 107  VAL C 113  VAL C 117                    
SITE     2 AI2  9 SER C 121  CLA C 503  BCR C 514  ASN Z  58                    
SITE     3 AI2  9 PHE Z  59                                                     
SITE     1 AI3 22 LEU A 210  MET A 214  PHE A 255  CLA A 607                    
SITE     2 AI3 22 PL9 A 611  ALA D  41  LEU D  45  TRP D  48                    
SITE     3 AI3 22 ILE D 114  GLY D 118  GLY D 121  LEU D 122                    
SITE     4 AI3 22 PHE D 125  GLN D 129  ASN D 142  PHE D 146                    
SITE     5 AI3 22 ALA D 148  PRO D 149  PHE D 153  GLY D 174                    
SITE     6 AI3 22 LEU D 279  CLA D 403                                          
SITE     1 AI4 16 MET A 172  ILE A 176  THR A 179  MET A 183                    
SITE     2 AI4 16 CLA A 606  PHO A 608  SQD A 614  MET D 198                    
SITE     3 AI4 16 VAL D 201  ALA D 202  LEU D 205  GLY D 206                    
SITE     4 AI4 16 CLA D 403  PL9 D 405  LHG D 407  LHG L 101                    
SITE     1 AI5 22 MET A 183  PHE A 206  CLA A 606  CLA A 607                    
SITE     2 AI5 22 LEU D  45  LEU D 122  PRO D 149  VAL D 152                    
SITE     3 AI5 22 PHE D 153  VAL D 156  LEU D 182  PHE D 185                    
SITE     4 AI5 22 GLN D 186  TRP D 191  THR D 192  HIS D 197                    
SITE     5 AI5 22 GLY D 200  SER D 282  ALA D 283  VAL D 286                    
SITE     6 AI5 22 PHO D 401  CLA D 402                                          
SITE     1 AI6 16 ILE D  35  PRO D  39  CYS D  40  LEU D  43                    
SITE     2 AI6 16 LEU D  89  LEU D  90  LEU D  91  LEU D  92                    
SITE     3 AI6 16 TRP D  93  TRP D 104  THR D 112  PHE D 113                    
SITE     4 AI6 16 HIS D 117  BCR F 101  GLY X  13  LEU X  14                    
SITE     1 AI7 20 PHE A  52  ILE A  53  ILE A  77  MET D 199                    
SITE     2 AI7 20 HIS D 214  THR D 217  TRP D 253  ALA D 260                    
SITE     3 AI7 20 PHE D 261  LEU D 267  PHE D 270  GLY D 278                    
SITE     4 AI7 20 CLA D 402  LHG D 407  LEU L  23  VAL L  26                    
SITE     5 AI7 20 LEU L  29  LEU L  30  LHG L 101  PHE T  10                    
SITE     1 AI8 15 SER A 232  ASN A 234  TRP B   5  TYR B   6                    
SITE     2 AI8 15 ARG B   7  LEU B 461  PHE B 464  TRP B 468                    
SITE     3 AI8 15 CLA B 608  CLA B 612  TYR D 141  PHE D 269                    
SITE     4 AI8 15 LEU D 272  THR D 277  LHG L 101                               
SITE     1 AI9 21 MET A  37  ARG A 129  ILE D 256  PHE D 257                    
SITE     2 AI9 21 ILE D 259  ALA D 260  PHE D 261  SER D 262                    
SITE     3 AI9 21 ASN D 263  TRP D 266  PHE D 270  CLA D 402                    
SITE     4 AI9 21 PL9 D 405  ASN L  13  THR L  15  SER L  16                    
SITE     5 AI9 21 TYR L  18  LEU L  19  LHG L 101  PHE T  17                    
SITE     6 AI9 21 ALA T  20                                                     
SITE     1 AJ1 16 CLA A 607  DGD C 517  TYR D  67  GLY D  70                    
SITE     2 AJ1 16 CYS D  71  ASN D  72  PHE D  73  THR F  30                    
SITE     3 AJ1 16 MET F  40  GLN F  41  BCR F 101  PHE J  28                    
SITE     4 AJ1 16 GLY J  31  ALA J  32  LEU J  36   MG J 101                    
SITE     1 AJ2  6 GLY D  99  ASP D 100  THR D 102  PHE E  37                    
SITE     2 AJ2  6 ASP E  45  BCR F 101                                          
SITE     1 AJ3 12 LEU A 258  PHE A 260  TYR A 262  PL9 A 611                    
SITE     2 AJ3 12 PHE D  27  LEU D  37  THR E   4  THR E   5                    
SITE     3 AJ3 12 GLU E   7  PRO E   9  PHE E  10  SER E  11                    
SITE     1 AJ4 14 ARG E   8  PHE E  10  ARG E  18  TYR E  19                    
SITE     2 AJ4 14 ILE E  22  HIS E  23  LEU E  30  ILE F  15                    
SITE     3 AJ4 14 ARG F  19  TRP F  20  VAL F  23  HIS F  24                    
SITE     4 AJ4 14 VAL F  28  ILE F  31                                          
SITE     1 AJ5 12 LEU D  43  LEU D  49  PHE D 101  PHE D 113                    
SITE     2 AJ5 12 CLA D 404  LMG D 408  DGD E 101  PRO F  29                    
SITE     3 AJ5 12 THR F  30  PHE F  33  LEU F  34  VAL J  21                    
