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Database: PDB
Entry: 5L8R
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HEADER    OXIDOREDUCTASE                          08-JUN-16   5L8R              
TITLE     THE STRUCTURE OF PLANT PHOTOSYSTEM I SUPER-COMPLEX AT 2.6 ANGSTROM    
TITLE    2 RESOLUTION.                                                          
CAVEAT     5L8R    LUT 1 502 HAS WRONG CHIRALITY AT ATOM C26 LUT 2 501 HAS      
CAVEAT   2 5L8R    WRONG CHIRALITY AT ATOM C26 LUT 3 302 HAS WRONG CHIRALITY    
CAVEAT   3 5L8R    AT ATOM C26 XAT 4 303 HAS WRONG CHIRALITY AT ATOM C5 XAT 4   
CAVEAT   4 5L8R    303 HAS WRONG CHIRALITY AT ATOM C6 LUT J 1109 HAS WRONG      
CAVEAT   5 5L8R    CHIRALITY AT ATOM C26                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LHCA1;                                                     
COMPND   3 CHAIN: 1;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: CHLOROPHYLL A-B BINDING PROTEIN, CHLOROPLASTIC;            
COMPND   6 CHAIN: 2;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: CHLOROPHYLL A-B BINDING PROTEIN 3, CHLOROPLASTIC;          
COMPND   9 CHAIN: 3;                                                            
COMPND  10 SYNONYM: LHCII TYPE III CAB-3;                                       
COMPND  11 MOL_ID: 4;                                                           
COMPND  12 MOLECULE: CHLOROPHYLL A-B BINDING PROTEIN P4, CHLOROPLASTIC;         
COMPND  13 CHAIN: 4;                                                            
COMPND  14 SYNONYM: LHCI TYPE III CAB-P4;                                       
COMPND  15 MOL_ID: 5;                                                           
COMPND  16 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1;            
COMPND  17 CHAIN: A;                                                            
COMPND  18 SYNONYM: PSI-A,PSAA;                                                 
COMPND  19 EC: 1.97.1.12;                                                       
COMPND  20 MOL_ID: 6;                                                           
COMPND  21 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2;            
COMPND  22 CHAIN: B;                                                            
COMPND  23 SYNONYM: PSI-B,PSAB;                                                 
COMPND  24 EC: 1.97.1.12;                                                       
COMPND  25 MOL_ID: 7;                                                           
COMPND  26 MOLECULE: PHOTOSYSTEM I IRON-SULFUR CENTER;                          
COMPND  27 CHAIN: C;                                                            
COMPND  28 SYNONYM: 9 KDA POLYPEPTIDE,PSI-C,PHOTOSYSTEM I SUBUNIT VII,PSAC;     
COMPND  29 EC: 1.97.1.12;                                                       
COMPND  30 MOL_ID: 8;                                                           
COMPND  31 MOLECULE: PSAD;                                                      
COMPND  32 CHAIN: D;                                                            
COMPND  33 MOL_ID: 9;                                                           
COMPND  34 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND  35 CHAIN: E;                                                            
COMPND  36 MOL_ID: 10;                                                          
COMPND  37 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT III;                 
COMPND  38 CHAIN: F;                                                            
COMPND  39 MOL_ID: 11;                                                          
COMPND  40 MOLECULE: PSAG;                                                      
COMPND  41 CHAIN: G;                                                            
COMPND  42 MOL_ID: 12;                                                          
COMPND  43 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT VI;                  
COMPND  44 CHAIN: H;                                                            
COMPND  45 MOL_ID: 13;                                                          
COMPND  46 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT VIII;                
COMPND  47 CHAIN: I;                                                            
COMPND  48 SYNONYM: PSI-I;                                                      
COMPND  49 MOL_ID: 14;                                                          
COMPND  50 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT IX;                  
COMPND  51 CHAIN: J;                                                            
COMPND  52 SYNONYM: PSI-J;                                                      
COMPND  53 MOL_ID: 15;                                                          
COMPND  54 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT X PSAK;              
COMPND  55 CHAIN: K;                                                            
COMPND  56 MOL_ID: 16;                                                          
COMPND  57 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND  58 CHAIN: L                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE   3 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE   4 ORGANISM_TAXID: 3888;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE   7 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE   8 ORGANISM_TAXID: 3888;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  11 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  12 ORGANISM_TAXID: 3888;                                                
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  15 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  16 ORGANISM_TAXID: 3888;                                                
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  19 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  20 ORGANISM_TAXID: 3888;                                                
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  23 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  24 ORGANISM_TAXID: 3888;                                                
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  27 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  28 ORGANISM_TAXID: 3888;                                                
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  31 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  32 ORGANISM_TAXID: 3888;                                                
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  35 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  36 ORGANISM_TAXID: 3888;                                                
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  39 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  40 ORGANISM_TAXID: 3888;                                                
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  43 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  44 ORGANISM_TAXID: 3888;                                                
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  47 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  48 ORGANISM_TAXID: 3888;                                                
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  51 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  52 ORGANISM_TAXID: 3888;                                                
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  55 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  56 ORGANISM_TAXID: 3888;                                                
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  59 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  60 ORGANISM_TAXID: 3888;                                                
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  63 ORGANISM_COMMON: GARDEN PEA;                                         
SOURCE  64 ORGANISM_TAXID: 3888                                                 
KEYWDS    PHOTOSYNTHESIS, MEMBRANE COMPLEX, CHLOROPHYLL, LIGHT HARVESTING,      
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.MAZOR,A.BOROVIKOVA,I.CASPY,N.NELSON                                 
REVDAT   3   29-NOV-17 5L8R    1       REMARK                                   
REVDAT   2   08-NOV-17 5L8R    1       COMPND HETNAM HETSYN                     
REVDAT   1   15-MAR-17 5L8R    0                                                
JRNL        AUTH   Y.MAZOR,A.BOROVIKOVA,I.CASPY,N.NELSON                        
JRNL        TITL   STRUCTURE OF THE PLANT PHOTOSYSTEM I SUPERCOMPLEX AT 2.6     
JRNL        TITL 2 ANGSTROM RESOLUTION.                                         
JRNL        REF    NAT PLANTS                    V.   3 17014 2017              
JRNL        REFN                   ESSN 2055-0278                               
JRNL        PMID   28248295                                                     
JRNL        DOI    10.1038/NPLANTS.2017.14                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 247956                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4916                            
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 39.9110 -  8.0573    1.00     8569   181  0.2169 0.1944        
REMARK   3     2  8.0573 -  6.4039    1.00     8280   186  0.1861 0.1987        
REMARK   3     3  6.4039 -  5.5969    1.00     8211   183  0.1851 0.2235        
REMARK   3     4  5.5969 -  5.0863    1.00     8214   175  0.1743 0.1995        
REMARK   3     5  5.0863 -  4.7223    1.00     8160   174  0.1636 0.1877        
REMARK   3     6  4.7223 -  4.4443    0.99     8103   150  0.1663 0.1858        
REMARK   3     7  4.4443 -  4.2220    1.00     8168   157  0.1645 0.2087        
REMARK   3     8  4.2220 -  4.0384    1.00     8125   144  0.1723 0.2139        
REMARK   3     9  4.0384 -  3.8831    1.00     8104   168  0.1755 0.1783        
REMARK   3    10  3.8831 -  3.7492    1.00     8109   153  0.1798 0.1953        
REMARK   3    11  3.7492 -  3.6320    0.99     8062   174  0.1925 0.2268        
REMARK   3    12  3.6320 -  3.5283    0.99     8028   146  0.2188 0.2723        
REMARK   3    13  3.5283 -  3.4354    0.99     8059   164  0.2190 0.2821        
REMARK   3    14  3.4354 -  3.3517    0.99     8061   138  0.2226 0.2636        
REMARK   3    15  3.3517 -  3.2755    1.00     8064   174  0.2253 0.2542        
REMARK   3    16  3.2755 -  3.2058    1.00     8082   144  0.2321 0.3076        
REMARK   3    17  3.2058 -  3.1417    1.00     8039   179  0.2443 0.2954        
REMARK   3    18  3.1417 -  3.0825    1.00     8070   170  0.2485 0.2757        
REMARK   3    19  3.0825 -  3.0274    0.99     8073   141  0.2622 0.2891        
REMARK   3    20  3.0274 -  2.9761    1.00     8027   172  0.2647 0.2893        
REMARK   3    21  2.9761 -  2.9281    1.00     8072   179  0.2709 0.3019        
REMARK   3    22  2.9281 -  2.8831    1.00     8028   150  0.2849 0.2973        
REMARK   3    23  2.8831 -  2.8407    1.00     8054   170  0.2913 0.3066        
REMARK   3    24  2.8407 -  2.8007    1.00     8040   181  0.3053 0.3322        
REMARK   3    25  2.8007 -  2.7629    1.00     8025   158  0.3208 0.3049        
REMARK   3    26  2.7629 -  2.7270    1.00     8128   128  0.3326 0.3714        
REMARK   3    27  2.7270 -  2.6929    1.00     7992   172  0.3495 0.3731        
REMARK   3    28  2.6929 -  2.6605    1.00     8029   171  0.3719 0.4065        
REMARK   3    29  2.6605 -  2.6295    1.00     8060   160  0.3891 0.4338        
REMARK   3    30  2.6295 -  2.6000    1.00     8004   174  0.4146 0.4601        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.270           
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      :  0.006          39485                                  
REMARK   3   ANGLE     :  1.846          55777                                  
REMARK   3   CHIRALITY :  0.116           4963                                  
REMARK   3   PLANARITY :  0.016           7070                                  
REMARK   3   DIHEDRAL  : 20.314          21909                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0380   7.6729  64.5628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5119 T22:   0.5604                                     
REMARK   3      T33:   0.5651 T12:   0.0885                                     
REMARK   3      T13:  -0.1498 T23:   0.0489                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6916 L22:   1.2618                                     
REMARK   3      L33:   0.7382 L12:  -0.0260                                     
REMARK   3      L13:  -0.0190 L23:  -0.0499                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0523 S12:  -0.0784 S13:   0.0985                       
REMARK   3      S21:  -0.0292 S22:   0.0776 S23:   0.2026                       
REMARK   3      S31:  -0.0384 S32:  -0.0046 S33:   0.0059                       
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 5L8R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000299.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 248807                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 84.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 83.90                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
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: 30MM TRIS-HCL PH8.75, 50MM KH2PO4,       
REMARK 280  0.03% OCTYL GLUCOSE NEOPENTYL GLYCOL, 14% PEG400, 2MM               
REMARK 280  GLUTATHIONE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       94.80550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      106.47150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      100.49700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      106.47150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       94.80550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      100.49700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC                     
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2, 3, 4, A, B, C, D, E, F,         
REMARK 350                    AND CHAINS: G, H, I, J, K, L                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET 2     1                                                      
REMARK 465     ALA 2     2                                                      
REMARK 465     SER 2     3                                                      
REMARK 465     ALA 2     4                                                      
REMARK 465     CYS 2     5                                                      
REMARK 465     ALA 2     6                                                      
REMARK 465     SER 2     7                                                      
REMARK 465     SER 2     8                                                      
REMARK 465     ALA 2     9                                                      
REMARK 465     ILE 2    10                                                      
REMARK 465     ALA 2    11                                                      
REMARK 465     ALA 2    12                                                      
REMARK 465     VAL 2    13                                                      
REMARK 465     ALA 2    14                                                      
REMARK 465     ILE 2    15                                                      
REMARK 465     SER 2    16                                                      
REMARK 465     THR 2    17                                                      
REMARK 465     PRO 2    18                                                      
REMARK 465     SER 2    19                                                      
REMARK 465     SER 2    20                                                      
REMARK 465     GLN 2    21                                                      
REMARK 465     LYS 2    22                                                      
REMARK 465     ASN 2    23                                                      
REMARK 465     GLY 2    24                                                      
REMARK 465     SER 2    25                                                      
REMARK 465     PRO 2    26                                                      
REMARK 465     SER 2    27                                                      
REMARK 465     GLY 2    28                                                      
REMARK 465     THR 2    29                                                      
REMARK 465     SER 2    30                                                      
REMARK 465     LYS 2    31                                                      
REMARK 465     ALA 2    32                                                      
REMARK 465     PHE 2    33                                                      
REMARK 465     LEU 2    34                                                      
REMARK 465     GLY 2    35                                                      
REMARK 465     ARG 2    36                                                      
REMARK 465     LYS 2    37                                                      
REMARK 465     LEU 2    38                                                      
REMARK 465     LYS 2    39                                                      
REMARK 465     VAL 2    40                                                      
REMARK 465     ASN 2    41                                                      
REMARK 465     SER 2    42                                                      
REMARK 465     SER 2    43                                                      
REMARK 465     THR 2    44                                                      
REMARK 465     ALA 2    45                                                      
REMARK 465     SER 2    46                                                      
REMARK 465     PRO 2    47                                                      
REMARK 465     SER 2    48                                                      
REMARK 465     ARG 2    49                                                      
REMARK 465     VAL 2    50                                                      
REMARK 465     ARG 2    51                                                      
REMARK 465     SER 2    52                                                      
REMARK 465     THR 2    53                                                      
REMARK 465     SER 2    54                                                      
REMARK 465     THR 2    55                                                      
REMARK 465     VAL 2    56                                                      
REMARK 465     CYS 2    57                                                      
REMARK 465     PHE 2   266                                                      
REMARK 465     THR 2   267                                                      
REMARK 465     PRO 2   268                                                      
REMARK 465     LYS 2   269                                                      
REMARK 465     MET 3     1                                                      
REMARK 465     ALA 3     2                                                      
REMARK 465     THR 3     3                                                      
REMARK 465     GLN 3     4                                                      
REMARK 465     ALA 3     5                                                      
REMARK 465     LEU 3     6                                                      
REMARK 465     VAL 3     7                                                      
REMARK 465     SER 3     8                                                      
REMARK 465     SER 3     9                                                      
REMARK 465     SER 3    10                                                      
REMARK 465     SER 3    11                                                      
REMARK 465     LEU 3    12                                                      
REMARK 465     THR 3    13                                                      
REMARK 465     PHE 3    14                                                      
REMARK 465     ALA 3    15                                                      
REMARK 465     ALA 3    16                                                      
REMARK 465     GLU 3    17                                                      
REMARK 465     ALA 3    18                                                      
REMARK 465     VAL 3    19                                                      
REMARK 465     ARG 3    20                                                      
REMARK 465     GLN 3    21                                                      
REMARK 465     SER 3    22                                                      
REMARK 465     PHE 3    23                                                      
REMARK 465     ARG 3    24                                                      
REMARK 465     ALA 3    25                                                      
REMARK 465     ARG 3    26                                                      
REMARK 465     SER 3    27                                                      
REMARK 465     LEU 3    28                                                      
REMARK 465     PRO 3    29                                                      
REMARK 465     SER 3    30                                                      
REMARK 465     SER 3    31                                                      
REMARK 465     VAL 3    32                                                      
REMARK 465     GLY 3    33                                                      
REMARK 465     CYS 3    34                                                      