SITE     1 AJ6  2 ARG F  45  GLU V  23                                          
SITE     1 AJ7  9 CLA B 602  CLA B 610  CLA B 611  MET H  35                    
SITE     2 AJ7  9 LEU H  37  PHE H  38  PHE H  41  ILE H  44                    
SITE     3 AJ7  9 THR X   2                                                     
SITE     1 AJ8 16 TYR B 193  GLY B 254  TYR B 258  TYR B 273                    
SITE     2 AJ8 16 GLN B 274  PHE B 463  CLA B 603  CLA B 609                    
SITE     3 AJ8 16 HIS D  87  PHE D 120  ILE D 159  TYR H  49                    
SITE     4 AJ8 16 ASN H  50  VAL H  60  SER H  61  TRP H  62                    
SITE     1 AJ9 13 CLA A 609  ILE C 209  PHE C 210  LEU C 213                    
SITE     2 AJ9 13 GLY C 236  HIS C 237  CLA C 501  CLA C 505                    
SITE     3 AJ9 13 CLA C 506  CLA C 507  VAL I  20  PHE I  23                    
SITE     4 AJ9 13 LEU I  24                                                     
SITE     1 AK1  5 LMG D 408  GLY J  31  ALA J  34  GLY J  35                    
SITE     2 AK1  5 LEU J  36                                                     
SITE     1 AK2 16 PHE C  62  ALA J  14  THR J  15  GLY J  18                    
SITE     2 AK2 16 MET J  19  LEU K  21  LEU K  25  LEU K  31                    
SITE     3 AK2 16 ALA K  34  LEU K  35  ALA K  41  BCR K 102                    
SITE     4 AK2 16 GLY Y  29  PRO Y  33  VAL Z  13  PHE Z  17                    
SITE     1 AK3 15 ALA C  55  LEU C  59  PHE C  62  PHE C 112                    
SITE     2 AK3 15 ALA C 123  GLY C 126  ALA C 133  CLA C 511                    
SITE     3 AK3 15 TYR K  15  LEU K  25  PHE K  32  ALA K  36                    
SITE     4 AK3 15 TRP K  39  BCR K 101  SER Z  16                               
SITE     1 AK4 19 SER A 232  ASN A 234  PRO B   4  TRP B   5                    
SITE     2 AK4 19 TYR B   6  LMG B 621  TRP D 266  PHE D 273                    
SITE     3 AK4 19 CLA D 402  PL9 D 405  LHG D 406  LHG D 407                    
SITE     4 AK4 19 GLU L  11  LEU L  12  ASN L  13  SER L  16                    
SITE     5 AK4 19 GLY L  20  LEU L  22  PHE M  21                               
SITE     1 AK5 19 ARG L  14  TYR L  18  LEU L  21  LEU L  25                    
SITE     2 AK5 19 VAL M  15  SER M  19  TYR M  26  LEU T  16                    
SITE     3 AK5 19 PHE T  19  PHE T  23  BCR T 101  ARG b  18                    
SITE     4 AK5 19 SER b 104  PHE b 108  TRP b 115  SQD b 601                    
SITE     5 AK5 19 CLA b 616  BCR b 619  ARG l   7                               
SITE     1 AK6  3 THR O 138  ASN O 200  VAL O 201                               
SITE     1 AK7 15 LEU A  28  SQD A 614  SQD L 102  PHE T   8                    
SITE     2 AK7 15 ALA T  11  ALA T  15  PHE T  18  ILE T  21                    
SITE     3 AK7 15 SER b  36  MET b  37  TYR b  40  LEU b 109                    
SITE     4 AK7 15 CLA b 609  BCR b 619  BCR b 620                               
SITE     1 AK8  1 LYS U 104                                                     
SITE     1 AK9 16 ALA V  36  CYS V  37  CYS V  40  HIS V  41                    
SITE     2 AK9 16 THR V  46  THR V  48  LEU V  52  ASP V  53                    
SITE     3 AK9 16 THR V  58  LEU V  72  TYR V  75  MET V  76                    
SITE     4 AK9 16 THR V  81  TYR V  82  HIS V  92  PRO V  93                    
SITE     1 AL1 10 PL9 A 611  TRP D  21  ARG D  24  ARG D  26                    
SITE     2 AL1 10 PHE F  16  THR F  17  VAL F  18  VAL X  27                    
SITE     3 AL1 10 ILE X  31  ASP X  35                                          
SITE     1 AL2  7 PHE C 127  TYR C 131  CLA C 513  MET Z  19                    
SITE     2 AL2  7 TYR Z  27  TRP Z  33  PHE Z  41                               
SITE     1 AL3 10 ASP a  61  ASP a 170  GLU a 189  HIS a 332                    
SITE     2 AL3 10 GLU a 333  HIS a 337  ASP a 342  ALA a 344                    
SITE     3 AL3 10 GLU c 354  ARG c 357                                          
SITE     1 AL4  5 HIS a 215  HIS a 272  BCT a 605  HIS d 214                    
SITE     2 AL4  5 HIS d 268                                                     
SITE     1 AL5  4 ASN a 181  HIS a 332  GLU a 333  LYS d 317                    
SITE     1 AL6  3 ASN a 338  GLY c 353  GLU c 354                               
SITE     1 AL7  7 GLU a 244  TYR a 246  HIS a 272  FE2 a 602                    
SITE     2 AL7  7 HIS d 214  TYR d 244  HIS d 268                               
SITE     1 AL8 21 TYR a 147  PRO a 150  SER a 153  VAL a 157                    
SITE     2 AL8 21 MET a 183  PHE a 186  GLN a 187  ILE a 192                    
SITE     3 AL8 21 LEU a 193  HIS a 198  VAL a 205  PHE a 206                    
SITE     4 AL8 21 ALA a 286  ALA a 287  ILE a 290  CLA a 607                    
SITE     5 AL8 21 PHO a 608  CLA a 615  LEU d 205  CLA d 402                    
SITE     6 AL8 21 PHE t  17                                                     
SITE     1 AL9 15 GLN a 199  VAL a 202  ALA a 203  GLY a 207                    
SITE     2 AL9 15 LEU a 210  CLA a 606  PL9 a 611  PHE d 157                    
SITE     3 AL9 15 VAL d 175  ILE d 178  LEU d 182  PHO d 401                    
SITE     4 AL9 15 CLA d 402  LEU f  26  LMG j 101                               
SITE     1 AM1 18 LEU a  41  THR a  45  PHE a  48  TYR a 126                    
SITE     2 AM1 18 GLN a 130  TYR a 147  ALA a 149  PRO a 150                    
SITE     3 AM1 18 PHE a 158  VAL a 283  CLA a 606  CLA a 615                    
SITE     4 AM1 18 LEU d 205  LEU d 209  ILE d 213  TRP d 253                    
SITE     5 AM1 18 PHE d 257  PL9 d 404                                          
SITE     1 AM2 17 ILE a  36  PRO a  39  THR a  40  PHE a  93                    
SITE     2 AM2 17 PRO a  95  ILE a  96  TRP a  97  LEU a 114                    
SITE     3 AM2 17 HIS a 118  LEU a 121  BCR a 610  LMG a 613                    
SITE     4 AM2 17 DGD c 516  VAL i   8  TYR i   9  VAL i  12                    
SITE     5 AM2 17 PHE i  15                                                     
SITE     1 AM3  9 LEU a  42  ALA a  43  ILE a  50  ILE a  96                    
SITE     2 AM3  9 LEU a 102  TRP a 105  LEU a 106  CLA a 609                    
SITE     3 AM3  9 PHE i  15                                                     
SITE     1 AM4 21 PHE a 211  MET a 214  HIS a 215  LEU a 218                    
SITE     2 AM4 21 PHE a 255  SER a 264  PHE a 265  LEU a 271                    
SITE     3 AM4 21 PHE a 274  CLA a 607  VAL d  30  PHE d  38                    
SITE     4 AM4 21 PRO d  39  ALA d  41  PHO d 401  LHG e 101                    
SITE     5 AM4 21 VAL f  18  THR f  25  THR x  24  LEU x  28                    
SITE     6 AM4 21 SQD x 101                                                     
SITE     1 AM5 16 GLY a 204  ASN a 267  SER a 270  PHE a 273                    
SITE     2 AM5 16 PHE a 274  ALA a 277  TRP a 278  GLY a 282                    
SITE     3 AM5 16 LHG a 616  GLN c  28  ALA c  34  TRP c  36                    
SITE     4 AM5 16 CLA c 508  PHE d 232  ARG d 233  PHE k  37                    
SITE     1 AM6 14 PHE a  93  TRP a  97  GLU a  98  PHE a 117                    
SITE     2 AM6 14 SER a 124  CLA a 609  LEU c 214  SER c 216                    
SITE     3 AM6 14 GLU c 221  TRP c 223  CLA c 505  DGD c 516                    
SITE     4 AM6 14 LYS i   5  TYR i   9                                          
SITE     1 AM7 13 VAL B 102  TRP B 113  TYR B 117  CLA B 607                    
SITE     2 AM7 13 BCR B 620  TRP a  20  ASN a  26  ARG a  27                    
SITE     3 AM7 13 LEU a  28  ILE a  38  CLA a 615  PHE t  22                    
SITE     4 AM7 13 BCR t 101                                                     
SITE     1 AM8 18 VAL a 157  MET a 172  ILE a 176  THR a 179                    
SITE     2 AM8 18 PHE a 180  MET a 183  CLA a 606  PHO a 608                    
SITE     3 AM8 18 SQD a 614  MET d 198  VAL d 201  LEU d 205                    
SITE     4 AM8 18 GLY d 206  CLA d 402  PL9 d 404  LHG d 407                    
SITE     5 AM8 18 LHG l 102  PHE t  10                                          
SITE     1 AM9 19 ARG a 140  TRP a 142  ALA a 146  PHE a 273                    
SITE     2 AM9 19 VAL a 281  SQD a 612  TRP c  36  TRP c 443                    
SITE     3 AM9 19 ARG c 447  CLA c 504  CLA c 508  CLA c 510                    
SITE     4 AM9 19 DGD c 518  GLU d 219  ASN d 220  ALA d 229                    