REMARK 465     SER 3    35                                                      
REMARK 465     ARG 3    36                                                      
REMARK 465     LYS 3    37                                                      
REMARK 465     GLY 3    38                                                      
REMARK 465     LEU 3    39                                                      
REMARK 465     VAL 3    40                                                      
REMARK 465     ARG 3    41                                                      
REMARK 465     ALA 3    42                                                      
REMARK 465     ALA 3    43                                                      
REMARK 465     ALA 3    44                                                      
REMARK 465     THR 3    45                                                      
REMARK 465     PRO 3    46                                                      
REMARK 465     PRO 3    47                                                      
REMARK 465     VAL 3    48                                                      
REMARK 465     LYS 3    49                                                      
REMARK 465     GLN 3    50                                                      
REMARK 465     GLY 3    51                                                      
REMARK 465     GLY 3    52                                                      
REMARK 465     VAL 3    53                                                      
REMARK 465     ASP 3    54                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     GLN A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET I     1                                                      
REMARK 465     ILE I     2                                                      
REMARK 465     LEU I    33                                                      
REMARK 465     PHE I    34                                                      
REMARK 465     SER I    35                                                      
REMARK 465     THR I    36                                                      
REMARK 465     LYS I    37                                                      
REMARK 465     LYS I    38                                                      
REMARK 465     ILE I    39                                                      
REMARK 465     ASN I    40                                                      
REMARK 465     GLY K    80A                                                     
REMARK 465     LEU K    80B                                                     
REMARK 465     LYS K    80C                                                     
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS 3 215    CG   CD   CE   NZ                                   
REMARK 470     ASP 3 262    CG   OD1  OD2                                       
REMARK 470     LYS 3 273    CG   CD   CE   NZ                                   
REMARK 470     LYS F 229    CG   CD   CE   NZ                                   
REMARK 470     LEU K  70    CG   CD1  CD2                                       
REMARK 470     ASN K  75    CG   OD1  ND2                                       
REMARK 470     ARG K  76    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS K  77    CG   CD   CE   NZ                                   
REMARK 470     ARG K  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER B   613     O    HOH B   901              2.04            
REMARK 500   OH   TYR H    78     OE1  GLU L   101              2.09            
REMARK 500   O    LEU A   255     N    TYR A   259              2.14            
REMARK 500   NH1  ARG B   694     O    SER L   151              2.14            
REMARK 500   O    LEU L   109     O    HOH L   401              2.16            
REMARK 500   NZ   LYS 2   223     O5   LHG 2   517              2.17            
REMARK 500   OBD  CLA G   202     O3'  LMT G   209              2.18            
REMARK 500   O    VAL A    18     O    HOH A   901              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP 1  62       61.89   -159.38                                   
REMARK 500    ALA 1 108        2.88    -68.90                                   
REMARK 500    PRO 1 125       85.16    -63.62                                   
REMARK 500    LYS 1 172      -77.49    -53.16                                   
REMARK 500    ASP 2  88       61.92   -162.71                                   
REMARK 500    LYS 2 187      175.78     64.55                                   
REMARK 500    GLN 2 212      -32.57     75.60                                   
REMARK 500    ALA 2 260       89.55    -63.41                                   
REMARK 500    THR 2 261     -152.33   -140.57                                   
REMARK 500    ASP 3  79       69.55   -152.62                                   
REMARK 500    GLU 3  87      -71.44    -62.23                                   
REMARK 500    PHE 3  92       -4.96     68.56                                   
REMARK 500    ASN 3 154      -24.24     72.70                                   
REMARK 500    LEU 3 190      -11.57     63.61                                   
REMARK 500    ASN 3 266       74.96     50.52                                   
REMARK 500    ASP 4  77       62.28   -155.62                                   
REMARK 500    ILE 4 171      -60.51    -91.83                                   
REMARK 500    GLU 4 199      -34.64     71.60                                   
REMARK 500    SER 4 238      -71.61    -52.20                                   
REMARK 500    ASP A  25       63.14     38.36                                   
REMARK 500    ASN A 105       35.12    -98.40                                   
REMARK 500    ILE A 126      -65.19   -109.58                                   
REMARK 500    LYS A 188      -77.09   -109.38                                   
REMARK 500    VAL A 225      -57.36   -125.44                                   
REMARK 500    LEU A 250      -78.11    -72.16                                   
REMARK 500    ALA A 266       13.27     58.27                                   
REMARK 500    ASN A 273       32.78    -83.59                                   
REMARK 500    THR A 319      -86.59   -127.66                                   
REMARK 500    HIS A 343      -18.01     83.75                                   
REMARK 500    THR A 426      -57.46   -128.11                                   
REMARK 500    SER A 457      -59.72   -120.81                                   
REMARK 500    ALA A 481      -86.70   -130.43                                   
REMARK 500    LEU A 484       78.46   -117.95                                   
REMARK 500    THR A 502      -84.45   -106.04                                   
REMARK 500    TRP A 515      -76.69    -77.31                                   
REMARK 500    ALA A 528      -60.06   -106.90                                   
REMARK 500    CYS A 581      178.00    173.26                                   
REMARK 500    VAL A 624      -75.03   -122.68                                   
REMARK 500    SER A 695     -161.89   -115.63                                   
REMARK 500    THR A 720       96.55    -64.57                                   
REMARK 500    LEU B   3      -18.07     76.86                                   
REMARK 500    ARG B 130      -39.75   -131.60                                   
REMARK 500    LYS B 160      -14.90     67.04                                   
REMARK 500    VAL B 197      -56.40   -123.44                                   
REMARK 500    LEU B 222      102.10     59.65                                   
REMARK 500    THR B 293     -103.61   -125.60                                   
REMARK 500    LEU B 478      -26.69     69.63                                   
REMARK 500    ILE B 492     -106.36   -116.36                                   
REMARK 500    CYS B 559     -169.21    172.49                                   
REMARK 500    TYR B 623      -70.93   -114.32                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      77 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     BCR 1  503                                                       
REMARK 610     CLA 1  505                                                       
REMARK 610     CLA 1  506                                                       
REMARK 610     CLA 1  509                                                       
REMARK 610     CLA 1  510                                                       
REMARK 610     CLA 1  511                                                       
REMARK 610     CHL 1  512                                                       
REMARK 610     CHL 1  514                                                       
REMARK 610     CLA 1  515                                                       
REMARK 610     CLA 1  516                                                       
REMARK 610     LMG 1  518                                                       
REMARK 610     LMG 1  519                                                       
REMARK 610     LHG 1  520                                                       
REMARK 610     CHL 1  521                                                       
REMARK 610     CLA 2  504                                                       
REMARK 610     CLA 2  505                                                       
REMARK 610     CLA 2  508                                                       
REMARK 610     CLA 2  509                                                       
REMARK 610     CLA 2  510                                                       
REMARK 610     CLA 2  511                                                       
REMARK 610     CHL 2  512                                                       
REMARK 610     CHL 2  513                                                       
REMARK 610     CLA 2  514                                                       
REMARK 610     CHL 2  515                                                       
REMARK 610     CHL 2  516                                                       
REMARK 610     LHG 2  517                                                       
REMARK 610     LMG 2  518                                                       
REMARK 610     LMG 2  519                                                       
REMARK 610     LMG 2  520                                                       
REMARK 610     LMG 2  521                                                       
REMARK 610     LMG 2  522                                                       
REMARK 610     LMG 2  524                                                       
REMARK 610     LMG 2  525                                                       
REMARK 610     CLA 3  305                                                       
REMARK 610     CLA 3  306                                                       
REMARK 610     CLA 3  307                                                       
REMARK 610     CLA 3  309                                                       
REMARK 610     CLA 3  310                                                       
REMARK 610     CLA 3  311                                                       
REMARK 610     CLA 3  312                                                       
REMARK 610     CLA 3  313                                                       
REMARK 610     CHL 3  314                                                       
REMARK 610     CLA 3  315                                                       
REMARK 610     CLA 3  316                                                       
REMARK 610     CLA 3  317                                                       
REMARK 610     LMT 3  318                                                       
REMARK 610     CLA 4  304                                                       
REMARK 610     CLA 4  305                                                       
REMARK 610     CLA 4  307                                                       
REMARK 610     CLA 4  308                                                       
REMARK 610     CLA 4  309                                                       
REMARK 610     CLA 4  310                                                       
REMARK 610     CLA 4  311                                                       
REMARK 610     CLA 4  312                                                       
REMARK 610     CHL 4  313                                                       
REMARK 610     CHL 4  314                                                       
REMARK 610     CHL 4  316                                                       
REMARK 610     CHL 4  317                                                       
REMARK 610     DGD 4  319                                                       
REMARK 610     LMG 4  321                                                       
REMARK 610     LMG 4  322                                                       
REMARK 610     CLA A  807                                                       
REMARK 610     CLA A  810                                                       
REMARK 610     CLA A  812                                                       
REMARK 610     CLA A  815                                                       
REMARK 610     CLA A  816                                                       
REMARK 610     CLA A  818                                                       
REMARK 610     CLA A  820                                                       
REMARK 610     CLA A  822                                                       
REMARK 610     CLA A  823                                                       
REMARK 610     CLA A  826                                                       
REMARK 610     CLA A  835                                                       
REMARK 610     CLA A  836                                                       
REMARK 610     CLA A  842                                                       
REMARK 610     LHG A  845                                                       
REMARK 610     LMG A  847                                                       
REMARK 610     DGD B  801                                                       
REMARK 610     CLA B  812                                                       
REMARK 610     CLA B  813                                                       
REMARK 610     CLA B  816                                                       
REMARK 610     CLA B  817                                                       
REMARK 610     CLA B  821                                                       
REMARK 610     CLA B  823                                                       
REMARK 610     CLA B  831                                                       
REMARK 610     CLA B  832                                                       
REMARK 610     CLA B  833                                                       
REMARK 610     CLA B  834                                                       
REMARK 610     CLA B  835                                                       
REMARK 610     CLA B  837                                                       
REMARK 610     LHG B  842                                                       
REMARK 610     LMG B  844                                                       
REMARK 610     LMG B  845                                                       
REMARK 610     LMT B  847                                                       
REMARK 610     DGD B  854                                                       
REMARK 610     LMT B  855                                                       
REMARK 610     LMG F  304                                                       
REMARK 610     LMG F  305                                                       
REMARK 610     CLA G  202                                                       
REMARK 610     CLA G  203                                                       
REMARK 610     LMG G  206                                                       
REMARK 610     DGD G  207                                                       
REMARK 610     LMT G  209                                                       
REMARK 610     LMG G  210                                                       
REMARK 610     CLA H 1000                                                       
REMARK 610     CLA J 1102                                                       
REMARK 610     LMG J 1103                                                       
REMARK 610     LMG J 1104                                                       
REMARK 610     CLA J 1105                                                       
REMARK 610     DGD J 1106                                                       
REMARK 610     LMT J 1107                                                       
REMARK 610     CLA K 1001                                                       
REMARK 610     CLA K 1002                                                       
REMARK 610     CLA K 1003                                                       
REMARK 610     CLA K 1004                                                       
REMARK 610     CLA L  301                                                       
REMARK 610     CLA L  303                                                       
REMARK 610     CLA L  304                                                       
REMARK 610     CLA L  305                                                       
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                             CHL 1 521  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP 1  41   O                                                      
REMARK 620 2 CHL 1 521   NA  100.7                                              
REMARK 620 3 CHL 1 521   NB  104.7  91.6                                        
REMARK 620 4 CHL 1 521   NC   77.5 174.3  94.1                                  
REMARK 620 5 CHL 1 521   ND   74.5  89.3 178.9  85.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 1 507  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 1  80   OE2                                                    
REMARK 620 2 CLA 1 507   NA   85.6                                              
REMARK 620 3 CLA 1 507   NB   94.8  89.0                                        
REMARK 620 4 CLA 1 507   NC  100.4 172.9  94.3                                  
REMARK 620 5 CLA 1 507   ND   92.4  92.8 172.7  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CHL 1 514  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 1 146   OE2                                                    
REMARK 620 2 CHL 1 514   NA   84.2                                              
REMARK 620 3 CHL 1 514   NB  111.5  85.8                                        
REMARK 620 4 CHL 1 514   NC   93.8 174.5  99.7                                  
REMARK 620 5 CHL 1 514   ND   68.6  94.4 179.8  80.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 1 504  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 1 184   OE2                                                    
REMARK 620 2 CLA 1 504   NA   98.0                                              
REMARK 620 3 CLA 1 504   NB   89.1  89.4                                        
REMARK 620 4 CLA 1 504   NC   86.9 174.0  94.1                                  
REMARK 620 5 CLA 1 504   ND   94.8  93.0 175.1  83.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 1 505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN 1 187   OD1                                                    
REMARK 620 2 CLA 1 505   NA   94.3                                              
REMARK 620 3 CLA 1 505   NB   92.5  89.1                                        
REMARK 620 4 CLA 1 505   NC   79.5 173.2  93.8                                  
REMARK 620 5 CLA 1 505   ND   79.1  93.5 171.3  82.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 1 516  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU 1 230   O                                                      
REMARK 620 2 CLA 1 516   NA   82.6                                              
REMARK 620 3 CLA 1 516   NB   91.7  89.2                                        
REMARK 620 4 CLA 1 516   NC   91.9 173.8  93.9                                  
REMARK 620 5 CLA 1 516   ND   79.9  93.0 171.0  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CHL 2 526  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP 2  67   O                                                      
REMARK 620 2 CHL 2 526   NA   86.2                                              
REMARK 620 3 CHL 2 526   NB   99.3  88.8                                        
REMARK 620 4 CHL 2 526   NC   91.8 174.4  96.7                                  
REMARK 620 5 CHL 2 526   ND   80.2  91.7 179.3  82.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 2 507  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 2 106   OE2                                                    
REMARK 620 2 CLA 2 507   NA   85.7                                              
REMARK 620 3 CLA 2 507   NB   97.3  89.1                                        
REMARK 620 4 CLA 2 507   NC  100.8 172.4  94.1                                  
REMARK 620 5 CLA 2 507   ND   90.2  93.0 172.3  83.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 2 514  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 2 164   OE1                                                    
REMARK 620 2 CLA 2 514   NA   68.8                                              
REMARK 620 3 CLA 2 514   NB   89.9  89.3                                        
REMARK 620 4 CLA 2 514   NC  119.3 171.3  93.9                                  