SITE     5 AM9 19 SER d 230  THR d 231  PHE d 232                               
SITE     1 AN1 15 ARG L  14  TYR L  18  SQD L 102  LEU M  16                    
SITE     2 AN1 15 PHE T  19  PHE T  23  ARG b  18  LEU b  29                    
SITE     3 AN1 15 SER b 104  PHE b 108  TRP b 115  CLA b 616                    
SITE     4 AN1 15 BCR b 619  ASN l   4  ARG l   7                               
SITE     1 AN2  2 GLU b 435  ASN b 438                                          
SITE     1 AN3  5 TRP b 185  PRO b 187  PHE b 190  CLA b 604                    
SITE     2 AN3  5 BCR h 101                                                     
SITE     1 AN4 19 TRP b 185  GLY b 189  PHE b 190  GLY b 197                    
SITE     2 AN4 19 ALA b 200  HIS b 201  ALA b 204  ALA b 205                    
SITE     3 AN4 19 VAL b 208  PHE b 246  PHE b 247  PHE b 250                    
SITE     4 AN4 19 CLA b 603  CLA b 605  PHE h  38  PHE h  41                    
SITE     5 AN4 19 ILE h  45  BCR h 101  DGD h 102                               
SITE     1 AN5 15 ARG b  68  LEU b  69  ALA b 146  LEU b 149                    
SITE     2 AN5 15 CYS b 150  PHE b 153  HIS b 201  HIS b 202                    
SITE     3 AN5 15 VAL b 252  THR b 262  CLA b 604  CLA b 607                    
SITE     4 AN5 15 CLA b 608  CLA b 612  PHE h  38                               
SITE     1 AN6 16 TRP b  33  PHE b  65  ARG b  68  LEU b 149                    
SITE     2 AN6 16 VAL b 245  ALA b 249  VAL b 252  PHE b 451                    
SITE     3 AN6 16 HIS b 455  PHE b 458  ALA b 459  CLA b 607                    
SITE     4 AN6 16 CLA b 609  CLA b 614  CLA b 615  CLA b 617                    
SITE     1 AN7 18 THR b  27  VAL b  30  ALA b  34  VAL b  62                    
SITE     2 AN7 18 MET b  66  LEU b  69  HIS b 100  LEU b 103                    
SITE     3 AN7 18 ALA b 146  GLY b 147  CYS b 150  ALA b 205                    
SITE     4 AN7 18 GLY b 209  CLA b 605  CLA b 606  CLA b 608                    
SITE     5 AN7 18 CLA b 612  BCR b 621                                          
SITE     1 AN8 16 SQD A 614  VAL b  71  TRP b  91  VAL b  96                    
SITE     2 AN8 16 VAL b 102  LEU b 106  GLY b 152  PHE b 153                    
SITE     3 AN8 16 PHE b 156  HIS b 157  PHE b 162  GLY b 163                    
SITE     4 AN8 16 PRO b 164  CLA b 605  CLA b 607  BCR b 621                    
SITE     1 AN9 20 BCR T 101  TRP b  33  TYR b  40  GLN b  58                    
SITE     2 AN9 20 GLY b  59  MET b  60  PHE b  61  LEU b 324                    
SITE     3 AN9 20 THR b 327  GLY b 328  PRO b 329  TRP b 450                    
SITE     4 AN9 20 PHE b 451  HIS b 455  CLA b 606  BCR b 619                    
SITE     5 AN9 20 BCR b 620  LMG b 622  LHG d 406  PHE m  14                    
SITE     1 AO1 18 THR b 236  SER b 239  SER b 240  ALA b 243                    
SITE     2 AO1 18 PHE b 246  PHE b 463  HIS b 466  GLY b 470                    
SITE     3 AO1 18 CLA b 611  CLA b 612  PHE d 120  ILE d 123                    
SITE     4 AO1 18 MET d 126  LEU d 127  ILE d 150  LEU h  39                    
SITE     5 AO1 18 LEU h  43  DGD h 102                                          
SITE     1 AO2 18 PHE b 139  LEU b 143  VAL b 208  ALA b 212                    
SITE     2 AO2 18 PHE b 215  HIS b 216  VAL b 219  ARG b 220                    
SITE     3 AO2 18 PRO b 221  PRO b 222  LEU b 229  CLA b 610                    
SITE     4 AO2 18 CLA b 612  THR h  27  MET h  31  PHE h  34                    
SITE     5 AO2 18 LEU h  43  BCR h 101                                          
SITE     1 AO3 15 LEU b 135  MET b 138  PHE b 139  HIS b 142                    
SITE     2 AO3 15 LEU b 143  ALA b 146  MET b 231  VAL b 237                    
SITE     3 AO3 15 SER b 240  CLA b 605  CLA b 607  CLA b 610                    
SITE     4 AO3 15 CLA b 611  CLA b 614  CLA b 617                               
SITE     1 AO4 19 TRP b   5  TYR b   6  ARG b   7  VAL b   8                    
SITE     2 AO4 19 HIS b   9  THR b  10  LEU b 238  ILE b 242                    
SITE     3 AO4 19 LEU b 461  PHE b 462  PHE b 464  GLY b 465                    
SITE     4 AO4 19 TRP b 468  HIS b 469  CLA b 614  CLA b 615                    
SITE     5 AO4 19 CLA b 616  LHG d 406  PHE m  21                               
SITE     1 AO5 14 HIS b   9  LEU b  19  HIS b  23  HIS b  26                    
SITE     2 AO5 14 THR b  27  LEU b 238  SER b 241  VAL b 245                    
SITE     3 AO5 14 CLA b 606  CLA b 612  CLA b 613  CLA b 615                    
SITE     4 AO5 14 CLA b 616  CLA b 617                                          
SITE     1 AO6 12 HIS b   9  HIS b  26  VAL b  30  TRP b  33                    
SITE     2 AO6 12 PHE b 462  CLA b 606  CLA b 613  CLA b 614                    
SITE     3 AO6 12 CLA b 616  BCR b 619  BCR b 620  LMG b 622                    
SITE     1 AO7 14 SQD L 102  PHE T   8  VAL b   8  HIS b   9                    
SITE     2 AO7 14 LEU b  29  TRP b 115  SQD b 601  CLA b 613                    
SITE     3 AO7 14 CLA b 614  CLA b 615  BCR b 619  LMG b 622                    
SITE     4 AO7 14 VAL l  10  PHE m  21                                          
SITE     1 AO8 13 HIS b  23  LEU b  24  MET b 138  ILE b 141                    
SITE     2 AO8 13 HIS b 142  LEU b 145  CLA b 606  CLA b 612                    
SITE     3 AO8 13 CLA b 614  CLA b 618  BCR b 621  LEU h  11                    
SITE     4 AO8 13 LEU h  14                                                     
SITE     1 AO9 11 LEU b  24  ALA b 110  TRP b 113  HIS b 114                    
SITE     2 AO9 11 LEU b 120  LEU b 122  CLA b 617  BCR b 621                    
SITE     3 AO9 11 THR h   5  GLY h   8  LEU h  11                               
SITE     1 AP1 15 SQD L 102  PHE T  19  BCR T 101  MET b  25                    
SITE     2 AP1 15 LEU b  29  PHE b 108  TRP b 115  SQD b 601                    
SITE     3 AP1 15 CLA b 609  CLA b 615  CLA b 616  BCR b 620                    
SITE     4 AP1 15 LMG b 622  ALA m  10  LEU m  13                               
SITE     1 AP2 11 BCR T 101  LEU b  29  GLY b  32  TRP b  33                    
SITE     2 AP2 11 SER b  36  ILE b 101  VAL b 102  CLA b 609                    
SITE     3 AP2 11 CLA b 615  BCR b 619  LMG b 622                               
SITE     1 AP3  9 SQD A 614  PHE T  22  PHE T  23  LEU b 106                    
SITE     2 AP3  9 TRP b 113  CLA b 607  CLA b 608  CLA b 617                    
SITE     3 AP3  9 CLA b 618                                                     
SITE     1 AP4 11 TYR b  40  THR b 327  PRO b 329  LYS b 332                    
SITE     2 AP4 11 CLA b 609  CLA b 615  CLA b 616  BCR b 619                    
SITE     3 AP4 11 BCR b 620  LHG l 102  ASN m   4                               
SITE     1 AP5 18 LEU c  95  LEU c 168  GLY c 171  ALA c 172                    
SITE     2 AP5 18 LEU c 175  LEU c 185  VAL c 233  HIS c 237                    
SITE     3 AP5 18 ILE c 240  MET c 282  ILE c 285  PHE c 289                    
SITE     4 AP5 18 TYR c 297  CLA c 502  CLA c 503  CLA c 506                    
SITE     5 AP5 18 CLA c 507  BCR c 515                                          
SITE     1 AP6 15 TRP c  63  HIS c  91  LYS c 178  PHE c 182                    
SITE     2 AP6 15 LEU c 279  MET c 282  ALA c 286  TYR c 297                    
SITE     3 AP6 15 HIS c 430  LEU c 433  PHE c 437  CLA c 501                    
SITE     4 AP6 15 CLA c 503  CLA c 504  CLA c 510                               
SITE     1 AP7 13 ILE c  60  VAL c  61  THR c  68  LEU c  88                    
SITE     2 AP7 13 HIS c  91  ILE c  92  LEU c  95  VAL c 114                    
SITE     3 AP7 13 HIS c 118  CLA c 501  CLA c 502  CLA c 510                    
SITE     4 AP7 13 CLA c 512                                                     
SITE     1 AP8 16 LHG a 616  TRP c  63  PHE c  70  GLN c  84                    
SITE     2 AP8 16 GLY c  85  ILE c  87  TRP c 425  SER c 429                    
SITE     3 AP8 16 PHE c 436  CLA c 502  CLA c 508  DGD c 517                    
SITE     4 AP8 16 DGD c 518  LMG c 519  PRO k  26  VAL k  30                    
SITE     1 AP9 17 MET a 127  TRP a 131  LMG a 613  PHE c 264                    
SITE     2 AP9 17 SER c 273  TYR c 274  GLY c 277  ALA c 278                    
SITE     3 AP9 17 LEU c 438  HIS c 441  LEU c 442  ALA c 445                    
SITE     4 AP9 17 ARG c 449  CLA c 507  BCR c 515  VAL i  16                    
SITE     5 AP9 17 PHE i  23                                                     