REMARK 620 5 CLA 2 514   ND   96.7  92.4 173.4  83.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CHL 2 516  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP 2 180   OD2                                                    
REMARK 620 2 CHL 2 516   NA   95.5                                              
REMARK 620 3 CHL 2 516   NB   88.2  89.0                                        
REMARK 620 4 CHL 2 516   NC   84.7 174.4  96.6                                  
REMARK 620 5 CHL 2 516   ND   92.1  91.9 179.0  82.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 2 504  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 2 221   OE2                                                    
REMARK 620 2 CLA 2 504   NA   98.8                                              
REMARK 620 3 CLA 2 504   NB   96.1  89.1                                        
REMARK 620 4 CLA 2 504   NC   87.9 172.1  94.4                                  
REMARK 620 5 CLA 2 504   ND   89.8  92.9 173.4  83.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 2 505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN 2 224   OD1                                                    
REMARK 620 2 CLA 2 505   NA   83.4                                              
REMARK 620 3 CLA 2 505   NB   94.3  88.9                                        
REMARK 620 4 CLA 2 505   NC   90.7 173.6  93.9                                  
REMARK 620 5 CLA 2 505   ND   81.1  93.4 174.6  83.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA 3 319  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP 3  85   O                                                      
REMARK 620 2 GLY 3  88   O    81.1                                              
REMARK 620 3 ILE A  20   O   148.2  89.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 3 313  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL 3 141   O                                                      
REMARK 620 2 CLA 3 313   NA   80.4                                              
REMARK 620 3 CLA 3 313   NB   81.6  88.9                                        
REMARK 620 4 CLA 3 313   NC  105.8 173.5  93.9                                  
REMARK 620 5 CLA 3 313   ND  107.5  93.3 170.8  83.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 3 315  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 3 169   OE1                                                    
REMARK 620 2 CLA 3 315   NA   72.6                                              
REMARK 620 3 CLA 3 315   NB   88.1  89.3                                        
REMARK 620 4 CLA 3 315   NC  114.6 172.2  93.8                                  
REMARK 620 5 CLA 3 315   ND   97.4  92.7 174.5  83.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 4 312  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP 4  56   O                                                      
REMARK 620 2 CLA 4 312   NA   86.3                                              
REMARK 620 3 CLA 4 312   NB  101.1  88.5                                        
REMARK 620 4 CLA 4 312   NC   96.5 176.1  93.8                                  
REMARK 620 5 CLA 4 312   ND   83.5  93.9 175.0  83.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 4 307  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 4  95   OE2                                                    
REMARK 620 2 CLA 4 307   NA   91.4                                              
REMARK 620 3 CLA 4 307   NB   90.8  88.9                                        
REMARK 620 4 CLA 4 307   NC   94.9 172.9  94.4                                  
REMARK 620 5 CLA 4 307   ND   97.4  92.9 171.6  82.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 4 308  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN 4  98   OD1                                                    
REMARK 620 2 CLA 4 308   NA   89.2                                              
REMARK 620 3 CLA 4 308   NB   86.7  88.8                                        
REMARK 620 4 CLA 4 308   NC   86.1 174.6  93.6                                  
REMARK 620 5 CLA 4 308   ND   84.5  93.8 170.8  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 4 315  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 4 153   OE1                                                    
REMARK 620 2 CLA 4 315   NA   81.9                                              
REMARK 620 3 CLA 4 315   NB  100.2  88.8                                        
REMARK 620 4 CLA 4 315   NC  104.0 172.8  94.2                                  
REMARK 620 5 CLA 4 315   ND   84.7  93.0 175.0  83.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CHL 4 317  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP 4 169   OD2                                                    
REMARK 620 2 CHL 4 317   NA   86.4                                              
REMARK 620 3 CHL 4 317   NB   68.7  84.0                                        
REMARK 620 4 CHL 4 317   NC   95.2 175.0 101.1                                  
REMARK 620 5 CHL 4 317   ND  111.7  97.0 179.0  78.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 4 304  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 4 204   OE2                                                    
REMARK 620 2 CLA 4 304   NA   92.1                                              
REMARK 620 3 CLA 4 304   NB   94.3  89.2                                        
REMARK 620 4 CLA 4 304   NC   93.9 172.8  94.3                                  
REMARK 620 5 CLA 4 304   ND   90.9  93.4 174.1  82.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 4 305  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN 4 207   OD1                                                    
REMARK 620 2 CLA 4 305   NA   75.7                                              
REMARK 620 3 CLA 4 305   NB   94.9  89.0                                        
REMARK 620 4 CLA 4 305   NC   98.8 174.0  93.9                                  
REMARK 620 5 CLA 4 305   ND   79.7  93.5 173.2  83.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 806  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A  85   OE1                                                    
REMARK 620 2 CLA A 806   NA   84.4                                              
REMARK 620 3 CLA A 806   NB   90.3  89.1                                        
REMARK 620 4 CLA A 806   NC   91.5 174.9  93.9                                  
REMARK 620 5 CLA A 806   ND   84.5  93.4 174.0  83.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 808  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 121   OE1                                                    
REMARK 620 2 CLA A 808   NA   93.9                                              
REMARK 620 3 CLA A 808   NB   94.3  88.8                                        
REMARK 620 4 CLA A 808   NC   92.4 172.8  94.3                                  
REMARK 620 5 CLA A 808   ND   93.2  93.2 172.0  82.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 809  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 129   OE1                                                    
REMARK 620 2 CLA A 809   NA   85.7                                              
REMARK 620 3 CLA A 809   NB   86.0  89.0                                        
REMARK 620 4 CLA A 809   NC  101.4 172.5  93.9                                  
REMARK 620 5 CLA A 809   ND  101.1  93.3 172.6  82.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 835  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 503   O                                                      
REMARK 620 2 CLA A 835   NA   79.9                                              
REMARK 620 3 CLA A 835   NB   95.7  89.1                                        
REMARK 620 4 CLA A 835   NC  104.3 174.6  93.9                                  
REMARK 620 5 CLA A 835   ND   82.8  93.7 176.6  83.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 843  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 581   SG                                                     
REMARK 620 2 SF4 A 843   S2  116.9                                              
REMARK 620 3 SF4 A 843   S3  121.7 104.7                                        
REMARK 620 4 SF4 A 843   S4  102.2 105.3 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 843  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 590   SG                                                     
REMARK 620 2 SF4 A 843   S1  133.6                                              
REMARK 620 3 SF4 A 843   S2  107.5 105.2                                        
REMARK 620 4 SF4 A 843   S3   99.0 103.8 104.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 807  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B  53   OE1                                                    
REMARK 620 2 CLA B 807   NA   88.7                                              
REMARK 620 3 CLA B 807   NB   85.0  89.1                                        
REMARK 620 4 CLA B 807   NC   85.8 173.5  93.9                                  
REMARK 620 5 CLA B 807   ND   88.1  93.1 172.7  83.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 810  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  93   OD2                                                    
REMARK 620 2 CLA B 810   NA   93.5                                              
REMARK 620 3 CLA B 810   NB   87.1  89.4                                        
REMARK 620 4 CLA B 810   NC   93.4 172.5  93.7                                  
REMARK 620 5 CLA B 810   ND   99.0  93.0 173.2  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 848  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B 501   O                                                      
REMARK 620 2 GLU B 503   O    95.1                                              
REMARK 620 3 ASN B 506   OD1 129.5  88.1                                        
REMARK 620 4 LEU B 508   O    83.2 174.6  89.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 843  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 559   SG                                                     
REMARK 620 2 SF4 A 843   S1   99.4                                              
REMARK 620 3 SF4 A 843   S3  131.9 104.7                                        
REMARK 620 4 SF4 A 843   S4  108.5 105.1 104.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 843  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 568   SG                                                     
REMARK 620 2 SF4 A 843   S1  113.9                                              
REMARK 620 3 SF4 A 843   S2  118.7 104.7                                        
REMARK 620 4 SF4 A 843   S4  110.7 102.9 104.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 102  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  11   SG                                                     
REMARK 620 2 SF4 C 102   S1  113.4                                              
REMARK 620 3 SF4 C 102   S3  117.2 104.5                                        
REMARK 620 4 SF4 C 102   S4  111.4 104.6 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 102  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  14   SG                                                     
REMARK 620 2 SF4 C 102   S2  104.9                                              
REMARK 620 3 SF4 C 102   S3  115.2 104.0                                        
REMARK 620 4 SF4 C 102   S4  121.9 104.7 104.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 102  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  17   SG                                                     
REMARK 620 2 SF4 C 102   S1  119.8                                              
REMARK 620 3 SF4 C 102   S2  122.9 104.7                                        
REMARK 620 4 SF4 C 102   S3   98.2 104.1 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 101  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  21   SG                                                     
REMARK 620 2 SF4 C 101   S2  106.4                                              
REMARK 620 3 SF4 C 101   S3  122.1 104.4                                        
REMARK 620 4 SF4 C 101   S4  112.5 105.2 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 101  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  48   SG                                                     
REMARK 620 2 SF4 C 101   S1  109.6                                              
REMARK 620 3 SF4 C 101   S2  114.6 104.0                                        
REMARK 620 4 SF4 C 101   S3  117.4 104.6 105.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 101  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  51   SG                                                     
REMARK 620 2 SF4 C 101   S1  122.1                                              
REMARK 620 3 SF4 C 101   S2  116.5 103.3                                        
REMARK 620 4 SF4 C 101   S4  104.8 103.9 104.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 101  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  54   SG                                                     
REMARK 620 2 SF4 C 101   S1  118.9                                              
REMARK 620 3 SF4 C 101   S3  120.3 103.5                                        
REMARK 620 4 SF4 C 101   S4  102.6 104.3 105.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA F 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER F 151   O                                                      
REMARK 620 2 CLA F 303   NA   84.9                                              
REMARK 620 3 CLA F 303   NB   99.5  89.1                                        
REMARK 620 4 CLA F 303   NC   89.3 174.0  93.7                                  
REMARK 620 5 CLA F 303   ND   73.2  93.1 172.1  83.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA G 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 119   OD2                                                    
REMARK 620 2 CLA G 203   NA   68.8                                              
REMARK 620 3 CLA G 203   NB   75.1  89.0                                        
REMARK 620 4 CLA G 203   NC  106.7 173.8  94.1                                  
REMARK 620 5 CLA G 203   ND   99.6  93.2 173.1  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA L 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU L 101   OE2                                                    
REMARK 620 2 CLA L 303   NA   85.1                                              
REMARK 620 3 CLA L 303   NB   90.0  89.1                                        
REMARK 620 4 CLA L 303   NC   99.3 174.8  93.7                                  
REMARK 620 5 CLA L 303   ND   98.2  93.3 171.6  83.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 2 510  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LHG 2 517   O5                                                     
REMARK 620 2 CLA 2 510   NA   77.6                                              
REMARK 620 3 CLA 2 510   NB   98.7  89.3                                        
REMARK 620 4 CLA 2 510   NC  107.9 173.1  93.9                                  
REMARK 620 5 CLA 2 510   ND   86.3  93.1 174.8  83.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 3 310  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH 3 402   O                                                      
REMARK 620 2 CLA 3 310   NA   70.6                                              
REMARK 620 3 CLA 3 310   NB  106.9  89.2                                        
REMARK 620 4 CLA 3 310   NC  113.0 174.3  93.8                                  
REMARK 620 5 CLA 3 310   ND   77.5  93.3 175.4  83.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CHL 4 314  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH 4 408   O                                                      
REMARK 620 2 CHL 4 314   NA   90.3                                              
REMARK 620 3 CHL 4 314   NB  114.0  76.4                                        
REMARK 620 4 CHL 4 314   NC   87.7 175.7 107.8                                  
REMARK 620 5 CHL 4 314   ND   66.5 102.9 179.1  72.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 803  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 910   O                                                      
REMARK 620 2 CLA A 803   NA  100.5                                              
REMARK 620 3 CLA A 803   NB   92.1  90.1                                        
REMARK 620 4 CLA A 803   NC   87.0 171.7  93.2                                  
REMARK 620 5 CLA A 803   ND   89.3  92.7 176.6  83.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 825  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 905   O                                                      
REMARK 620 2 CLA A 825   NA   79.2                                              
REMARK 620 3 CLA A 825   NB   89.3  89.2                                        
REMARK 620 4 CLA A 825   NC   96.6 175.2  93.1                                  
REMARK 620 5 CLA A 825   ND   86.8  93.4 174.9  84.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 826  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 924   O                                                      
REMARK 620 2 CLA A 826   NA   81.6                                              
REMARK 620 3 CLA A 826   NB  102.0  89.2                                        
REMARK 620 4 CLA A 826   NC  105.7 171.0  94.4                                  
REMARK 620 5 CLA A 826   ND   86.5  92.6 171.5  82.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 840  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 919   O                                                      
REMARK 620 2 CLA A 840   NA   85.7                                              
REMARK 620 3 CLA A 840   NB   95.9  89.2                                        
REMARK 620 4 CLA A 840   NC  102.2 171.0  94.2                                  
REMARK 620 5 CLA A 840   ND   91.2  92.6 172.8  83.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 842  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LHG A 845   O5                                                     
REMARK 620 2 CLA A 842   NA   92.8                                              
REMARK 620 3 CLA A 842   NB   98.5  89.5                                        
REMARK 620 4 CLA A 842   NC   92.5 173.2  93.9                                  
REMARK 620 5 CLA A 842   ND   87.1  92.9 173.8  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 854  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 904   O                                                      
REMARK 620 2 CLA A 854   NA   94.4                                              
REMARK 620 3 CLA A 854   NB   84.5  89.0                                        
REMARK 620 4 CLA A 854   NC   91.1 173.8  94.3                                  
REMARK 620 5 CLA A 854   ND   93.2  93.8 176.5  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 820  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 914   O                                                      
REMARK 620 2 CLA B 820   NA   78.6                                              
REMARK 620 3 CLA B 820   NB  101.8  88.9                                        
REMARK 620 4 CLA B 820   NC  107.9 171.9  94.3                                  
REMARK 620 5 CLA B 820   ND   85.7  92.8 172.5  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 824  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 957   O                                                      
REMARK 620 2 CLA B 824   NA   81.7                                              
REMARK 620 3 CLA B 824   NB  104.8  89.8                                        
REMARK 620 4 CLA B 824   NC   93.1 174.5  93.3                                  
REMARK 620 5 CLA B 824   ND   76.1  93.3 176.8  83.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 825  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 953   O                                                      
REMARK 620 2 CLA B 825   NA   90.9                                              
REMARK 620 3 CLA B 825   NB  111.3  89.4                                        
REMARK 620 4 CLA B 825   NC   96.5 170.1  94.0                                  
REMARK 620 5 CLA B 825   ND   75.2  92.4 173.3  83.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 834  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 903   O                                                      
REMARK 620 2 CLA B 834   NA   84.8                                              
REMARK 620 3 CLA B 834   NB   93.6  88.5                                        
REMARK 620 4 CLA B 834   NC  101.4 172.8  94.8                                  
REMARK 620 5 CLA B 834   ND   95.5  93.4 170.8  82.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 838  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 924   O                                                      
REMARK 620 2 CLA B 838   NA   71.8                                              
REMARK 620 3 CLA B 838   NB   89.6  89.3                                        
REMARK 620 4 CLA B 838   NC  116.0 171.6  93.9                                  
REMARK 620 5 CLA B 838   ND  100.3  92.2 170.0  83.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 840  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LHG B 842   O5                                                     
REMARK 620 2 CLA B 840   NA   92.6                                              
REMARK 620 3 CLA B 840   NB   87.5  88.1                                        
REMARK 620 4 CLA B 840   NC   82.2 174.1  94.4                                  
REMARK 620 5 CLA B 840   ND   84.5  94.2 171.7  82.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA G 204  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH G 301   O                                                      
REMARK 620 2 CLA G 204   NA   95.0                                              
REMARK 620 3 CLA G 204   NB   94.5  89.0                                        
REMARK 620 4 CLA G 204   NC   88.9 174.7  94.3                                  
REMARK 620 5 CLA G 204   ND   92.8  93.3 172.1  82.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA J1102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH J1203   O                                                      
REMARK 620 2 CLA J1102   NA   87.9                                              
REMARK 620 3 CLA J1102   NB   94.1  88.9                                        
REMARK 620 4 CLA J1102   NC  101.6 169.8  94.1                                  
REMARK 620 5 CLA J1102   ND   92.3  93.0 173.4  83.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA L 305  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH L 401   O                                                      
REMARK 620 2 CLA L 305   NA   93.7                                              
REMARK 620 3 CLA L 305   NB   84.2  89.3                                        
REMARK 620 4 CLA L 305   NC   92.8 173.1  93.7                                  
REMARK 620 5 CLA L 305   ND  103.3  93.1 171.9  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LUT 1 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LUT 1 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR 1 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 1 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 1 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 1 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG 1 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 1 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 1 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG 1 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 1 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LUT 2 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XAT 2 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR 2 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 2 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 2 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 2 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 2 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG 2 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 2 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 2 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 2 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 2 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 2 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT 2 523                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 2 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 2 525                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 2 526                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LUT 3 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LUT 3 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR 3 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR 3 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 312                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 3 314                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 315                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 316                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 317                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT 3 318                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA 3 319                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR 4 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LUT 4 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XAT 4 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 312                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 4 313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 4 314                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 315                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 4 316                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CHL 4 317                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 318                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD 4 319                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT 4 320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 4 321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG 4 322                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL0 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 810                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 811                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 812                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 813                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 814                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 815                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 816                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 817                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 818                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 819                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 820                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 821                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 822                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 823                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 824                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 825                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 826                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 827                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 828                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 829                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 830                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 831                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 832                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 833                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 834                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 835                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 836                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 837                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 838                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 839                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 840                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 841                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 842                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 A 843                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PQN A 844                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 845                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT A 846                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG A 847                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 848                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 849                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 850                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 851                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 852                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 853                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 854                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 855                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 856                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 810                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 811                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 812                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 813                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 814                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 815                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 816                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 817                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 818                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 819                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 820                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 821                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 822                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 823                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 824                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 825                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 826                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 827                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 828                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 829                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 830                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 831                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 832                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 833                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 834                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 835                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 836                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 837                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 838                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 839                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 840                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PQN B 841                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG B 842                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG B 843                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 844                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 845                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AX1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 846                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AX2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 847                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AX3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 848                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AX4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 849                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AX5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 850                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AX6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 851                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AX7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 852                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AX8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 853                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AX9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD B 854                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AY1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT B 855                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AY2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 856                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AY3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 C 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AY4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 C 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AY5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZEX F 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AY6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA F 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AY7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA F 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AY8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG F 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AY9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG F 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AZ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR F 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AZ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AZ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA G 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AZ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA G 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AZ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA G 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AZ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR G 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AZ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG G 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AZ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD G 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AZ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT G 208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT G 209                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG G 210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA H 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR I 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR I 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA J 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA J 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG J 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG J 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA J 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD J 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT J 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR J 1108                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LUT J 1109                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA K 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA K 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA K 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA K 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA L 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR L 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA L 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA L 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA L 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR L 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR L 307                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Y28   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1JB0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4XK8   RELATED DB: PDB                                   
DBREF  5L8R 1   40   232  PDB    5L8R     5L8R            40    232             
DBREF  5L8R 2    1   269  UNP    Q41038   Q41038_PEA       1    269             
DBREF  5L8R 3    1   275  UNP    Q32904   CB23_PEA         1    275             
DBREF  5L8R 4   52   249  UNP    Q9SQL2   CB24_PEA        52    249             
DBREF  5L8R A    1   758  UNP    P05310   PSAA_PEA         1    758             
DBREF1 5L8R B    1   734  UNP                  A0A0F6NGI2_PEA                   
DBREF2 5L8R B     A0A0F6NGI2                          1         734             
DBREF  5L8R C    1    81  UNP    P10793   PSAC_PEA         1     81             
DBREF  5L8R D   69   211  PDB    5L8R     5L8R            69    211             
DBREF  5L8R E   66   129  UNP    E1C9K6   E1C9K6_PEA       1     64             
DBREF1 5L8R F   78   231  UNP                  A0A0M3KL12_PEA                   
DBREF2 5L8R F     A0A0M3KL12                          1         154             
DBREF  5L8R G   58   154  PDB    5L8R     5L8R            58    154             
DBREF1 5L8R H   53   138  UNP                  A0A0M3KL10_PEA                   
DBREF2 5L8R H     A0A0M3KL10                          2          87             
DBREF  5L8R I    1    40  UNP    P17227   PSAI_PEA         1     40             
DBREF  5L8R J    1    42  UNP    D5MAL3   D5MAL3_PEA       1     42             
DBREF  5L8R K   47   125  UNP    E1C9L3   E1C9L3_PEA       3     82             
DBREF  5L8R L   54   210  UNP    E1C9L1   E1C9L1_PEA       4    160             
SEQADV 5L8R LYS 4   89  UNP  Q9SQL2    ARG    89 CONFLICT                       
SEQADV 5L8R ASP 4  128  UNP  Q9SQL2    ALA   128 CONFLICT                       
SEQADV 5L8R PHE 4  149  UNP  Q9SQL2    SER   149 CONFLICT                       
SEQADV 5L8R ARG A  117  UNP  P05310    GLY   117 CONFLICT                       
SEQADV 5L8R ALA A  176  UNP  P05310    GLY   176 CONFLICT                       
SEQADV 5L8R VAL A  194  UNP  P05310    ALA   194 CONFLICT                       
SEQADV 5L8R GLY A  220  UNP  P05310    ARG   220 CONFLICT                       
SEQADV 5L8R ILE A  371  UNP  P05310    VAL   371 CONFLICT                       
SEQADV 5L8R HIS A  374  UNP  P05310    GLN   374 CONFLICT                       
SEQADV 5L8R ALA A  378  UNP  P05310    SER   378 CONFLICT                       
SEQADV 5L8R GLY A  390  UNP  P05310    ALA   390 CONFLICT                       
SEQADV 5L8R THR A  509  UNP  P05310    ALA   509 CONFLICT                       
SEQADV 5L8R SER A  522  UNP  P05310    ALA   522 CONFLICT                       
SEQADV 5L8R GLY A  525  UNP  P05310    ASN   525 CONFLICT                       
SEQADV 5L8R ALA A  608  UNP  P05310    SER   608 CONFLICT                       
SEQADV 5L8R SER A  627  UNP  P05310    THR   627 CONFLICT                       
SEQADV 5L8R GLY A  639  UNP  P05310    ALA   639 CONFLICT                       
SEQADV 5L8R PRO E   64  UNP  E1C9K6              EXPRESSION TAG                 
SEQADV 5L8R PRO E   65  UNP  E1C9K6              EXPRESSION TAG                 
SEQADV 5L8R GLN E   79  UNP  E1C9K6    LYS    14 CONFLICT                       
SEQADV 5L8R VAL E  125  UNP  E1C9K6    ILE    60 CONFLICT                       
SEQADV 5L8R GLU E  126  UNP  E1C9K6    VAL    61 CONFLICT                       
SEQADV 5L8R LYS E  129  UNP  E1C9K6    GLU    64 CONFLICT                       
SEQADV 5L8R ALA F   80  UNP  A0A0M3KL1 SER     3 CONFLICT                       
SEQADV 5L8R ASP F   87  UNP  A0A0M3KL1 GLU    10 CONFLICT                       
SEQADV 5L8R LEU F  108  UNP  A0A0M3KL1 ILE    31 CONFLICT                       
SEQADV 5L8R PRO F  111  UNP  A0A0M3KL1 ALA    34 CONFLICT                       
SEQADV 5L8R GLY F  134  UNP  A0A0M3KL1 ALA    57 CONFLICT                       
SEQADV 5L8R ASP F  188  UNP  A0A0M3KL1 GLU   111 CONFLICT                       
SEQADV 5L8R THR F  204  UNP  A0A0M3KL1 SER   127 CONFLICT                       
SEQADV 5L8R LEU H   60  UNP  A0A0M3KL1 ILE     9 CONFLICT                       
SEQADV 5L8R ASN H   79  UNP  A0A0M3KL1 SER    28 CONFLICT                       
SEQADV 5L8R SER H   80  UNP  A0A0M3KL1 PRO    29 CONFLICT                       
SEQADV 5L8R ALA H  116  UNP  A0A0M3KL1 THR    65 CONFLICT                       
SEQADV 5L8R LYS H  126  UNP  A0A0M3KL1 VAL    75 CONFLICT                       
SEQADV 5L8R GLN H  134  UNP  A0A0M3KL1 LYS    83 CONFLICT                       
SEQADV 5L8R LEU H  139  UNP  A0A0M3KL1           EXPRESSION TAG                 
SEQADV 5L8R GLY H  140  UNP  A0A0M3KL1           EXPRESSION TAG                 
SEQADV 5L8R PHE J   32  UNP  D5MAL3    LEU    32 CONFLICT                       
SEQADV 5L8R ALA K   85  UNP  E1C9L3    VAL    42 CONFLICT                       
SEQADV 5L8R VAL L   57  UNP  E1C9L1    ILE     7 CONFLICT                       
SEQADV 5L8R VAL L   79  UNP  E1C9L1    ILE    29 CONFLICT                       
SEQADV 5L8R GLY L   88  UNP  E1C9L1    ALA    38 CONFLICT                       
SEQADV 5L8R ASN L   94  UNP  E1C9L1    SER    44 CONFLICT                       
SEQADV 5L8R PHE L  108  UNP  E1C9L1    TYR    58 CONFLICT                       
SEQADV 5L8R ILE L  143  UNP  E1C9L1    LEU    93 CONFLICT                       
SEQADV 5L8R ASP L  157  UNP  E1C9L1    ALA   107 CONFLICT                       
SEQADV 5L8R GLN L  172  UNP  E1C9L1    GLU   122 CONFLICT                       
SEQADV 5L8R PHE L  201  UNP  E1C9L1    TYR   151 CONFLICT                       
SEQRES   1 1  193  ASP TRP MET PRO GLY GLN PRO ARG PRO SER TYR LEU ASP          
SEQRES   2 1  193  GLY SER ALA PRO GLY ASP PHE GLY PHE ASP PRO LEU ARG          
SEQRES   3 1  193  LEU GLY GLU VAL PRO GLU ASN LEU GLU ARG PHE LYS GLU          
SEQRES   4 1  193  SER GLU LEU ILE HIS CYS ARG TRP ALA MET LEU ALA VAL          
SEQRES   5 1  193  PRO GLY ILE LEU VAL PRO GLU ALA LEU GLY LEU GLY ASN          
SEQRES   6 1  193  TRP VAL LYS ALA GLN GLU TRP ALA ALA LEU PRO GLY GLY          
SEQRES   7 1  193  GLN ALA THR TYR LEU GLY ASN PRO VAL PRO TRP GLY THR          
SEQRES   8 1  193  LEU PRO THR ILE LEU VAL ILE GLU PHE LEU SER ILE ALA          
SEQRES   9 1  193  PHE VAL GLU HIS GLN ARG SER MET GLU LYS ASP PRO GLU          