SITE     1 AQ1 16 LEU c 161  LEU c 165  LEU c 213  LEU c 214                    
SITE     2 AQ1 16 ILE c 243  GLY c 247  TRP c 250  HIS c 251                    
SITE     3 AQ1 16 THR c 254  THR c 255  PRO c 256  PHE c 257                    
SITE     4 AQ1 16 TRP c 259  CLA c 501  CLA c 507  BCR c 515                    
SITE     1 AQ2 15 LEU c 161  HIS c 164  LEU c 168  TRP c 259                    
SITE     2 AQ2 15 TRP c 266  TYR c 271  TYR c 274  SER c 275                    
SITE     3 AQ2 15 LEU c 279  MET c 282  CLA c 501  CLA c 505                    
SITE     4 AQ2 15 CLA c 506  CLA c 509  BCR c 515                               
SITE     1 AQ3 21 SQD a 612  LHG a 616  TRP c  36  ALA c  37                    
SITE     2 AQ3 21 GLY c  38  ASN c  39  GLU c 269  LEU c 272                    
SITE     3 AQ3 21 LEU c 276  PHE c 436  PHE c 437  GLY c 440                    
SITE     4 AQ3 21 TRP c 443  HIS c 444  ARG c 447  CLA c 504                    
SITE     5 AQ3 21 CLA c 509  CLA c 510  CLA c 511  LMG c 519                    
SITE     6 AQ3 21 VAL k  30                                                     
SITE     1 AQ4 16 ASN c  39  LEU c  49  ALA c  52  HIS c  53                    
SITE     2 AQ4 16 HIS c  56  MET c 157  ILE c 160  GLY c 268                    
SITE     3 AQ4 16 GLU c 269  TYR c 271  LEU c 272  SER c 275                    
SITE     4 AQ4 16 CLA c 507  CLA c 508  CLA c 510  CLA c 511                    
SITE     1 AQ5 16 LHG a 616  ASN c  39  HIS c  56  LEU c  59                    
SITE     2 AQ5 16 ILE c  60  TRP c  63  LEU c 279  PHE c 436                    
SITE     3 AQ5 16 PHE c 437  CLA c 502  CLA c 503  CLA c 508                    
SITE     4 AQ5 16 CLA c 509  CLA c 511  PRO k  29  LEU k  33                    
SITE     1 AQ6 27 ARG c  26  TRP c  35  GLY c  38  ASN c  39                    
SITE     2 AQ6 27 ARG c  41  LEU c  42  LEU c  45  LYS c  48                    
SITE     3 AQ6 27 ALA c  52  ALA c 123  PHE c 127  ILE c 134                    
SITE     4 AQ6 27 CLA c 508  CLA c 509  CLA c 510  BCR c 521                    
SITE     5 AQ6 27 PHE k  32  LEU k  33  TRP k  39  GLN k  40                    
SITE     6 AQ6 27 BCR k 101  ILE y  35  ILE y  36  ASN y  45                    
SITE     7 AQ6 27 VAL z  20  ALA z  28  LMG z 101                               
SITE     1 AQ7 14 LEU c  50  HIS c  53  LEU c 125  PHE c 146                    
SITE     2 AQ7 14 PHE c 147  PHE c 163  HIS c 164  ILE c 166                    
SITE     3 AQ7 14 VAL c 167  ILE c 170  GLY c 171  CLA c 503                    
SITE     4 AQ7 14 CLA c 513  BCR c 514                                          
SITE     1 AQ8  9 VAL c 124  GLY c 128  TYR c 131  HIS c 132                    
SITE     2 AQ8  9 TYR c 143  PHE c 147  CLA c 512  BCR c 514                    
SITE     3 AQ8  9 LMG z 101                                                     
SITE     1 AQ9 10 PHE c 112  VAL c 116  SER c 121  VAL c 124                    
SITE     2 AQ9 10 LEU c 125  CLA c 512  CLA c 513  TYR k  15                    
SITE     3 AQ9 10 GLY z  55  ASN z  58                                          
SITE     1 AR1 14 ILE c 209  PHE c 210  TYR c 212  LEU c 213                    
SITE     2 AR1 14 ASP c 232  GLY c 236  HIS c 237  CLA c 501                    
SITE     3 AR1 14 CLA c 505  CLA c 506  CLA c 507  VAL i  20                    
SITE     4 AR1 14 PHE i  23  LEU i  24                                          
SITE     1 AR2 22 LEU a  91  PHE a 155  CLA a 609  LMG a 613                    
SITE     2 AR2 22 PRO c 217  GLY c 219  GLY c 220  GLU c 221                    
SITE     3 AR2 22 GLY c 222  TRP c 223  SER c 226  VAL c 227                    
SITE     4 AR2 22 ASN c 228  CYS c 288  PHE c 292  ASN c 293                    
SITE     5 AR2 22 ASN c 294  THR c 295  ASP c 360  PHE c 361                    
SITE     6 AR2 22 ARG c 362  LEU c 438                                          
SITE     1 AR3 18 HIS a 195  PHE a 197  LEU a 297  GLU c  83                    
SITE     2 AR3 18 GLN c  84  GLY c  85  SER c 406  ASN c 418                    
SITE     3 AR3 18 PHE c 419  VAL c 420  TRP c 425  THR c 428                    
SITE     4 AR3 18 SER c 429  CLA c 504  DGD c 518  LMG c 519                    