SEQRES  10 1  193  LYS LYS LYS TYR PRO GLY GLY ALA PHE ASP PRO LEU GLY          
SEQRES  11 1  193  TYR SER LYS ASP PRO LYS LYS PHE HIS GLU TYR LYS ILE          
SEQRES  12 1  193  LYS GLU VAL LYS ASN GLY ARG LEU ALA LEU LEU ALA PHE          
SEQRES  13 1  193  VAL GLY ILE CYS VAL GLN GLN SER ALA TYR PRO GLY THR          
SEQRES  14 1  193  GLY PRO LEU GLU ASN LEU ALA THR HIS LEU ALA ASP PRO          
SEQRES  15 1  193  TRP HIS ASN THR ILE GLY ASN VAL LEU ILE PRO                  
SEQRES   1 2  269  MET ALA SER ALA CYS ALA SER SER ALA ILE ALA ALA VAL          
SEQRES   2 2  269  ALA ILE SER THR PRO SER SER GLN LYS ASN GLY SER PRO          
SEQRES   3 2  269  SER GLY THR SER LYS ALA PHE LEU GLY ARG LYS LEU LYS          
SEQRES   4 2  269  VAL ASN SER SER THR ALA SER PRO SER ARG VAL ARG SER          
SEQRES   5 2  269  THR SER THR VAL CYS THR VAL ALA GLU PRO ASP ARG PRO          
SEQRES   6 2  269  LEU TRP PHE PRO GLY SER THR PRO PRO PRO TRP LEU ASP          
SEQRES   7 2  269  GLY SER LEU PRO GLY ASP PHE GLY PHE ASP PRO LEU GLY          
SEQRES   8 2  269  LEU GLY SER ASP PRO GLU SER LEU ARG TRP ASN VAL GLN          
SEQRES   9 2  269  ALA GLU LEU VAL HIS SER ARG TRP ALA MET LEU GLY ALA          
SEQRES  10 2  269  ALA GLY ILE PHE ILE PRO GLU PHE LEU THR LYS LEU GLY          
SEQRES  11 2  269  ILE LEU ASN THR PRO SER TRP TYR THR ALA GLY GLU GLN          
SEQRES  12 2  269  GLU TYR PHE THR ASP THR THR THR LEU PHE ILE VAL GLU          
SEQRES  13 2  269  LEU VAL PHE ILE GLY TRP ALA GLU GLY ARG ARG TRP ALA          
SEQRES  14 2  269  ASP ILE LEU ASN PRO GLY CYS VAL ASN THR ASP PRO ILE          
SEQRES  15 2  269  PHE PRO ASN ASN LYS LEU THR GLY THR ASP VAL GLY TYR          
SEQRES  16 2  269  PRO GLY GLY LEU TRP PHE ASP PRO LEU GLY TRP GLY SER          
SEQRES  17 2  269  ALA SER PRO GLN LYS LEU LYS GLU LEU ARG THR LYS GLU          
SEQRES  18 2  269  ILE LYS ASN GLY ARG LEU ALA MET LEU ALA VAL MET GLY          
SEQRES  19 2  269  ALA TRP PHE GLN HIS ILE TYR THR GLY THR GLY PRO ILE          
SEQRES  20 2  269  ASP ASN LEU PHE ALA HIS LEU ALA ASP PRO GLY HIS ALA          
SEQRES  21 2  269  THR ILE PHE ALA ALA PHE THR PRO LYS                          
SEQRES   1 3  275  MET ALA THR GLN ALA LEU VAL SER SER SER SER LEU THR          
SEQRES   2 3  275  PHE ALA ALA GLU ALA VAL ARG GLN SER PHE ARG ALA ARG          
SEQRES   3 3  275  SER LEU PRO SER SER VAL GLY CYS SER ARG LYS GLY LEU          
SEQRES   4 3  275  VAL ARG ALA ALA ALA THR PRO PRO VAL LYS GLN GLY GLY          
SEQRES   5 3  275  VAL ASP ARG PRO LEU TRP PHE ALA SER LYS GLN SER LEU          
SEQRES   6 3  275  SER TYR LEU ASP GLY SER LEU PRO GLY ASP TYR GLY PHE          
SEQRES   7 3  275  ASP PRO LEU GLY LEU SER ASP PRO GLU GLY THR GLY GLY          
SEQRES   8 3  275  PHE ILE GLU PRO ARG TRP LEU ALA TYR GLY GLU VAL ILE          
SEQRES   9 3  275  ASN GLY ARG PHE ALA MET LEU GLY ALA VAL GLY ALA ILE          
SEQRES  10 3  275  ALA PRO GLU TYR LEU GLY LYS VAL GLY LEU ILE PRO GLN          
SEQRES  11 3  275  GLU THR ALA LEU ALA TRP PHE GLN THR GLY VAL ILE PRO          
SEQRES  12 3  275  PRO ALA GLY THR TYR ASN TYR TRP ALA ASP ASN TYR THR          
SEQRES  13 3  275  LEU PHE VAL LEU GLU MET ALA LEU MET GLY PHE ALA GLU          
SEQRES  14 3  275  HIS ARG ARG PHE GLN ASP TRP ALA LYS PRO GLY SER MET          
SEQRES  15 3  275  GLY LYS GLN TYR PHE LEU GLY LEU GLU LYS GLY PHE GLY          
SEQRES  16 3  275  GLY SER GLY ASN PRO ALA TYR PRO GLY GLY PRO PHE PHE          
SEQRES  17 3  275  ASN PRO LEU GLY PHE GLY LYS ASP GLU LYS SER LEU LYS          
SEQRES  18 3  275  GLU LEU LYS LEU LYS GLU VAL LYS ASN GLY ARG LEU ALA          
SEQRES  19 3  275  MET LEU ALA ILE LEU GLY TYR PHE ILE GLN GLY LEU VAL          
SEQRES  20 3  275  THR GLY VAL GLY PRO TYR GLN ASN LEU LEU ASP HIS VAL          
SEQRES  21 3  275  ALA ASP PRO VAL ASN ASN ASN VAL LEU THR SER LEU LYS          
SEQRES  22 3  275  PHE HIS                                                      
SEQRES   1 4  198  LYS LYS GLY GLU TRP LEU PRO GLY LEU ALA SER PRO GLY          
SEQRES   2 4  198  TYR LEU THR GLY SER LEU PRO GLY ASP ASN GLY PHE ASP          
SEQRES   3 4  198  PRO LEU GLY LEU ALA GLU ASP PRO GLU ASN LEU LYS TRP          
SEQRES   4 4  198  PHE VAL GLN ALA GLU LEU VAL ASN GLY ARG TRP ALA MET          
SEQRES   5 4  198  LEU GLY VAL ALA GLY MET LEU LEU PRO GLU VAL PHE THR          
SEQRES   6 4  198  SER ILE GLY ILE ILE ASN VAL PRO LYS TRP TYR ASP ALA          
SEQRES   7 4  198  GLY LYS GLU GLU TYR PHE ALA SER SER SER THR LEU PHE          
SEQRES   8 4  198  VAL ILE GLU PHE ILE LEU PHE HIS TYR VAL GLU ILE ARG          
SEQRES   9 4  198  ARG TRP GLN ASP ILE LYS ASN PRO GLY SER VAL ASN GLN          
SEQRES  10 4  198  ASP PRO ILE PHE LYS GLN TYR SER LEU PRO ALA GLY GLU          
SEQRES  11 4  198  VAL GLY TYR PRO GLY GLY ILE PHE ASN PRO LEU ASN PHE          
SEQRES  12 4  198  ALA PRO THR LEU GLU ALA LYS GLU LYS GLU ILE ALA ASN          
SEQRES  13 4  198  GLY ARG LEU ALA MET LEU ALA PHE LEU GLY PHE ILE ILE          
SEQRES  14 4  198  GLN HIS ASN VAL THR GLY LYS GLY PRO PHE ASP ASN LEU          
SEQRES  15 4  198  LEU GLN HIS ILE SER ASP PRO TRP HIS ASN THR ILE VAL          
SEQRES  16 4  198  GLN THR LEU                                                  
SEQRES   1 A  758  MET ILE ILE ARG SER PRO GLU PRO LYS VAL GLN ILE LEU          
SEQRES   2 A  758  ALA ASP PRO GLU VAL LYS ILE LEU VAL ASP ARG ASP PRO          
SEQRES   3 A  758  ILE LYS THR SER PHE GLU GLN TRP ALA LYS PRO GLY HIS          
SEQRES   4 A  758  PHE SER ARG THR ILE ALA LYS GLY PRO ASP THR THR THR          
SEQRES   5 A  758  TRP ILE TRP ASN LEU HIS ALA ASP ALA HIS ASP PHE ASP          
SEQRES   6 A  758  SER HIS THR SER ASP LEU GLU GLU ILE SER ARG LYS VAL          
SEQRES   7 A  758  PHE SER ALA HIS PHE GLY GLN LEU SER ILE ILE PHE LEU          
SEQRES   8 A  758  TRP LEU SER GLY MET TYR PHE HIS GLY ALA ARG PHE SER          
SEQRES   9 A  758  ASN TYR GLU ALA TRP LEU ASN ASP PRO THR HIS ILE ARG          
SEQRES  10 A  758  PRO SER ALA GLN VAL VAL TRP PRO ILE VAL GLY GLN GLU          
SEQRES  11 A  758  ILE LEU ASN GLY ASP VAL GLY GLY GLY PHE ARG GLY ILE          
SEQRES  12 A  758  GLN ILE THR SER GLY PHE PHE GLN ILE TRP ARG ALA SER          
SEQRES  13 A  758  GLY ILE THR SER GLU LEU GLN LEU TYR CYS THR ALA ILE          
SEQRES  14 A  758  GLY ALA LEU VAL PHE ALA ALA LEU MET LEU PHE ALA GLY          
SEQRES  15 A  758  TRP PHE HIS TYR HIS LYS ALA ALA PRO LYS LEU VAL TRP          
SEQRES  16 A  758  PHE GLN ASP VAL GLU SER MET LEU ASN HIS HIS LEU ALA          
SEQRES  17 A  758  GLY LEU LEU GLY LEU GLY SER LEU SER TRP ALA GLY HIS          
SEQRES  18 A  758  GLN VAL HIS VAL SER LEU PRO ILE ASN GLN PHE LEU ASN          
SEQRES  19 A  758  ALA GLY VAL ASP PRO LYS GLU ILE PRO LEU PRO HIS GLU          
SEQRES  20 A  758  PHE ILE LEU ASN ARG ASP LEU LEU ALA GLN LEU TYR PRO          
SEQRES  21 A  758  SER PHE ALA GLU GLY ALA THR PRO PHE PHE THR LEU ASN          
SEQRES  22 A  758  TRP SER LYS TYR ALA ASP PHE LEU THR PHE ARG GLY GLY          
SEQRES  23 A  758  LEU ASP PRO LEU THR GLY GLY LEU TRP LEU THR ASP ILE          
SEQRES  24 A  758  ALA HIS HIS HIS LEU ALA ILE ALA ILE LEU PHE LEU ILE          
SEQRES  25 A  758  ALA GLY HIS MET TYR ARG THR ASN TRP GLY ILE GLY HIS          
SEQRES  26 A  758  GLY ILE LYS ASP ILE LEU GLU ALA HIS LYS GLY PRO PHE          
SEQRES  27 A  758  THR GLY GLN GLY HIS LYS GLY LEU TYR GLU ILE LEU THR          
SEQRES  28 A  758  THR SER TRP HIS ALA GLN LEU SER ILE ASN LEU ALA MET          
SEQRES  29 A  758  LEU GLY SER LEU THR ILE ILE VAL ALA HIS HIS MET TYR          
SEQRES  30 A  758  ALA MET PRO PRO TYR PRO TYR LEU ALA THR ASP TYR GLY          
SEQRES  31 A  758  THR GLN LEU SER LEU PHE THR HIS HIS MET TRP ILE GLY          
SEQRES  32 A  758  GLY PHE LEU ILE VAL GLY ALA ALA ALA HIS ALA ALA ILE          
SEQRES  33 A  758  PHE MET VAL ARG ASP TYR ASP PRO THR THR ARG TYR ASN          
SEQRES  34 A  758  ASP LEU LEU ASP ARG VAL LEU ARG HIS ARG ASP ALA ILE          
SEQRES  35 A  758  ILE SER HIS LEU ASN TRP VAL CYS ILE PHE LEU GLY PHE          
SEQRES  36 A  758  HIS SER PHE GLY LEU TYR ILE HIS ASN ASP THR MET SER          
SEQRES  37 A  758  ALA LEU GLY ARG PRO GLN ASP MET PHE SER ASP THR ALA          
SEQRES  38 A  758  ILE GLN LEU GLN PRO VAL PHE ALA GLN TRP ILE GLN ASN          
SEQRES  39 A  758  THR HIS ALA LEU ALA PRO GLY THR THR ALA PRO GLY ALA          
SEQRES  40 A  758  THR THR SER THR SER LEU THR TRP GLY GLY GLY ASP LEU          
SEQRES  41 A  758  VAL SER VAL GLY GLY LYS VAL ALA LEU LEU PRO ILE PRO          
SEQRES  42 A  758  LEU GLY THR ALA ASP PHE LEU VAL HIS HIS ILE HIS ALA          
SEQRES  43 A  758  PHE THR ILE HIS VAL THR VAL LEU ILE LEU LEU LYS GLY          
SEQRES  44 A  758  VAL LEU PHE ALA ARG SER SER ARG LEU ILE PRO ASP LYS          
SEQRES  45 A  758  ALA ASN LEU GLY PHE ARG PHE PRO CYS ASP GLY PRO GLY          
SEQRES  46 A  758  ARG GLY GLY THR CYS GLN VAL SER ALA TRP ASP HIS VAL          
SEQRES  47 A  758  PHE LEU GLY LEU PHE TRP MET TYR ASN ALA ILE SER VAL          
SEQRES  48 A  758  VAL ILE PHE HIS PHE SER TRP LYS MET GLN SER ASP VAL          
SEQRES  49 A  758  TRP GLY SER ILE ASN ASP GLN GLY VAL VAL THR HIS ILE          
SEQRES  50 A  758  THR GLY GLY ASN PHE ALA GLN SER SER ILE THR ILE ASN          
SEQRES  51 A  758  GLY TRP LEU ARG ASP PHE LEU TRP ALA GLN ALA SER GLN          
SEQRES  52 A  758  VAL ILE GLN SER TYR GLY SER SER LEU SER ALA TYR GLY          
SEQRES  53 A  758  LEU PHE PHE LEU GLY ALA HIS PHE VAL TRP ALA PHE SER          
SEQRES  54 A  758  LEU MET PHE LEU PHE SER GLY ARG GLY TYR TRP GLN GLU          
SEQRES  55 A  758  LEU ILE GLU SER ILE VAL TRP ALA HIS ASN LYS LEU LYS          
SEQRES  56 A  758  VAL ALA PRO ALA THR GLN PRO ARG ALA LEU SER ILE VAL          
SEQRES  57 A  758  GLN GLY ARG ALA VAL GLY VAL THR HIS TYR LEU LEU GLY          
SEQRES  58 A  758  GLY ILE ALA THR THR TRP ALA PHE PHE LEU ALA ARG ILE          
SEQRES  59 A  758  ILE ALA VAL GLY                                              
SEQRES   1 B  734  MET ALA LEU ARG PHE PRO ARG PHE SER GLN GLY LEU ALA          
SEQRES   2 B  734  GLN ASP PRO THR THR ARG ARG ILE TRP PHE GLY ILE ALA          
SEQRES   3 B  734  THR ALA HIS ASP PHE GLU SER HIS ASP ASP ILE THR GLU          
SEQRES   4 B  734  GLY ARG LEU TYR GLN ASN ILE PHE ALA SER HIS PHE GLY          
SEQRES   5 B  734  GLN LEU ALA ILE ILE PHE LEU TRP THR SER GLY ASN LEU          
SEQRES   6 B  734  PHE HIS VAL ALA TRP GLN GLY ASN PHE GLU ALA TRP VAL          
SEQRES   7 B  734  GLN ASP PRO LEU HIS VAL ARG PRO ILE ALA HIS ALA ILE          
SEQRES   8 B  734  TRP ASP PRO HIS PHE GLY GLN PRO ALA VAL GLU ALA PHE          
SEQRES   9 B  734  THR ARG GLY GLY ALA LEU GLY PRO VAL ASN ILE ALA TYR          
SEQRES  10 B  734  SER GLY VAL TYR GLN TRP TRP TYR THR ILE GLY LEU ARG          
SEQRES  11 B  734  THR ASN GLU ASP LEU TYR THR GLY ALA ILE PHE LEU LEU          
SEQRES  12 B  734  PHE LEU SER PHE ILE SER LEU LEU ALA GLY TRP LEU HIS          
SEQRES  13 B  734  LEU GLN PRO LYS TRP LYS PRO SER VAL SER TRP PHE LYS          
SEQRES  14 B  734  ASN ALA GLU SER ARG LEU ASN HIS HIS LEU SER GLY LEU          
SEQRES  15 B  734  PHE GLY VAL SER SER LEU ALA TRP ALA GLY HIS LEU VAL          
SEQRES  16 B  734  HIS VAL ALA ILE PRO GLY SER ARG GLY GLU TYR VAL ARG          
SEQRES  17 B  734  TRP ASN ASN PHE LEU SER VAL LEU PRO HIS PRO GLN GLY          
SEQRES  18 B  734  LEU GLY PRO LEU PHE THR GLY GLN TRP ASN LEU TYR ALA          
SEQRES  19 B  734  GLN ASN PRO ASP SER SER ASN HIS LEU PHE SER THR SER          
SEQRES  20 B  734  GLN GLY ALA GLY THR ALA ILE LEU THR LEU LEU GLY GLY          
SEQRES  21 B  734  PHE HIS PRO GLN THR GLN SER LEU TRP LEU THR ASP MET          
SEQRES  22 B  734  ALA HIS HIS HIS LEU ALA ILE ALA ILE LEU PHE LEU ILE          
SEQRES  23 B  734  GLY GLY HIS MET TYR ARG THR ASN PHE GLY ILE GLY HIS          
SEQRES  24 B  734  SER ILE LYS TYR ILE LEU GLU ALA HIS ILE PRO PRO GLY          
SEQRES  25 B  734  GLY ARG LEU GLY ARG GLY HIS LYS GLY LEU TYR ASP THR          
SEQRES  26 B  734  ILE ASN ASN SER ILE HIS PHE GLN LEU GLY LEU ALA LEU          
SEQRES  27 B  734  ALA SER LEU GLY VAL ILE THR SER LEU VAL ALA GLN HIS          
SEQRES  28 B  734  MET TYR SER LEU PRO ALA TYR ALA PHE ILE ALA GLN ASP          
SEQRES  29 B  734  PHE THR THR GLN ALA ALA LEU TYR THR HIS HIS GLN TYR          
SEQRES  30 B  734  ILE ALA GLY PHE ILE MET THR GLY ALA PHE ALA HIS GLY          
SEQRES  31 B  734  ALA ILE PHE PHE ILE ARG ASP TYR ASN PRO GLU GLN ASN          
SEQRES  32 B  734  ALA ASP ASN VAL LEU ALA ARG MET LEU GLU HIS LYS GLU          
SEQRES  33 B  734  ALA ILE ILE SER HIS LEU SER TRP ALA SER LEU PHE LEU          
SEQRES  34 B  734  GLY PHE HIS THR LEU GLY LEU TYR VAL HIS ASN ASP VAL          
SEQRES  35 B  734  MET LEU ALA PHE GLY THR PRO GLU LYS GLN ILE LEU ILE          
SEQRES  36 B  734  GLU PRO ILE PHE ALA GLN TRP ILE GLN SER ALA HIS GLY          
SEQRES  37 B  734  LYS THR SER TYR GLY PHE ASP VAL LEU LEU SER SER THR          
SEQRES  38 B  734  ASN SER PRO ALA LEU ASN ALA GLY ARG SER ILE TRP LEU          
SEQRES  39 B  734  PRO GLY TRP LEU ASN ALA ILE ASN GLU ASN SER ASN SER          
SEQRES  40 B  734  LEU PHE LEU THR ILE GLY PRO GLY ASP PHE LEU VAL HIS          
SEQRES  41 B  734  HIS ALA ILE ALA LEU GLY LEU HIS THR THR THR LEU ILE          
SEQRES  42 B  734  LEU VAL LYS GLY ALA LEU ASP ALA ARG GLY SER LYS LEU          
SEQRES  43 B  734  MET PRO ASP LYS LYS ASP PHE GLY TYR SER PHE PRO CYS          
SEQRES  44 B  734  ASP GLY PRO GLY ARG GLY GLY THR CYS ASP ILE SER ALA          
SEQRES  45 B  734  TRP ASP ALA PHE TYR LEU ALA VAL PHE TRP MET LEU ASN          
SEQRES  46 B  734  THR ILE GLY TRP VAL THR PHE TYR TRP HIS TRP LYS HIS          
SEQRES  47 B  734  ILE THR LEU TRP GLN GLY ASN VAL SER GLN PHE ASN GLU          
SEQRES  48 B  734  SER SER THR TYR LEU MET GLY TRP LEU ARG ASP TYR LEU          
SEQRES  49 B  734  TRP LEU ASN SER SER GLN LEU ILE ASN GLY TYR ASN PRO          
SEQRES  50 B  734  PHE GLY MET ASN SER LEU SER VAL TRP ALA TRP MET PHE          
SEQRES  51 B  734  LEU PHE GLY HIS LEU VAL TRP ALA THR GLY PHE MET PHE          
SEQRES  52 B  734  LEU ILE SER TRP ARG GLY TYR TRP GLN GLU LEU ILE GLU          
SEQRES  53 B  734  THR LEU ALA TRP ALA HIS GLU ARG THR PRO LEU ALA ASN          
SEQRES  54 B  734  LEU ILE ARG TRP ARG ASP LYS PRO VAL ALA LEU SER ILE          
SEQRES  55 B  734  VAL GLN ALA ARG LEU VAL GLY LEU VAL HIS PHE SER VAL          
SEQRES  56 B  734  GLY TYR ILE PHE THR TYR ALA ALA PHE LEU ILE ALA SER          
SEQRES  57 B  734  THR SER GLY LYS PHE GLY                                      
SEQRES   1 C   81  MET SER HIS SER VAL LYS ILE TYR ASP THR CYS ILE GLY          
SEQRES   2 C   81  CYS THR GLN CYS VAL ARG ALA CYS PRO THR ASP VAL LEU          
SEQRES   3 C   81  GLU MET ILE PRO TRP GLY GLY CYS LYS ALA LYS GLN ILE          
SEQRES   4 C   81  ALA SER ALA PRO ARG THR GLU ASP CYS VAL GLY CYS LYS          
SEQRES   5 C   81  ARG CYS GLU SER ALA CYS PRO THR ASP PHE LEU SER VAL          
SEQRES   6 C   81  ARG VAL TYR LEU TRP HIS GLU THR THR ARG SER MET GLY          
SEQRES   7 C   81  LEU ALA TYR                                                  
SEQRES   1 D  143  GLY PHE THR PRO PRO GLU LEU ASP PRO ASN THR PRO SER          
SEQRES   2 D  143  PRO ILE PHE GLY GLY SER THR GLY GLY LEU LEU ARG LYS          
SEQRES   3 D  143  ALA GLN VAL GLU GLU PHE TYR VAL ILE THR TRP GLU SER          
SEQRES   4 D  143  PRO LYS GLU GLN ILE PHE GLU MET PRO THR GLY GLY ALA          
SEQRES   5 D  143  ALA ILE MET ARG GLU GLY PRO ASN LEU LEU LYS LEU ALA          
SEQRES   6 D  143  ARG LYS GLU GLN CYS LEU ALA LEU GLY THR ARG LEU ARG          
SEQRES   7 D  143  SER LYS TYR LYS ILE LYS TYR GLN PHE TYR ARG VAL PHE          
SEQRES   8 D  143  PRO SER GLY GLU VAL GLN TYR LEU HIS PRO LYS ASP GLY          
SEQRES   9 D  143  VAL TYR PRO GLU LYS VAL ASN PRO GLY ARG GLN GLY VAL          
SEQRES  10 D  143  GLY VAL ASN PHE ARG SER ILE GLY LYS ASN VAL SER PRO          
SEQRES  11 D  143  ILE GLU VAL LYS PHE THR GLY LYS GLN PRO TYR ASP LEU          
SEQRES   1 E   66  PRO PRO ILE GLY PRO LYS ARG GLY ALA LYS VAL LYS ILE          
SEQRES   2 E   66  LEU ARG GLN GLU SER TYR TRP TYR LYS GLY THR GLY SER          
SEQRES   3 E   66  VAL VAL ALA VAL ASP GLN ASP PRO ASN THR ARG TYR PRO          
SEQRES   4 E   66  VAL VAL VAL ARG PHE ASN LYS VAL ASN TYR ALA ASN VAL          
SEQRES   5 E   66  SER THR ASN ASN TYR ALA LEU ASP GLU VAL GLU GLU VAL          
SEQRES   6 E   66  LYS                                                          
SEQRES   1 F  154  ASP ILE ALA GLY LEU THR PRO CYS LYS ASP SER LYS GLN          
SEQRES   2 F  154  PHE ALA LYS ARG GLU LYS GLN SER ILE LYS LYS LEU GLU          
SEQRES   3 F  154  SER SER LEU LYS LEU TYR ALA PRO ASP SER ALA PRO ALA          
SEQRES   4 F  154  LEU ALA ILE ASN ALA THR ILE GLU LYS THR LYS ARG ARG          
SEQRES   5 F  154  PHE ASP ASN TYR GLY LYS GLN GLY LEU LEU CYS GLY ALA          
SEQRES   6 F  154  ASP GLY LEU PRO HIS LEU ILE VAL SER GLY ASP GLN ARG          
SEQRES   7 F  154  HIS TRP GLY GLU PHE ILE THR PRO GLY ILE LEU PHE LEU          
SEQRES   8 F  154  TYR ILE ALA GLY TRP ILE GLY TRP VAL GLY ARG SER TYR          
SEQRES   9 F  154  LEU ILE ALA ILE ARG ASP ASP LYS LYS PRO THR GLN LYS          
SEQRES  10 F  154  GLU ILE ILE ILE ASP VAL PRO LEU ALA THR ARG LEU VAL          
SEQRES  11 F  154  PHE ARG GLY PHE SER TRP PRO ILE ALA ALA TYR ARG GLU          
SEQRES  12 F  154  LEU LEU ASN GLY GLU LEU VAL ALA LYS ASP VAL                  
SEQRES   1 G   97  LEU ASN PRO SER LEU VAL ILE SER LEU SER THR GLY LEU          
SEQRES   2 G   97  SER LEU PHE LEU GLY ARG PHE VAL PHE PHE ASN PHE GLN          
SEQRES   3 G   97  ARG GLU ASN VAL ALA LYS GLN GLY LEU PRO GLU GLN ASN          
SEQRES   4 G   97  GLY VAL THR HIS PHE GLU ALA GLY ASP THR ARG ALA LYS          
SEQRES   5 G   97  GLU TYR VAL SER LEU LEU LYS SER ASN ASP PRO VAL GLY          
SEQRES   6 G   97  PHE ASN ILE VAL ASP VAL LEU ALA TRP GLY SER ILE GLY          
SEQRES   7 G   97  HIS ILE VAL ALA TYR TYR ILE LEU ALA THR SER SER ASN          
SEQRES   8 G   97  GLY TYR ASP PRO LYS PHE                                      
SEQRES   1 H   88  VAL TYR PHE ASP LEU GLU ASP LEU GLY ASN THR THR GLY          
SEQRES   2 H   88  GLN TRP ASP LEU TYR GLY SER ASP ALA PRO SER PRO TYR          
SEQRES   3 H   88  ASN SER LEU GLN SER LYS PHE PHE GLU THR PHE ALA ALA          
SEQRES   4 H   88  PRO PHE THR LYS ARG GLY LEU LEU LEU LYS PHE LEU ILE          
SEQRES   5 H   88  LEU GLY GLY GLY SER THR LEU ALA TYR PHE SER ALA THR          
SEQRES   6 H   88  ALA SER GLY ASP ILE LEU PRO ILE LYS LYS GLY PRO GLN          
SEQRES   7 H   88  LEU PRO PRO GLN LEU GLY PRO ARG LEU GLY                      
SEQRES   1 I   40  MET ILE ASN LEU PRO SER LEU PHE VAL PRO LEU VAL GLY          
SEQRES   2 I   40  LEU LEU PHE PRO ALA VAL ALA MET ALA SER LEU PHE LEU          
SEQRES   3 I   40  HIS VAL GLU LYS ARG LEU LEU PHE SER THR LYS LYS ILE          
SEQRES   4 I   40  ASN                                                          
SEQRES   1 J   42  MET ARG ASP LEU LYS THR TYR LEU SER VAL ALA PRO VAL          
SEQRES   2 J   42  ALA SER THR LEU TRP PHE ALA ALA LEU ALA GLY LEU LEU          
SEQRES   3 J   42  ILE GLU ILE ASN ARG PHE PHE PRO ASP ALA LEU THR PHE          
SEQRES   4 J   42  PRO PHE PHE                                                  
SEQRES   1 K   80  ILE GLY SER PRO THR ASN LEU ILE MET VAL THR SER THR          
SEQRES   2 K   80  SER LEU MET LEU PHE ALA GLY ARG PHE GLY LEU ALA PRO          
SEQRES   3 K   80  SER ALA ASN ARG LYS ALA THR ALA GLY LEU LYS LEU GLU          
SEQRES   4 K   80  ALA ARG ASP SER GLY LEU GLN THR GLY ASP PRO ALA GLY          
SEQRES   5 K   80  PHE THR LEU ALA ASP THR LEU ALA CYS GLY VAL VAL GLY          
SEQRES   6 K   80  HIS ILE ILE GLY VAL GLY VAL VAL LEU GLY LEU LYS ASN          
SEQRES   7 K   80  ILE GLY                                                      
SEQRES   1 L  157  TYR GLN VAL VAL GLN PRO ILE ASN GLY ASP PRO PHE ILE          
SEQRES   2 L  157  GLY SER LEU GLU THR PRO VAL THR SER SER PRO LEU VAL          
SEQRES   3 L  157  ALA TRP TYR LEU SER ASN LEU PRO GLY TYR ARG THR ALA          
SEQRES   4 L  157  VAL ASN PRO LEU LEU ARG GLY ILE GLU VAL GLY LEU ALA          
SEQRES   5 L  157  HIS GLY PHE LEU LEU VAL GLY PRO PHE VAL LYS ALA GLY          
SEQRES   6 L  157  PRO LEU ARG ASN THR GLU ILE ALA GLY GLN ALA GLY SER          
SEQRES   7 L  157  LEU ALA ALA GLY GLY LEU VAL VAL ILE LEU SER ILE CYS          
SEQRES   8 L  157  LEU THR ILE TYR GLY ILE SER SER PHE ASN GLU GLY ASP          
SEQRES   9 L  157  PRO SER THR ALA PRO SER LEU THR LEU THR GLY ARG LYS          
SEQRES  10 L  157  LYS GLN PRO ASP GLN LEU GLN THR ALA ASP GLY TRP ALA          
SEQRES  11 L  157  LYS PHE THR GLY GLY PHE PHE PHE GLY GLY ILE SER GLY          
SEQRES  12 L  157  VAL ILE TRP ALA PHE PHE LEU LEU TYR VAL LEU ASP LEU          
SEQRES  13 L  157  PRO                                                          
HET    LUT  1 501      42                                                       
HET    LUT  1 502      42                                                       
HET    BCR  1 503      19                                                       
HET    CLA  1 504      65                                                       
HET    CLA  1 505      46                                                       
HET    CLA  1 506      55                                                       
HET    CLA  1 507      65                                                       
HET    CLA  1 508      65                                                       
HET    CLA  1 509      50                                                       
HET    CLA  1 510      46                                                       
HET    CLA  1 511      46                                                       
HET    CHL  1 512      47                                                       
HET    CLA  1 513      65                                                       
HET    CHL  1 514      61                                                       
HET    CLA  1 515      45                                                       
HET    CLA  1 516      60                                                       
HET    LHG  1 517      49                                                       
HET    LMG  1 518      46                                                       
HET    LMG  1 519      13                                                       
HET    LHG  1 520      42                                                       
HET    CHL  1 521      56                                                       
HET    LUT  2 501      42                                                       
HET    XAT  2 502      44                                                       
HET    BCR  2 503      40                                                       
HET    CLA  2 504      60                                                       
HET    CLA  2 505      52                                                       
HET    CLA  2 506      65                                                       
HET    CLA  2 507      65                                                       
HET    CLA  2 508      55                                                       
HET    CLA  2 509      50                                                       
HET    CLA  2 510      60                                                       
HET    CLA  2 511      50                                                       
HET    CHL  2 512      47                                                       
HET    CHL  2 513      48                                                       
HET    CLA  2 514      55                                                       
HET    CHL  2 515      46                                                       
HET    CHL  2 516      56                                                       
HET    LHG  2 517      35                                                       
HET    LMG  2 518      25                                                       
HET    LMG  2 519      36                                                       
HET    LMG  2 520      13                                                       
HET    LMG  2 521      13                                                       
HET    LMG  2 522      13                                                       
HET    LMT  2 523      35                                                       
HET    LMG  2 524      13                                                       
HET    LMG  2 525      13                                                       
HET    CHL  2 526      66                                                       
HET    LUT  3 301      42                                                       
HET    LUT  3 302      42                                                       
HET    BCR  3 303      40                                                       
HET    BCR  3 304      40                                                       
HET    CLA  3 305      55                                                       
HET    CLA  3 306      52                                                       
HET    CLA  3 307      55                                                       
HET    CLA  3 308      65                                                       
HET    CLA  3 309      55                                                       
HET    CLA  3 310      50                                                       
HET    CLA  3 311      41                                                       
HET    CLA  3 312      48                                                       
HET    CLA  3 313      60                                                       
HET    CHL  3 314      47                                                       
HET    CLA  3 315      50                                                       
HET    CLA  3 316      46                                                       
HET    CLA  3 317      46                                                       
HET    LMT  3 318      31                                                       
HET     CA  3 319       1                                                       
HET    BCR  4 301      40                                                       
HET    LUT  4 302      42                                                       
HET    XAT  4 303      44                                                       
HET    CLA  4 304      60                                                       
HET    CLA  4 305      50                                                       
HET    CLA  4 306      65                                                       
HET    CLA  4 307      60                                                       
HET    CLA  4 308      60                                                       
HET    CLA  4 309      50                                                       
HET    CLA  4 310      60                                                       
HET    CLA  4 311      46                                                       
HET    CLA  4 312      50                                                       
HET    CHL  4 313      47                                                       
HET    CHL  4 314      51                                                       
HET    CLA  4 315      65                                                       
HET    CHL  4 316      61                                                       
HET    CHL  4 317      43                                                       
HET    CLA  4 318      65                                                       
HET    DGD  4 319      51                                                       
HET    LMT  4 320      35                                                       
HET    LMG  4 321      13                                                       
HET    LMG  4 322      45                                                       
HET    CL0  A 801      65                                                       
HET    CLA  A 802      65                                                       
HET    CLA  A 803      65                                                       
HET    CLA  A 804      65                                                       
HET    CLA  A 805      65                                                       
HET    CLA  A 806      65                                                       
HET    CLA  A 807      60                                                       
HET    CLA  A 808      65                                                       
HET    CLA  A 809      65                                                       
HET    CLA  A 810      50                                                       
HET    CLA  A 811      65                                                       
HET    CLA  A 812      55                                                       
HET    CLA  A 813      65                                                       
HET    CLA  A 814      65                                                       
HET    CLA  A 815      45                                                       
HET    CLA  A 816      46                                                       
HET    CLA  A 817      65                                                       
HET    CLA  A 818      56                                                       
HET    CLA  A 819      65                                                       
HET    CLA  A 820      50                                                       
HET    CLA  A 821      65                                                       
HET    CLA  A 822      60                                                       
HET    CLA  A 823      60                                                       
HET    CLA  A 824      65                                                       
HET    CLA  A 825      65                                                       
HET    CLA  A 826      55                                                       
HET    CLA  A 827      65                                                       
HET    CLA  A 828      65                                                       
HET    CLA  A 829      65                                                       
HET    CLA  A 830      65                                                       
HET    CLA  A 831      65                                                       
HET    CLA  A 832      65                                                       
HET    CLA  A 833      65                                                       
HET    CLA  A 834      65                                                       
HET    CLA  A 835      55                                                       
HET    CLA  A 836      51                                                       
HET    CLA  A 837      65                                                       
HET    CLA  A 838      65                                                       
HET    CLA  A 839      65                                                       
HET    CLA  A 840      65                                                       
HET    CLA  A 841      65                                                       
HET    CLA  A 842      60                                                       
HET    SF4  A 843       8                                                       
HET    PQN  A 844      33                                                       
HET    LHG  A 845      40                                                       
HET    LMT  A 846      35                                                       
HET    LMG  A 847      50                                                       
HET    BCR  A 848      40                                                       
HET    BCR  A 849      40                                                       
HET    BCR  A 850      40                                                       
HET    BCR  A 851      40                                                       
HET    BCR  A 852      40                                                       
HET    LHG  A 853      49                                                       
HET    CLA  A 854      65                                                       
HET    CLA  A 855      65                                                       
HET    BCR  A 856      40                                                       
HET    DGD  B 801      41                                                       
HET    BCR  B 802      40                                                       
HET    CLA  B 803      65                                                       
HET    CLA  B 804      65                                                       
HET    CLA  B 805      65                                                       
HET    CLA  B 806      65                                                       
HET    CLA  B 807      65                                                       
HET    CLA  B 808      65                                                       
HET    CLA  B 809      65                                                       
HET    CLA  B 810      65                                                       
HET    CLA  B 811      65                                                       
HET    CLA  B 812      60                                                       
HET    CLA  B 813      46                                                       
HET    CLA  B 814      65                                                       
HET    CLA  B 815      65                                                       
HET    CLA  B 816      55                                                       
HET    CLA  B 817      60                                                       
HET    CLA  B 818      65                                                       
HET    CLA  B 819      65                                                       
HET    CLA  B 820      65                                                       
HET    CLA  B 821      46                                                       
HET    CLA  B 822      65                                                       
HET    CLA  B 823      55                                                       
HET    CLA  B 824      65                                                       
HET    CLA  B 825      65                                                       
HET    CLA  B 826      65                                                       
HET    CLA  B 827      65                                                       
HET    CLA  B 828      65                                                       
HET    CLA  B 829      65                                                       
HET    CLA  B 830      65                                                       
HET    CLA  B 831      60                                                       
HET    CLA  B 832      58                                                       
HET    CLA  B 833      60                                                       
HET    CLA  B 834      55                                                       
HET    CLA  B 835      55                                                       
HET    CLA  B 836      65                                                       
HET    CLA  B 837      50                                                       
HET    CLA  B 838      65                                                       
HET    CLA  B 839      65                                                       
HET    CLA  B 840      65                                                       
HET    PQN  B 841      33                                                       
HET    LHG  B 842      21                                                       
HET    LHG  B 843      49                                                       
HET    LMG  B 844      35                                                       
HET    LMG  B 845      33                                                       
HET    LMT  B 846      35                                                       
HET    LMT  B 847      32                                                       
HET     CA  B 848       1                                                       
HET    BCR  B 849      40                                                       
HET    BCR  B 850      40                                                       
HET    BCR  B 851      40                                                       
HET    BCR  B 852      40                                                       
HET    BCR  B 853      40                                                       
HET    DGD  B 854      61                                                       
HET    LMT  B 855      31                                                       
HET    BCR  B 856      40                                                       
HET    SF4  C 101       8                                                       
HET    SF4  C 102       8                                                       
HET    ZEX  F 301      42                                                       
HET    CLA  F 302      65                                                       
HET    CLA  F 303      65                                                       
HET    LMG  F 304      47                                                       
HET    LMG  F 305      36                                                       
HET    BCR  F 306      40                                                       
HET    CLA  G 201      65                                                       
HET    CLA  G 202      55                                                       
HET    CLA  G 203      46                                                       
HET    CLA  G 204      65                                                       
HET    BCR  G 205      40                                                       
HET    LMG  G 206      50                                                       
HET    DGD  G 207      47                                                       
HET    LMT  G 208      35                                                       
HET    LMT  G 209      31                                                       
HET    LMG  G 210      25                                                       
HET    CLA  H1000      60                                                       
HET    BCR  I 101      40                                                       
HET    BCR  I 102      40                                                       
HET    CLA  J1101      65                                                       
HET    CLA  J1102      45                                                       
HET    LMG  J1103      30                                                       
HET    LMG  J1104      34                                                       
HET    CLA  J1105      50                                                       
HET    DGD  J1106      58                                                       
HET    LMT  J1107      25                                                       
HET    BCR  J1108      40                                                       
HET    LUT  J1109      42                                                       
HET    CLA  K1001      45                                                       
HET    CLA  K1002      60                                                       
HET    CLA  K1003      27                                                       
HET    CLA  K1004      27                                                       
HET    BCR  K1005      40                                                       
HET    CLA  L 301      55                                                       
HET    BCR  L 302      40                                                       
HET    CLA  L 303      50                                                       
HET    CLA  L 304      60                                                       
HET    CLA  L 305      50                                                       
HET    BCR  L 306      40                                                       
HET    BCR  L 307      40                                                       
HETNAM     LUT (3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-                 
HETNAM   2 LUT  CAROTENE-3,3'-DIOL                                              
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     CHL CHLOROPHYLL B                                                    
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM     XAT (3S,5R,6S,3'S,5'R,6'S)-5,6,5',6'-DIEPOXY-5,6,5',6'-              
HETNAM   2 XAT  TETRAHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL                         
HETNAM     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     CL0 CHLOROPHYLL A ISOMER                                             
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     PQN PHYLLOQUINONE                                                    
HETNAM     ZEX (1R,2S)-4-{(1E,3E,5E,7E,9E,11E,13E,15E,17E)-18-[(4S)-4-          
HETNAM   2 ZEX  HYDROXY-2,6,6-TRIMETHYLCYCLOHEX-1-EN-1-YL]-3,7,12,16-           
HETNAM   3 ZEX  TETRAMETHYLOCTADECA-1,3,5,7,9,11,13,15,17-NONAEN-1-             
HETNAM   4 ZEX  YL}-2,5,5-TRIMETHYLCYCLOHEX-3-EN-1-OL                           
HETSYN     LUT (3R,3'R)-BETA,BETA-CAROTENE-3,3'-DIOL, LUTEIN                    
HETSYN     XAT VIOLAXANTHIN                                                     
HETSYN     PQN VITAMIN K1; 2-METHYL-3-PHYTYL-1,4-NAPHTHOQUINONE                 
FORMUL  17  LUT    7(C40 H56 O2)                                                
FORMUL  19  BCR    27(C40 H56)                                                  
FORMUL  20  CLA    142(C55 H72 MG N4 O5 2+)                                     
FORMUL  28  CHL    13(C55 H70 MG N4 O6 2+)                                      
FORMUL  33  LHG    7(C38 H75 O10 P)                                             
FORMUL  34  LMG    20(C45 H86 O10)                                              
FORMUL  39  XAT    2(C40 H56 O4)                                                
FORMUL  60  LMT    10(C24 H46 O11)                                              
FORMUL  82   CA    2(CA 2+)                                                     
FORMUL  01  DGD    5(C51 H96 O15)                                               
FORMUL  05  CL0    C55 H72 MG N4 O5 2+                                          
FORMUL  47  SF4    3(FE4 S4)                                                    
FORMUL  48  PQN    2(C31 H46 O2)                                                
FORMUL  19  ZEX    C40 H56 O2                                                   
FORMUL  59  HOH   *209(H2 O)                                                    
HELIX    1 AA1 VAL 1   69  LEU 1  100  1                                  32    
HELIX    2 AA2 VAL 1  106  ALA 1  113  5                                   8    
HELIX    3 AA3 THR 1  130  MET 1  151  1                                  22    
HELIX    4 AA4 PRO 1  155  TYR 1  160  1                                   6    
HELIX    5 AA5 GLY 1  162  ASP 1  166  5                                   5    
HELIX    6 AA6 ASP 1  173  TYR 1  205  1                                  33    
HELIX    7 AA7 GLY 1  209  ASP 1  220  1                                  12    
HELIX    8 AA8 THR 1  225  ILE 1  231  1                                   7    
HELIX    9 AA9 ASP 2   95  LEU 2  129  1                                  35    