SITE     5 AR3 18 PHE j  29  TYR j  33                                          
SITE     1 AR4 21 GLN a 199  LEU a 200  ASN a 301  PHE a 302                    
SITE     2 AR4 21 SER a 305  LHG a 616  ASN c 405  VAL c 407                    
SITE     3 AR4 21 ASN c 415  SER c 416  VAL c 417  ASN c 418                    
SITE     4 AR4 21 CLA c 504  DGD c 517  ALA j  32  TYR j  33                    
SITE     5 AR4 21 GLY j  37  SER j  38  SER j  39  LMG j 101                    
SITE     6 AR4 21 GLN v  34                                                     
SITE     1 AR5  8 HIS c  74  GLN c  84  CLA c 504  CLA c 508                    
SITE     2 AR5  8 DGD c 517  ASP k  23  VAL k  27  VAL k  30                    
SITE     1 AR6  8 TRP c  97  ASP c 107  VAL c 113  VAL c 117                    
SITE     2 AR6  8 HIS c 118  SER c 121  PHE z  59  VAL z  62                    
SITE     1 AR7 17 ALA c  55  GLY c  58  LEU c  59  PHE c  62                    
SITE     2 AR7 17 LEU c 119  SER c 122  ALA c 123  GLY c 126                    
SITE     3 AR7 17 CLA c 511  TYR k  15  PHE k  18  PHE k  32                    
SITE     4 AR7 17 ALA k  36  TRP k  39  BCR k 101  LEU z   9                    
SITE     5 AR7 17 SER z  16                                                     
SITE     1 AR8 21 PHE a 206  LEU a 210  MET a 214  CLA a 607                    
SITE     2 AR8 21 PL9 a 611  ALA d  41  TRP d  48  ILE d 114                    
SITE     3 AR8 21 GLY d 118  GLY d 121  LEU d 122  PHE d 125                    
SITE     4 AR8 21 GLN d 129  ASN d 142  ALA d 145  PHE d 146                    
SITE     5 AR8 21 PRO d 149  PHE d 153  PRO d 275  VAL d 276                    
SITE     6 AR8 21 CLA d 402                                                     
SITE     1 AR9 19 PHE a 206  CLA a 606  CLA a 607  CLA a 615                    
SITE     2 AR9 19 LEU d  45  LEU d 122  PRO d 149  VAL d 152                    
SITE     3 AR9 19 PHE d 153  VAL d 156  LEU d 182  PHE d 185                    
SITE     4 AR9 19 GLN d 186  TRP d 191  HIS d 197  GLY d 200                    
SITE     5 AR9 19 SER d 282  VAL d 286  PHO d 401                               
SITE     1 AS1 15 CYS d  40  LEU d  43  LEU d  89  LEU d  90                    
SITE     2 AS1 15 LEU d  91  LEU d  92  TRP d  93  THR d 112                    
SITE     3 AS1 15 PHE d 113  HIS d 117  GLY h  36  LEU h  39                    
SITE     4 AS1 15 GLY x  13  LEU x  14  LEU x  21                               
SITE     1 AS2 21 PHE a  52  ILE a  53  PHO a 608  CLA a 615                    
SITE     2 AS2 21 MET d 198  HIS d 214  THR d 217  ALA d 249                    
SITE     3 AS2 21 TRP d 253  ALA d 260  PHE d 261  LEU d 267                    
SITE     4 AS2 21 PHE d 273  VAL d 274  GLY d 278  LHG d 407                    
SITE     5 AS2 21 LEU l  23  VAL l  26  LEU l  29  LHG l 102                    
SITE     6 AS2 21 PHE t  10                                                     
SITE     1 AS3  7 GLY d  99  ASP d 100  PHE d 101  THR d 102                    
SITE     2 AS3  7 PHE e  37  ASP e  45  BCR f 101                               
SITE     1 AS4 17 SER a 232  ASN a 234  TRP b   5  TYR b   6                    
SITE     2 AS4 17 ARG b   7  LEU b 461  PHE b 464  TRP b 468                    
SITE     3 AS4 17 CLA b 609  CLA b 613  TYR d 141  TRP d 266                    
SITE     4 AS4 17 PHE d 269  LEU d 272  THR d 277  LEU l  23                    
SITE     5 AS4 17 LHG l 102                                                     
SITE     1 AS5 21 MET a  37  CLA a 615  ILE d 256  PHE d 257                    
SITE     2 AS5 21 ILE d 259  ALA d 260  SER d 262  ASN d 263                    
SITE     3 AS5 21 TRP d 266  PHE d 270  PL9 d 404  ASN l  13                    
SITE     4 AS5 21 THR l  15  SER l  16  TYR l  18  LEU l  19                    
SITE     5 AS5 21 LHG l 102  PHE t  10  ILE t  13  PHE t  17                    
SITE     6 AS5 21 ALA t  20                                                     
SITE     1 AS6 13 LEU a 258  PHE a 260  TYR a 262  PL9 a 611                    
SITE     2 AS6 13 PHE d  27  LEU d  37  THR e   4  THR e   5                    
SITE     3 AS6 13 PRO e   9  PHE e  10  SER e  11  ALA f  22                    
SITE     4 AS6 13 VAL f  23                                                     
SITE     1 AS7 11 ARG e   8  ILE e  13  ARG e  18  TYR e  19                    
SITE     2 AS7 11 HIS e  23  LEU e  30  ARG f  19  TRP f  20                    
SITE     3 AS7 11 VAL f  23  HIS f  24  ILE f  31                               
SITE     1 AS8 12 TYR d  42  LEU d  43  LEU d  49  PHE d 101                    
SITE     2 AS8 12 DGD d 405  PRO f  29  THR f  30  PHE f  33                    
SITE     3 AS8 12 LEU f  34  VAL j  21  VAL j  25  LMG j 101                    
SITE     1 AS9  2 ARG f  45  GLU v  23                                          
SITE     1 AT1  8 CLA b 603  CLA b 604  CLA b 611  MET h  31                    
SITE     2 AT1  8 LEU h  37  PHE h  38  PHE h  41  LEU h  55                    
SITE     1 AT2 14 TYR b 193  TYR b 258  GLN b 274  PHE b 463                    
SITE     2 AT2 14 CLA b 604  CLA b 610  HIS d  87  ILE d 123                    
SITE     3 AT2 14 LEU d 162  TYR h  49  ASN h  50  VAL h  60                    
SITE     4 AT2 14 SER h  61  TRP h  62                                          
SITE     1 AT3 16 CLA a 607  DGD c 518  TYR d  67  GLY d  70                    
SITE     2 AT3 16 CYS d  71  ASN d  72  PHE d  73  THR f  30                    
SITE     3 AT3 16 ILE f  37  GLN f  41  BCR f 101  PHE j  28                    
SITE     4 AT3 16 GLY j  31  ALA j  32  LEU j  36   MG j 102                    
SITE     1 AT4  4 GLY j  31  ALA j  34  LEU j  36  LMG j 101                    
SITE     1 AT5 16 CLA c 511  BCR c 521  ALA j  14  THR j  15                    
SITE     2 AT5 16 GLY j  18  MET j  19  LEU k  21  LEU k  31                    
SITE     3 AT5 16 PHE k  32  ALA k  34  PHE k  37  ALA k  41                    
SITE     4 AT5 16 ILE y  28  GLY y  29  PRO y  33  PHE z  17                    
SITE     1 AT6 18 ARG B  18  SER B 104  TRP B 115  CLA B 615                    
SITE     2 AT6 18 BCR B 618  BCR B 619  SQD B 622  ARG L   7                    
SITE     3 AT6 18 ARG l  14  TYR l  18  LEU l  21  VAL m  15                    
SITE     4 AT6 18 TYR m  26  CYS t  12  LEU t  16  PHE t  19                    
SITE     5 AT6 18 PHE t  23  BCR t 101                                          
SITE     1 AT7 22 SER a 232  ASN a 234  CLA a 615  TRP b   5                    
SITE     2 AT7 22 TYR b   6  LMG b 622  TRP d 266  PHE d 273                    
SITE     3 AT7 22 PL9 d 404  LHG d 406  LHG d 407  GLU l  11                    
SITE     4 AT7 22 LEU l  12  ASN l  13  SER l  16  LEU l  19                    
SITE     5 AT7 22 GLY l  20  LEU l  22  LEU l  23  PRO m  18                    
SITE     6 AT7 22 PHE m  21  LEU m  22                                          
SITE     1 AT8  3 THR o 138  ASN o 200  VAL o 201                               
SITE     1 AT9 14 TRP B  33  SER B  36  MET B  37  PHE B 108                    
SITE     2 AT9 14 LEU B 109  CLA B 608  BCR B 618  BCR B 619                    
SITE     3 AT9 14 SQD a 614  SQD l 101  PHE t   8  ALA t  15                    
SITE     4 AT9 14 PHE t  18  PHE t  22                                          
SITE     1 AU1 20 ALA c 393  ALA v  36  CYS v  37  CYS v  40                    
SITE     2 AU1 20 HIS v  41  THR v  48  LEU v  52  ASP v  53                    
SITE     3 AU1 20 LEU v  54  THR v  58  ALA v  62  LEU v  72                    
SITE     4 AU1 20 TYR v  75  MET v  76  THR v  81  TYR v  82                    
SITE     5 AU1 20 ILE v  88  HIS v  92  PRO v  93  MET v 104                    
SITE     1 AU2 12 PL9 a 611  TRP d  21  ARG d  24  ARG d  26                    
SITE     2 AU2 12 PHE f  16  THR f  17  VAL f  18  LEU x  23                    
SITE     3 AU2 12 THR x  24  VAL x  27  ILE x  31  ASP x  35                    
SITE     1 AU3  9 PHE c 127  TYR c 131  ARG c 135  CLA c 511                    
SITE     2 AU3  9 CLA c 513  MET z  19  TYR z  27  TRP z  33                    
SITE     3 AU3  9 TRP z  47                                                     
CRYST1  250.800  250.800  250.800  90.00  90.00  90.00 P 1           2          
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      0.003987  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003987  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003987        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system