HELIX   10 AB1 SER 2  136  ALA 2  140  5                                   5    
HELIX   11 AB2 ASP 2  148  ASN 2  173  1                                  26    
HELIX   12 AB3 GLY 2  197  ASP 2  202  1                                   6    
HELIX   13 AB4 GLN 2  212  THR 2  242  1                                  31    
HELIX   14 AB5 GLY 2  245  ASP 2  256  1                                  12    
HELIX   15 AB6 THR 2  261  ALA 2  265  5                                   5    
HELIX   16 AB7 GLN 3   63  LEU 3   68  1                                   6    
HELIX   17 AB8 GLU 3   94  VAL 3  125  1                                  32    
HELIX   18 AB9 ASN 3  154  LYS 3  178  1                                  25    
HELIX   19 AC1 GLY 3  180  LYS 3  184  5                                   5    
HELIX   20 AC2 GLU 3  191  GLY 3  195  5                                   5    
HELIX   21 AC3 GLY 3  204  ASN 3  209  1                                   6    
HELIX   22 AC4 ASP 3  216  THR 3  248  1                                  33    
HELIX   23 AC5 GLY 3  251  HIS 3  259  1                                   9    
HELIX   24 AC6 ASN 3  266  SER 3  271  1                                   6    
HELIX   25 AC7 ASP 4   84  GLY 4  119  1                                  36    
HELIX   26 AC8 SER 4  137  ASN 4  162  1                                  26    
HELIX   27 AC9 GLY 4  186  ASN 4  190  5                                   5    
HELIX   28 AD1 GLU 4  199  GLY 4  226  1                                  28    
HELIX   29 AD2 GLY 4  228  ASP 4  239  1                                  12    
HELIX   30 AD3 THR 4  244  LEU 4  249  1                                   6    
HELIX   31 AD4 THR A   43  GLY A   47  5                                   5    
HELIX   32 AD5 THR A   51  ASP A   60  1                                  10    
HELIX   33 AD6 ASP A   63  THR A   68  1                                   6    
HELIX   34 AD7 ASP A   70  PHE A  103  1                                  34    
HELIX   35 AD8 ASN A  105  ASP A  112  1                                   8    
HELIX   36 AD9 GLY A  128  ASN A  133  5                                   6    
HELIX   37 AE1 GLY A  148  SER A  156  1                                   9    
HELIX   38 AE2 SER A  160  LYS A  188  1                                  29    
HELIX   39 AE3 LYS A  192  ASP A  198  1                                   7    
HELIX   40 AE4 ASP A  198  ALA A  208  1                                  11    
HELIX   41 AE5 GLY A  209  VAL A  225  1                                  17    
HELIX   42 AE6 VAL A  225  ALA A  235  1                                  11    
HELIX   43 AE7 HIS A  246  ASN A  251  1                                   6    
HELIX   44 AE8 ASN A  251  TYR A  259  1                                   9    
HELIX   45 AE9 PRO A  260  GLU A  264  5                                   5    
HELIX   46 AF1 ALA A  266  THR A  271  1                                   6    
HELIX   47 AF2 ASN A  273  PHE A  280  5                                   8    
HELIX   48 AF3 TRP A  295  GLY A  314  1                                  20    
HELIX   49 AF4 GLY A  326  HIS A  334  1                                   9    
HELIX   50 AF5 GLY A  345  THR A  351  1                                   7    
HELIX   51 AF6 SER A  353  MET A  379  1                                  27    
HELIX   52 AF7 ASP A  388  ASP A  421  1                                  34    
HELIX   53 AF8 ASN A  429  HIS A  438  1                                  10    
HELIX   54 AF9 HIS A  438  LEU A  470  1                                  33    
HELIX   55 AG1 ARG A  472  MET A  476  5                                   5    
HELIX   56 AG2 PRO A  486  ALA A  499  1                                  14    
HELIX   57 AG3 GLY A  535  PHE A  562  1                                  28    
HELIX   58 AG4 ASP A  571  GLY A  576  5                                   6    
HELIX   59 AG5 SER A  593  VAL A  624  1                                  32    
HELIX   60 AG6 ASN A  641  SER A  646  1                                   6    
HELIX   61 AG7 THR A  648  PHE A  656  1                                   9    
HELIX   62 AG8 PHE A  656  ALA A  661  1                                   6    
HELIX   63 AG9 ALA A  661  GLN A  666  1                                   6    
HELIX   64 AH1 LEU A  672  SER A  695  1                                  24    
HELIX   65 AH2 GLY A  696  LEU A  714  1                                  19    
HELIX   66 AH3 SER A  726  GLY A  758  1                                  33    
HELIX   67 AH4 SER B    9  GLN B   14  1                                   6    
HELIX   68 AH5 THR B   18  THR B   27  1                                  10    
HELIX   69 AH6 ASP B   30  HIS B   34  5                                   5    
HELIX   70 AH7 THR B   38  GLY B   72  1                                  35    
HELIX   71 AH8 ASN B   73  ASP B   80  1                                   8    
HELIX   72 AH9 GLY B   97  THR B  105  1                                   9    
HELIX   73 AI1 GLY B  119  GLY B  128  1                                  10    
HELIX   74 AI2 THR B  131  HIS B  156  1                                  26    
HELIX   75 AI3 SER B  164  LYS B  169  1                                   6    
HELIX   76 AI4 ASN B  170  GLY B  181  1                                  12    
HELIX   77 AI5 PHE B  183  VAL B  197  1                                  15    
HELIX   78 AI6 VAL B  197  ARG B  203  1                                   7    
HELIX   79 AI7 GLY B  223  GLY B  228  1                                   6    
HELIX   80 AI8 GLN B  229  GLN B  235  5                                   7    
HELIX   81 AI9 TRP B  269  GLY B  288  1                                  20    
HELIX   82 AJ1 SER B  300  HIS B  308  1                                   9    
HELIX   83 AJ2 PRO B  310  ARG B  314  5                                   5    
HELIX   84 AJ3 GLY B  321  ASN B  328  1                                   8    
HELIX   85 AJ4 SER B  329  LEU B  355  1                                  27    
HELIX   86 AJ5 ASP B  364  ASP B  397  1                                  34    
HELIX   87 AJ6 ASN B  406  HIS B  414  1                                   9    
HELIX   88 AJ7 HIS B  414  PHE B  446  1                                  33    
HELIX   89 AJ8 THR B  448  GLN B  452  5                                   5    
HELIX   90 AJ9 PRO B  457  HIS B  467  1                                  11    
HELIX   91 AK1 SER B  483  ARG B  490  1                                   8    
HELIX   92 AK2 TRP B  493  ASN B  502  1                                  10    
HELIX   93 AK3 GLY B  513  ASP B  540  1                                  28    
HELIX   94 AK4 ASP B  549  GLY B  554  5                                   6    
HELIX   95 AK5 PRO B  562  GLY B  566  5                                   5    
HELIX   96 AK6 SER B  571  GLN B  603  1                                  33    
HELIX   97 AK7 ASN B  605  SER B  613  1                                   9    
HELIX   98 AK8 TYR B  615  TYR B  623  1                                   9    
HELIX   99 AK9 TYR B  623  SER B  628  1                                   6    
HELIX  100 AL1 SER B  628  ASN B  633  1                                   6    
HELIX  101 AL2 LEU B  643  SER B  666  1                                  24    
HELIX  102 AL3 TRP B  667  ARG B  684  1                                  18    
HELIX  103 AL4 LEU B  687  ILE B  691  5                                   5    
HELIX  104 AL5 SER B  701  PHE B  733  1                                  33    
HELIX  105 AL6 THR C   15  CYS C   21  1                                   7    
HELIX  106 AL7 ARG C   44  CYS C   48  5                                   5    
HELIX  107 AL8 LYS C   52  CYS C   58  1                                   7    
HELIX  108 AL9 LEU D   92  GLU D   98  1                                   7    
HELIX  109 AM1 ARG D  134  LYS D  148  1                                  15    
HELIX  110 AM2 SER D  191  ASN D  195  5                                   5    
HELIX  111 AM3 SER D  197  LYS D  202  5                                   6    
HELIX  112 AM4 ALA E  121  ASP E  123  5                                   3    
HELIX  113 AM5 ASP F   78  LEU F   82  5                                   5    
HELIX  114 AM6 SER F   88  LYS F  107  1                                  20    
HELIX  115 AM7 SER F  113  GLN F  136  1                                  24    
HELIX  116 AM8 ASP F  153  GLU F  159  5                                   7    
HELIX  117 AM9 PHE F  160  ARG F  186  1                                  27    
HELIX  118 AN1 LYS F  190  ILE F  197  1                                   8    
HELIX  119 AN2 ASP F  199  PHE F  208  1                                  10    
HELIX  120 AN3 ARG F  209  PHE F  211  5                                   3    
HELIX  121 AN4 SER F  212  GLY F  224  1                                  13    
HELIX  122 AN5 ASN G   59  VAL G   78  1                                  20    
HELIX  123 AN6 PHE G   79  GLY G   91  1                                  13    
HELIX  124 AN7 TYR G  111  LYS G  116  1                                   6    
HELIX  125 AN8 ASN G  124  SER G  147  1                                  24    
HELIX  126 AN9 ASP H   59  THR H   64  1                                   6    
HELIX  127 AO1 LEU H   81  ALA H   90  1                                  10    
HELIX  128 AO2 ALA H   91  THR H   94  5                                   4    
HELIX  129 AO3 LYS H   95  THR H  117  1                                  23    
HELIX  130 AO4 LEU H  123  GLY H  128  1                                   6    
HELIX  131 AO5 LEU I    4  LEU I   14  1                                  11    
HELIX  132 AO6 LEU I   14  LYS I   30  1                                  17    
HELIX  133 AO7 ARG J    2  SER J    9  1                                   8    
HELIX  134 AO8 VAL J   10  PHE J   33  1                                  24    
HELIX  135 AO9 SER K   49  PHE K   68  1                                  20    
HELIX  136 AP1 THR K   99  ASN K  123  1                                  25    
HELIX  137 AP2 ASN L   61  ASP L   63  5                                   3    
HELIX  138 AP3 SER L   76  ASN L   85  1                                  10    
HELIX  139 AP4 LEU L   86  ARG L   90  5                                   5    
HELIX  140 AP5 ASN L   94  GLY L  118  1                                  25    
HELIX  141 AP6 THR L  123  GLN L  128  1                                   6    
HELIX  142 AP7 GLY L  130  PHE L  153  1                                  24    
HELIX  143 AP8 ASP L  174  GLN L  177  5                                   4    
HELIX  144 AP9 THR L  178  LEU L  203  1                                  26    
SHEET    1 AA1 2 THR 1 120  TYR 1 121  0                                        
SHEET    2 AA1 2 ASN 1 124  PRO 1 125 -1  O  ASN 1 124   N  TYR 1 121           
SHEET    1 AA2 2 VAL A  22  ARG A  24  0                                        
SHEET    2 AA2 2 ALA A 189  PRO A 191 -1  O  ALA A 190   N  ASP A  23           
SHEET    1 AA3 3 SER A 119  GLN A 121  0                                        
SHEET    2 AA3 3 ARG A 141  GLN A 144 -1  O  ILE A 143   N  GLN A 121           
SHEET    3 AA3 3 GLY A 134  ASP A 135 -1  N  GLY A 134   O  GLY A 142           
SHEET    1 AA4 2 VAL A 521  VAL A 523  0                                        
SHEET    2 AA4 2 LYS A 526  LEU A 529 -1  O  ALA A 528   N  VAL A 521           
SHEET    1 AA5 2 GLY A 626  ILE A 628  0                                        
SHEET    2 AA5 2 VAL A 634  HIS A 636 -1  O  THR A 635   N  SER A 627           
SHEET    1 AA6 2 ILE B  87  ALA B  90  0                                        
SHEET    2 AA6 2 VAL B 113  ILE B 115 -1  O  ASN B 114   N  ALA B  88           
SHEET    1 AA7 2 TYR B 635  ASN B 636  0                                        
SHEET    2 AA7 2 GLY B 639  MET B 640 -1  O  GLY B 639   N  ASN B 636           
SHEET    1 AA8 3 VAL C  65  TYR C  68  0                                        
SHEET    2 AA8 3 SER C   4  TYR C   8 -1  N  SER C   4   O  TYR C  68           
SHEET    3 AA8 3 VAL D 187  ASN D 188  1  O  ASN D 188   N  ILE C   7           
SHEET    1 AA9 2 GLU C  27  PRO C  30  0                                        
SHEET    2 AA9 2 GLN C  38  SER C  41 -1  O  ILE C  39   N  ILE C  29           
SHEET    1 AB1 4 GLY D 126  LEU D 132  0                                        
SHEET    2 AB1 4 PHE D 100  SER D 107 -1  N  ILE D 103   O  LEU D 130           
SHEET    3 AB1 4 TYR D 153  VAL D 158 -1  O  VAL D 158   N  PHE D 100           
SHEET    4 AB1 4 VAL D 164  HIS D 168 -1  O  GLN D 165   N  ARG D 157           
SHEET    1 AB2 2 GLN D 111  GLU D 114  0                                        
SHEET    2 AB2 2 ALA D 120  MET D 123 -1  O  ALA D 121   N  PHE D 113           
SHEET    1 AB3 5 THR E 117  TYR E 120  0                                        
SHEET    2 AB3 5 VAL E 103  ARG E 106 -1  N  VAL E 105   O  ASN E 118           
SHEET    3 AB3 5 THR E  87  VAL E  93 -1  N  VAL E  91   O  VAL E 104           
SHEET    4 AB3 5 LYS E  73  ILE E  76 -1  N  VAL E  74   O  GLY E  88           
SHEET    5 AB3 5 VAL E 125  GLU E 127 -1  O  GLU E 126   N  LYS E  75           
SHEET    1 AB4 3 THR F  83  PRO F  84  0                                        
SHEET    2 AB4 3 LEU F 139  CYS F 140 -1  O  CYS F 140   N  THR F  83           
SHEET    3 AB4 3 PRO F 146  HIS F 147 -1  O  HIS F 147   N  LEU F 139           
SHEET    1 AB5 2 GLU G  94  GLN G  95  0                                        
SHEET    2 AB5 2 VAL G  98  THR G  99 -1  O  VAL G  98   N  GLN G  95           
SHEET    1 AB6 2 ARG K  76  LYS K  77  0                                        
SHEET    2 AB6 2 GLU K  84  ALA K  85 -1  O  GLU K  84   N  LYS K  77           
SHEET    1 AB7 2 GLN L  58  PRO L  59  0                                        
SHEET    2 AB7 2 LEU L  69  GLU L  70 -1  O  GLU L  70   N  GLN L  58           
SSBOND   1 CYS F   85    CYS F  140                          1555   1555  2.04  
LINK         O   TRP 1  41                MG   CHL 1 521     1555   1555  2.79  
LINK         OE2 GLU 1  80                MG   CLA 1 507     1555   1555  2.88  
LINK         OE2 GLU 1 146                MG   CHL 1 514     1555   1555  2.99  
LINK         OE2 GLU 1 184                MG   CLA 1 504     1555   1555  2.89  
LINK         OD1 ASN 1 187                MG   CLA 1 505     1555   1555  2.83  
LINK         O   LEU 1 230                MG   CLA 1 516     1555   1555  2.72  
LINK         O   TRP 2  67                MG   CHL 2 526     1555   1555  2.69  
LINK         OE2 GLU 2 106                MG   CLA 2 507     1555   1555  2.92  
LINK         OE1 GLU 2 164                MG   CLA 2 514     1555   1555  2.93  
LINK         OD2 ASP 2 180                MG   CHL 2 516     1555   1555  2.92  
LINK         OE2 GLU 2 221                MG   CLA 2 504     1555   1555  2.96  
LINK         OD1 ASN 2 224                MG   CLA 2 505     1555   1555  2.91  
LINK         O   ASP 3  85                CA    CA 3 319     1555   1555  3.04  
LINK         O   GLY 3  88                CA    CA 3 319     1555   1555  2.43  
LINK         O   VAL 3 141                MG   CLA 3 313     1555   1555  2.95  
LINK         OE1 GLU 3 169                MG   CLA 3 315     1555   1555  2.98  
LINK         O   TRP 4  56                MG   CLA 4 312     1555   1555  2.57  
LINK         OE2 GLU 4  95                MG   CLA 4 307     1555   1555  2.91  
LINK         OD1 ASN 4  98                MG   CLA 4 308     1555   1555  2.79  
LINK         OE1 GLU 4 153                MG   CLA 4 315     1555   1555  2.82  
LINK         OD2 ASP 4 169                MG   CHL 4 317     1555   1555  2.99  
LINK         OE2 GLU 4 204                MG   CLA 4 304     1555   1555  2.96  
LINK         OD1 ASN 4 207                MG   CLA 4 305     1555   1555  2.84  
LINK         O   ILE A  20                CA    CA 3 319     1555   1555  2.78  
LINK         OE1 GLN A  85                MG   CLA A 806     1555   1555  2.77  
LINK         OE1 GLN A 121                MG   CLA A 808     1555   1555  2.67  
LINK         OE1 GLN A 129                MG   CLA A 809     1555   1555  2.75  
LINK         O   THR A 503                MG   CLA A 835     1555   1555  2.75  
LINK         SG  CYS A 581                FE1  SF4 A 843     1555   1555  2.56  
LINK         SG  CYS A 590                FE4  SF4 A 843     1555   1555  2.70  
LINK         OE1 GLN B  53                MG   CLA B 807     1555   1555  2.76  
LINK         OD2 ASP B  93                MG   CLA B 810     1555   1555  2.85  
LINK         O   ILE B 501                CA    CA B 848     1555   1555  2.82  
LINK         O   GLU B 503                CA    CA B 848     1555   1555  2.43  
LINK         OD1 ASN B 506                CA    CA B 848     1555   1555  2.54  
LINK         O   LEU B 508                CA    CA B 848     1555   1555  2.93  
LINK         SG  CYS B 559                FE2  SF4 A 843     1555   1555  2.40  
LINK         SG  CYS B 568                FE3  SF4 A 843     1555   1555  2.68  
LINK         SG  CYS C  11                FE2  SF4 C 102     1555   1555  2.61  
LINK         SG  CYS C  14                FE1  SF4 C 102     1555   1555  2.57  
LINK         SG  CYS C  17                FE4  SF4 C 102     1555   1555  2.20  
LINK         SG  CYS C  21                FE1  SF4 C 101     1555   1555  2.66  
LINK         SG  CYS C  48                FE4  SF4 C 101     1555   1555  2.61  
LINK         SG  CYS C  51                FE3  SF4 C 101     1555   1555  2.62  
LINK         SG  CYS C  54                FE2  SF4 C 101     1555   1555  2.50  
LINK         O   SER F 151                MG   CLA F 303     1555   1555  2.78  
LINK         OD2 ASP G 119                MG   CLA G 203     1555   1555  2.93  
LINK         OE2 GLU L 101                MG   CLA L 303     1555   1555  2.76  
LINK        MG   CLA 2 510                 O5  LHG 2 517     1555   1555  2.88  
LINK        MG   CLA 3 310                 O   HOH 3 402     1555   1555  2.99  
LINK        MG   CHL 4 314                 O   HOH 4 408     1555   1555  2.91  
LINK        MG   CLA A 803                 O   HOH A 910     1555   1555  2.72  
LINK        MG   CLA A 825                 O   HOH A 905     1555   1555  2.82  
LINK        MG   CLA A 826                 O   HOH A 924     1555   1555  2.82  
LINK        MG   CLA A 840                 O   HOH A 919     1555   1555  2.67  
LINK        MG   CLA A 842                 O5  LHG A 845     1555   1555  2.77  
LINK        MG   CLA A 854                 O   HOH B 904     1555   1555  2.73  
LINK        MG   CLA B 820                 O   HOH B 914     1555   1555  2.84  
LINK        MG   CLA B 824                 O   HOH B 957     1555   1555  2.85  
LINK        MG   CLA B 825                 O   HOH B 953     1555   1555  2.77  
LINK        MG   CLA B 834                 O   HOH B 903     1555   1555  2.82  
LINK        MG   CLA B 838                 O   HOH B 924     1555   1555  2.86  
LINK        MG   CLA B 840                 O5  LHG B 842     1555   1555  2.85  
LINK        MG   CLA G 204                 O   HOH G 301     1555   1555  2.83  
LINK        MG   CLA J1102                 O   HOH J1203     1555   1555  2.85  
LINK        MG   CLA L 305                 O   HOH L 401     1555   1555  2.95  
CISPEP   1 ASP 1  154    PRO 1  155          0         3.29                     
CISPEP   2 PHE B    5    PRO B    6          0        -0.50                     
CISPEP   3 ASP C   61    PHE C   62          0         3.66                     
CISPEP   4 HIS D  168    PRO D  169          0        -2.63                     
SITE     1 AC1 17 MET 1  88  VAL 1  91  PHE 1 165  ASP 1 166                    
SITE     2 AC1 17 PRO 1 167  LEU 1 168  TYR 1 170  ASN 1 187                    
SITE     3 AC1 17 LEU 1 190  ALA 1 194  ILE 1 198  GLN 1 201                    
SITE     4 AC1 17 PRO 1 210  CLA 1 504  CLA 1 505  CLA 1 506                    
SITE     5 AC1 17 CLA 1 513                                                     
SITE     1 AC2 14 ASP 1  62  PRO 1  63  LEU 1  64  ALA 1  90                    
SITE     2 AC2 14 ILE 1  94  TRP 1 105  GLN 1 109  LEU 1 192                    
SITE     3 AC2 14 VAL 1 196  CLA 1 507  CLA 1 508  CLA 1 509                    
SITE     4 AC2 14 CHL 1 512  CLA 1 515                                          
SITE     1 AC3  6 SER 1 141  ILE 1 142  VAL 1 145  CLA 1 509                    
SITE     2 AC3  6 CLA 1 513  CLA 1 515                                          
SITE     1 AC4 17 ARG 1  85  MET 1  88  LEU 1  89  TYR 1 160                    
SITE     2 AC4 17 PRO 1 161  GLY 1 162  PHE 1 165  TYR 1 170                    
SITE     3 AC4 17 PHE 1 177  TYR 1 180  LYS 1 181  LYS 1 183                    
SITE     4 AC4 17 GLU 1 184  ASN 1 187  LUT 1 501  CLA 1 505                    
SITE     5 AC4 17 CLA 1 513                                                     
SITE     1 AC5  7 TYR 1 180  LYS 1 183  ASN 1 187  LEU 1 190                    
SITE     2 AC5  7 LUT 1 501  CLA 1 504  CLA 1 510                               
SITE     1 AC6 16 LEU 1 193  ALA 1 194  GLY 1 197  VAL 1 200                    
SITE     2 AC6 16 GLN 1 201  ALA 1 204  TYR 1 205  ASN 1 213                    
SITE     3 AC6 16 LEU 1 214  HIS 1 217  THR 1 225  ILE 1 226                    
SITE     4 AC6 16 VAL 1 229  LUT 1 501  CLA 1 511  LHG 1 517                    
SITE     1 AC7 15 PRO 1  56  GLY 1  57  ASP 1  58  PHE 1  59                    
SITE     2 AC7 15 GLY 1  60  PHE 1  61  LEU 1  73  PHE 1  76                    
SITE     3 AC7 15 LYS 1  77  GLU 1  80  ARG 1 189  LUT 1 502                    
SITE     4 AC7 15 CLA 1 508  LHG 1 517  CHL 1 521                               
SITE     1 AC8 11 ARG 1  75  PHE 1  76  SER 1  79  HIS 1  83                    
SITE     2 AC8 11 LUT 1 502  CLA 1 507  CHL 1 514  LHG 1 520                    
SITE     3 AC8 11 CLA B 822  CLA B 840  BCR B 852                               
SITE     1 AC9 10 GLY 1  93  PRO 1  97  LEU 1 102  ALA 1 108                    
SITE     2 AC9 10 THR 1 120  TYR 1 121  LEU 1 122  LUT 1 502                    
SITE     3 AC9 10 BCR 1 503  CLA 1 515                                          
SITE     1 AD1  8 GLU 1 179  ILE 1 182  LYS 1 183  LYS 1 186                    
SITE     2 AD1  8 ASN 1 187  LEU 1 190  CLA 1 505  LHG 1 517                    
SITE     1 AD2  9 HIS 1 217  PRO 1 221  TRP 1 222  THR 1 225                    
SITE     2 AD2  9 CLA 1 506  THR 4 140  VAL 4 143  ILE 4 144                    
SITE     3 AD2  9 ILE 4 147                                                     
SITE     1 AD3 10 TRP 1 105  VAL 1 106  GLN 1 109  GLU 1 138                    
SITE     2 AD3 10 LUT 1 502  CLA 1 515  PHE G 154  CLA G 204                    
SITE     3 AD3 10 LMG G 206  LMG G 210                                          
SITE     1 AD4 12 ILE 1  82  ARG 1  85  TRP 1  86  VAL 1 145                    
SITE     2 AD4 12 GLN 1 148  ARG 1 149  GLU 1 152  PHE 1 165                    
SITE     3 AD4 12 PRO 1 167  LUT 1 501  BCR 1 503  CLA 1 504                    
SITE     1 AD5 14 ARG 1  75  GLU 1  78  SER 1  79  ILE 1  82                    
SITE     2 AD5 14 HIS 1  83  TRP 1  86  ILE 1 142  ALA 1 143                    
SITE     3 AD5 14 GLU 1 146  ARG 1 149  SER 1 150  CLA 1 508                    
SITE     4 AD5 14 LHG 1 520  CLA G 201                                          
SITE     1 AD6 14 ALA 1 108  GLN 1 109  TRP 1 111  ALA 1 119                    
SITE     2 AD6 14 TRP 1 128  ILE 1 134  ILE 1 137  GLU 1 138                    
SITE     3 AD6 14 SER 1 141  ILE 1 142  LUT 1 502  BCR 1 503                    
SITE     4 AD6 14 CLA 1 509  CHL 1 512                                          
SITE     1 AD7  8 SER 1 203  LEU 1 230  LHG 1 517  CLA 4 318                    
SITE     2 AD7  8 DGD B 801  LMG B 845  ZEX F 301  LMG F 304                    
SITE     1 AD8 13 PHE 1  59  LYS 1 186  LEU 1 190  LEU 1 230                    
SITE     2 AD8 13 CLA 1 506  CLA 1 507  CLA 1 510  CLA 1 516                    
SITE     3 AD8 13 CHL 1 521  PHE 4 146  ILE 4 147  BCR 4 301                    
SITE     4 AD8 13 CLA 4 318                                                     
SITE     1 AD9  7 GLN 1  45  PRO 1  46  ARG 1  65  LMG 1 519                    
SITE     2 AD9  7 CLA 4 318  LMG 4 321  ZEX F 301                               
SITE     1 AE1  4 LEU 1  64  ARG 1  65  LMG 1 518  ARG B 314                    
SITE     1 AE2  9 ARG 1  75  SER 1 150  CLA 1 508  CHL 1 514                    
SITE     2 AE2  9 ALA B 307  CLA B 822  CLA B 840  CLA G 201                    
SITE     3 AE2  9 CLA G 204                                                     
SITE     1 AE3 15 ASP 1  40  TRP 1  41  PRO 1  43  PHE 1  59                    
SITE     2 AE3 15 CLA 1 507  LHG 1 517  ILE 4 147  HIS 4 150                    
SITE     3 AE3 15 TYR 4 151  ILE 4 154  ARG 4 155  GLN 4 158                    
SITE     4 AE3 15 PRO 4 170  BCR 4 301  CLA 4 318                               
SITE     1 AE4 16 MET 2 114  ALA 2 117  PHE 2 121  PHE 2 201                    
SITE     2 AE4 16 ASP 2 202  PRO 2 203  LEU 2 204  ASN 2 224                    
SITE     3 AE4 16 ALA 2 231  GLN 2 238  PRO 2 246  CLA 2 504                    
SITE     4 AE4 16 CLA 2 505  CLA 2 506  CLA 2 511  CHL 2 513                    
SITE     1 AE5 16 PHE 2  87  ASP 2  88  PRO 2  89  LEU 2  90                    
SITE     2 AE5 16 LEU 2  92  HIS 2 109  TRP 2 112  ALA 2 113                    
SITE     3 AE5 16 GLY 2 116  ILE 2 120  TRP 2 137  MET 2 229                    
SITE     4 AE5 16 CLA 2 507  CLA 2 508  CLA 2 509  CHL 2 512                    
SITE     1 AE6 10 PHE 2 159  TRP 2 162  ILE 2 182  CLA 2 509                    
SITE     2 AE6 10 CHL 2 513  CHL 2 515  CHL 2 516  CLA 4 310                    
SITE     3 AE6 10 CLA 4 312  DGD 4 319                                          
SITE     1 AE7 17 ARG 2 111  MET 2 114  TYR 2 195  PRO 2 196                    
SITE     2 AE7 17 GLY 2 197  PHE 2 201  ASP 2 202  TRP 2 206                    
SITE     3 AE7 17 GLY 2 207  LEU 2 217  ARG 2 218  LYS 2 220                    
SITE     4 AE7 17 GLU 2 221  ASN 2 224  LUT 2 501  CLA 2 505                    
SITE     5 AE7 17 CHL 2 513                                                     
SITE     1 AE8  6 LYS 2 220  ASN 2 224  LEU 2 227  LUT 2 501                    
SITE     2 AE8  6 CLA 2 504  CLA 2 510                                          
SITE     1 AE9 13 LEU 2 230  ALA 2 231  GLY 2 234  PHE 2 237                    
SITE     2 AE9 13 GLN 2 238  TYR 2 241  THR 2 242  ASN 2 249                    
SITE     3 AE9 13 HIS 2 253  THR 2 261  ILE 2 262  LUT 2 501                    
SITE     4 AE9 13 CLA 2 511                                                     
SITE     1 AF1 20 LEU 2  77  PRO 2  82  GLY 2  83  ASP 2  84                    
SITE     2 AF1 20 PHE 2  85  GLY 2  86  PHE 2  87  LEU 2  92                    
SITE     3 AF1 20 GLY 2  93  ASN 2 102  VAL 2 103  ALA 2 105                    
SITE     4 AF1 20 GLU 2 106  HIS 2 109  ARG 2 226  MET 2 229                    
SITE     5 AF1 20 PHE 2 237  XAT 2 502  CLA 2 508  CHL 2 526                    
SITE     1 AF2  7 TRP 2 101  ASN 2 102  HIS 2 109  XAT 2 502                    
SITE     2 AF2  7 CLA 2 507  CHL 2 512  CLA 2 514                               
SITE     1 AF3  8 ALA 2 118  ILE 2 122  THR 2 134  PRO 2 135                    
SITE     2 AF3  8 TYR 2 145  XAT 2 502  BCR 2 503  CHL 2 515                    
SITE     1 AF4 10 GLU 2 216  THR 2 219  LYS 2 220  LYS 2 223                    
SITE     2 AF4 10 ASN 2 224  CLA 2 505  LHG 2 517  LEU 3 188                    
SITE     3 AF4 10 BCR 3 303  LMT 3 318                                          
SITE     1 AF5 13 LEU 2 250  HIS 2 253  PRO 2 257  PHE 2 263                    
SITE     2 AF5 13 LUT 2 501  CLA 2 506  CHL 2 526  TRP 3 151                    
SITE     3 AF5 13 THR 3 156  VAL 3 159  LEU 3 160  ALA 3 163                    
SITE     4 AF5 13 LEU 3 164                                                     
SITE     1 AF6 11 TYR 2 138  THR 2 139  GLY 2 141  GLU 2 142                    
SITE     2 AF6 11 PHE 2 153  GLU 2 156  TRP 2 236  XAT 2 502                    
SITE     3 AF6 11 CLA 2 508  CHL 2 515  LMG 2 519                               
SITE     1 AF7 15 ARG 2 111  TRP 2 112  TRP 2 162  ALA 2 163                    
SITE     2 AF7 15 ARG 2 166  ARG 2 167  VAL 2 177  GLY 2 194                    
SITE     3 AF7 15 PRO 2 196  TRP 2 200  PHE 2 201  LUT 2 501                    
SITE     4 AF7 15 BCR 2 503  CLA 2 504  CHL 2 516                               
SITE     1 AF8 14 TRP 2 101  GLN 2 104  ALA 2 105  VAL 2 108                    
SITE     2 AF8 14 HIS 2 109  TRP 2 112  GLU 2 156  LEU 2 157                    
SITE     3 AF8 14 ILE 2 160  GLY 2 161  GLU 2 164  ARG 2 167                    
SITE     4 AF8 14 TRP 2 168  CLA 2 508                                          
SITE     1 AF9  8 TYR 2 145  PHE 2 146  GLU 2 156  BCR 2 503                    
SITE     2 AF9  8 CLA 2 509  CHL 2 512  HOH 2 604  TRP 4 241                    
SITE     1 AG1 14 TRP 2 162  ARG 2 166  VAL 2 177  ASN 2 178                    
SITE     2 AG1 14 THR 2 179  ASP 2 180  PRO 2 181  ILE 2 182                    
SITE     3 AG1 14 ASN 2 186  LYS 2 187  LEU 2 199  TRP 2 200                    
SITE     4 AG1 14 BCR 2 503  CHL 2 513                                          
SITE     1 AG2  8 PHE 2  85  LYS 2 223  ARG 2 226  LEU 2 230                    
SITE     2 AG2  8 CLA 2 510  CHL 2 526  HOH 2 602  BCR 3 303                    
SITE     1 AG3  8 GLU 2  97  SER 2  98  TRP 2 101  TRP 2 168                    
SITE     2 AG3  8 LMG 2 524  HOH 2 603  LYS J   5  LMG J1103                    
SITE     1 AG4  7 ASP 2 148  THR 2 149  THR 2 150  PHE 2 153                    
SITE     2 AG4  7 CHL 2 512  HOH 2 605  CLA J1105                               
SITE     1 AG5  1 SER 2  94                                                     
SITE     1 AG6  2 TRP 2  67  CLA 3 317                                          
SITE     1 AG7  1 PHE 2 146                                                     
SITE     1 AG8  6 ALA 2 255  ASP 2 256  TYR 3 150  TRP 3 151                    
SITE     2 AG8  6 CLA 3 310  CLA 3 316                                          
SITE     1 AG9  5 GLU 2  97  LMG 2 518  LMG 2 525  PRO F 201                    
SITE     2 AG9  5 ARG F 205                                                     
SITE     1 AH1  2 LMG 2 524  LMG 4 322                                          
SITE     1 AH2 18 TRP 2  67  PHE 2  68  PRO 2  69  PHE 2  85                    
SITE     2 AH2 18 CLA 2 507  CLA 2 511  LHG 2 517  HOH 2 602                    
SITE     3 AH2 18 VAL 3 159  ALA 3 163  GLY 3 166  PHE 3 167                    
SITE     4 AH2 18 HIS 3 170  ARG 3 171  GLN 3 174  PHE 3 187                    
SITE     5 AH2 18 BCR 3 303  CLA 3 317                                          
SITE     1 AH3 16 MET 3 110  PHE 3 208  ASN 3 209  PRO 3 210                    
SITE     2 AH3 16 LEU 3 211  GLY 3 212  ASN 3 230  LEU 3 233                    
SITE     3 AH3 16 ALA 3 237  GLN 3 244  PRO 3 252  LEU 3 256                    
SITE     4 AH3 16 BCR 3 304  CLA 3 305  CLA 3 306  CLA 3 307                    
SITE     1 AH4 16 PHE 3  78  ASP 3  79  PRO 3  80  LEU 3  81                    
SITE     2 AH4 16 LEU 3  83  ASN 3 105  PHE 3 108  GLY 3 112                    
SITE     3 AH4 16 TRP 3 136  THR 3 139  VAL 3 141  MET 3 235                    
SITE     4 AH4 16 ILE 3 238  CLA 3 308  CLA 3 309  CLA 3 310                    
SITE     1 AH5 12 CLA 2 510  LHG 2 517  CHL 2 526  LEU 3 164                    
SITE     2 AH5 12 MET 3 165  TYR 3 186  PHE 3 187  LEU 3 188                    
SITE     3 AH5 12 BCR 3 304  CLA 3 310  CHL 3 314  CLA 3 316                    
SITE     1 AH6  8 LEU 3 111  VAL 3 114  TYR 3 121  LEU 3 190                    
SITE     2 AH6  8 PHE 3 207  LUT 3 301  BCR 3 303  CHL 3 314                    
SITE     1 AH7 17 ARG 3 107  MET 3 110  LEU 3 111  TYR 3 202                    
SITE     2 AH7 17 GLY 3 204  PHE 3 208  ASN 3 209  PHE 3 213                    
SITE     3 AH7 17 LEU 3 220  LEU 3 223  LYS 3 224  LYS 3 226                    
SITE     4 AH7 17 GLU 3 227  ASN 3 230  LUT 3 301  CLA 3 306                    
SITE     5 AH7 17 CHL 3 314                                                     
SITE     1 AH8  8 PHE 3 213  LEU 3 223  LYS 3 226  ASN 3 230                    
SITE     2 AH8  8 LEU 3 233  LUT 3 301  CLA 3 305  CLA 3 311                    
SITE     1 AH9 14 LEU 3 236  ALA 3 237  GLY 3 240  ILE 3 243                    
SITE     2 AH9 14 GLN 3 244  THR 3 248  ASN 3 255  LEU 3 256                    
SITE     3 AH9 14 HIS 3 259  ASN 3 266  ASN 3 267  VAL 3 268                    
SITE     4 AH9 14 LUT 3 301  CLA 3 312                                          
SITE     1 AI1 19 LEU 3  68  LEU 3  72  GLY 3  74  ASP 3  75                    
SITE     2 AI1 19 TYR 3  76  GLY 3  77  PHE 3  78  ASP 3  79                    
SITE     3 AI1 19 LEU 3  83  SER 3  84  LEU 3  98  ALA 3  99                    
SITE     4 AI1 19 GLU 3 102  ASN 3 105  ARG 3 232  MET 3 235                    
SITE     5 AI1 19 LEU 3 236  LUT 3 302  CLA 3 309                               
SITE     1 AI2  9 PHE 3  92  TRP 3  97  LEU 3  98  ASN 3 105                    
SITE     2 AI2  9 LUT 3 302  CLA 3 308  CLA 3 315  CLA A 810                    
SITE     3 AI2  9 CLA A 813                                                     
SITE     1 AI3 10 LMT 2 523  LEU 3 111  GLY 3 115  THR 3 132                    
SITE     2 AI3 10 THR 3 139  TYR 3 150  LUT 3 302  BCR 3 303                    
SITE     3 AI3 10 CLA 3 316  HOH 3 402                                          
SITE     1 AI4  5 LEU 3 225  LYS 3 226  LYS 3 229  ASN 3 230                    
SITE     2 AI4  5 CLA 3 306                                                     
SITE     1 AI5  5 HIS 3 259  PRO 3 263  ASN 3 266  VAL 3 268                    
SITE     2 AI5  5 CLA 3 307                                                     
SITE     1 AI6  7 VAL 3 141  PRO 3 143  ASN 3 154  TYR 3 155                    
SITE     2 AI6  7 PHE 3 158  GLU 3 161  CLA 3 316                               
SITE     1 AI7 17 TYR 3 100  ILE 3 104  ARG 3 107  PHE 3 108                    
SITE     2 AI7 17 ALA 3 168  ARG 3 171  ARG 3 172  ASP 3 175                    
SITE     3 AI7 17 MET 3 182  PHE 3 187  PHE 3 194  PRO 3 200                    
SITE     4 AI7 17 PRO 3 203  PHE 3 208  BCR 3 303  BCR 3 304                    
SITE     5 AI7 17 CLA 3 305                                                     
SITE     1 AI8 16 PHE 3  92  TRP 3  97  TYR 3 100  GLY 3 101                    
SITE     2 AI8 16 ILE 3 104  ASN 3 105  PHE 3 108  MET 3 162                    
SITE     3 AI8 16 GLY 3 166  GLU 3 169  HIS 3 170  ARG 3 172                    
SITE     4 AI8 16 PHE 3 173  CLA 3 309  CLA 3 316  CLA 3 317                    
SITE     1 AI9 13 LMT 2 523  THR 3 139  VAL 3 141  TYR 3 150                    
SITE     2 AI9 13 TRP 3 151  LEU 3 157  LEU 3 160  GLU 3 161                    
SITE     3 AI9 13 LEU 3 164  BCR 3 303  CLA 3 310  CLA 3 313                    
SITE     4 AI9 13 CLA 3 315                                                     
SITE     1 AJ1  6 LMG 2 521  CHL 2 526  MET 3 162  HIS 3 170                    
SITE     2 AJ1  6 PHE 3 173  CLA 3 315                                          
SITE     1 AJ2  2 CLA 2 510  TYR 3 186                                          
SITE     1 AJ3  3 ASP 3  85  GLY 3  88  ILE A  20                               
SITE     1 AJ4 12 LHG 1 517  CHL 1 521  TRP 4 101  LEU 4 148                    
SITE     2 AJ4 12 PHE 4 149  TYR 4 151  VAL 4 152  ILE 4 171                    
SITE     3 AJ4 12 CLA 4 309  CHL 4 314  CHL 4 316  CHL 4 317                    
SITE     1 AJ5 16 MET 4 103  VAL 4 106  PHE 4 189  ASN 4 190                    
SITE     2 AJ5 16 PRO 4 191  LEU 4 192  ASN 4 207  ALA 4 214                    
SITE     3 AJ5 16 PHE 4 218  GLN 4 221  PRO 4 229  CLA 4 304                    
SITE     4 AJ5 16 CLA 4 305  CLA 4 306  CLA 4 311  CHL 4 314                    
SITE     1 AJ6 19 PHE 4  76  ASP 4  77  PRO 4  78  LEU 4  79                    
SITE     2 AJ6 19 ASN 4  98  TRP 4 101  ALA 4 102  GLY 4 105                    
SITE     3 AJ6 19 MET 4 109  TRP 4 126  ALA 4 129  MET 4 212                    
SITE     4 AJ6 19 PHE 4 215  CLA 4 307  CLA 4 308  CLA 4 309                    
SITE     5 AJ6 19 CHL 4 313  CHL 4 316  LMG 4 322                               
SITE     1 AJ7 16 ARG 4 100  MET 4 103  LEU 4 104  TYR 4 184                    
SITE     2 AJ7 16 PRO 4 185  PHE 4 189  ASN 4 190  PHE 4 194                    
SITE     3 AJ7 16 ALA 4 200  LYS 4 201  LYS 4 203  GLU 4 204                    
SITE     4 AJ7 16 ASN 4 207  LUT 4 302  CLA 4 305  CHL 4 314                    
SITE     1 AJ8  6 LYS 4 203  ASN 4 207  LEU 4 210  LUT 4 302                    
SITE     2 AJ8  6 CLA 4 304  CLA 4 310                                          
SITE     1 AJ9 13 LEU 4 213  ALA 4 214  GLY 4 217  ILE 4 220                    
SITE     2 AJ9 13 GLN 4 221  ASN 4 232  HIS 4 236  THR 4 244                    
SITE     3 AJ9 13 ILE 4 245  THR 4 248  LUT 4 302  CLA 4 310                    
SITE     4 AJ9 13 CLA 4 311                                                     
SITE     1 AK1 22 LEU 4  66  PRO 4  71  GLY 4  72  ASP 4  73                    
SITE     2 AK1 22 ASN 4  74  GLY 4  75  PHE 4  76  ASP 4  77                    
SITE     3 AK1 22 ALA 4  82  PHE 4  91  VAL 4  92  ALA 4  94                    
SITE     4 AK1 22 GLU 4  95  ASN 4  98  ARG 4 209  MET 4 212                    
SITE     5 AK1 22 LEU 4 213  XAT 4 303  CLA 4 308  CLA 4 312                    
SITE     6 AK1 22 PHE F 211  ILE F 215                                          
SITE     1 AK2 10 ASN 4  98  PHE 4 215  XAT 4 303  CLA 4 307                    
SITE     2 AK2 10 CHL 4 313  CLA 4 315  TYR F 169  PHE F 211                    
SITE     3 AK2 10 ILE F 215  TYR F 218                                          
SITE     1 AK3  9 GLY 4 108  LEU 4 111  PRO 4 112  VAL 4 123                    
SITE     2 AK3  9 PRO 4 124  TYR 4 134  BCR 4 301  XAT 4 303                    
SITE     3 AK3  9 CHL 4 316                                                     
SITE     1 AK4  9 BCR 2 503  GLU 4 199  GLU 4 202  LYS 4 203                    
SITE     2 AK4  9 ALA 4 206  ASN 4 207  CLA 4 305  CLA 4 306                    
SITE     3 AK4  9 DGD 4 319                                                     
SITE     1 AK5  9 THR 2 151  ILE 2 154  VAL 2 155  HIS 4 236                    
SITE     2 AK5  9 PRO 4 240  TRP 4 241  THR 4 244  LUT 4 302                    
SITE     3 AK5  9 CLA 4 306                                                     
SITE     1 AK6 16 LEU 2 157  GLY 2 161  TRP 2 162  GLY 2 165                    
SITE     2 AK6 16 ARG 2 166  PRO 2 181  BCR 2 503  GLU 4  55                    
SITE     3 AK6 16 TRP 4  56  LEU 4  57  PRO 4  58  ASN 4  74                    
SITE     4 AK6 16 PHE 4  76  CLA 4 307  DGD 4 319  LMG 4 322                    
SITE     1 AK7 10 TYR 4 127  ASP 4 128  GLY 4 130  LYS 4 131                    
SITE     2 AK7 10 SER 4 138  GLU 4 145  XAT 4 303  CLA 4 308                    
SITE     3 AK7 10 CHL 4 316  LMT 4 320                                          
SITE     1 AK8 17 ARG 4 100  TRP 4 101  TYR 4 151  VAL 4 152                    
SITE     2 AK8 17 ARG 4 155  ARG 4 156  ASP 4 159  VAL 4 166                    
SITE     3 AK8 17 ASN 4 167  GLY 4 183  PHE 4 189  PRO 4 191                    
SITE     4 AK8 17 BCR 4 301  LUT 4 302  CLA 4 304  CHL 4 317                    
SITE     5 AK8 17 HOH 4 408                                                     
SITE     1 AK9 15 TRP 4  90  ALA 4  94  VAL 4  97  ASN 4  98                    
SITE     2 AK9 15 TRP 4 101  PHE 4 146  PHE 4 149  HIS 4 150                    
SITE     3 AK9 15 GLU 4 153  ARG 4 156  TRP 4 157  CLA 4 308                    
SITE     4 AK9 15 CLA 4 318  LMT 4 320  ZEX F 301                               
SITE     1 AL1 15 ALA 4 129  GLY 4 130  TYR 4 134  PHE 4 135                    
SITE     2 AL1 15 LEU 4 141  ILE 4 144  GLU 4 145  PHE 4 149                    
SITE     3 AL1 15 PHE 4 189  BCR 4 301  XAT 4 303  CLA 4 309                    
SITE     4 AL1 15 CHL 4 313  CHL 4 317  HOH 4 406                               
SITE     1 AL2 15 TYR 4 151  ARG 4 155  VAL 4 166  ASN 4 167                    
SITE     2 AL2 15 GLN 4 168  ASP 4 169  PRO 4 170  PHE 4 172                    
SITE     3 AL2 15 TYR 4 175  SER 4 176  LEU 4 177  ILE 4 188                    
SITE     4 AL2 15 BCR 4 301  CHL 4 314  CHL 4 316                               
SITE     1 AL3 11 CLA 1 516  LHG 1 517  LMG 1 518  CHL 1 521                    
SITE     2 AL3 11 PHE 4 146  HIS 4 150  ILE 4 154  TRP 4 157                    
SITE     3 AL3 11 CLA 4 315  ZEX F 301  LMG F 304                               
SITE     1 AL4 11 PRO 2 181  BCR 2 503  LYS 4  52  ALA 4 206                    
SITE     2 AL4 11 ARG 4 209  LEU 4 210  LEU 4 213  CLA 4 310                    
SITE     3 AL4 11 CLA 4 312  HOH 4 402  HOH 4 409                               
SITE     1 AL5  4 SER 4 138  PHE 4 142  CHL 4 313  CLA 4 315                    
SITE     1 AL6  4 LMG 1 518  LYS 4 161  ZEX F 301  LMG F 305                    
SITE     1 AL7  8 LMG 2 525  LEU 4  60  PRO 4  78  LEU 4  79                    
SITE     2 AL7  8 XAT 4 303  CLA 4 312  ARG F 205  PHE F 208                    
SITE     1 AL8 20 TYR A 461  TYR A 606  ASN A 607  PHE A 614                    
SITE     2 AL8 20 ILE A 649  TRP A 652  LEU A 657  ALA A 661                    
SITE     3 AL8 20 PHE A 679  HIS A 683  TRP A 686  TYR A 738                    
SITE     4 AL8 20 THR A 745  THR A 746  PHE A 749  CLA A 803                    
SITE     5 AL8 20 CLA A 854  LEU B 620  TRP B 625  CLA B 803                    
SITE     1 AL9 23 PHE A 684  ALA A 687  PHE A 688  MET A 691                    
SITE     2 AL9 23 PHE A 694  TYR A 699  TRP A 700  LEU A 703                    
SITE     3 AL9 23 CLA A 841  CLA A 854  SER B 423  SER B 426                    
SITE     4 AL9 23 LEU B 427  GLY B 430  PHE B 431  LEU B 434                    
SITE     5 AL9 23 LEU B 525  LEU B 532  ILE B 533  LEU B 578                    
SITE     6 AL9 23 PHE B 581  TRP B 582  CLA J1101                               
SITE     1 AM1 23 PHE A 458  ILE A 462  PHE A 547  PHE A 603                    
SITE     2 AM1 23 TRP A 604  ASN A 607  ILE A 649  TRP A 686                    
SITE     3 AM1 23 TYR A 738  CL0 A 801  HOH A 910  TRP B 648                    
SITE     4 AM1 23 LEU B 651  HIS B 654  LEU B 655  TRP B 657                    
SITE     5 AM1 23 ALA B 658  BCR B 802  CLA B 803  CLA B 804                    
SITE     6 AM1 23 CLA B 810  CLA B 811  BCR I 101                               
SITE     1 AM2 13 TRP A  34  HIS A  39  PHE A  40  ALA A  61                    
SITE     2 AM2 13 HIS A  62  ILE A  88  CLA A 805  CLA A 806                    
SITE     3 AM2 13 CLA A 809  CLA A 811  CLA A 830  CLA J1101                    
SITE     4 AM2 13 LUT J1109                                                     
SITE     1 AM3 21 HIS A  62  PHE A  64  VAL A  78  HIS A  82                    
SITE     2 AM3 21 GLN A  85  LEU A  86  ILE A  89  PHE A  90                    
SITE     3 AM3 21 PHE A 174  TRP A 354  HIS A 355  LEU A 358                    
SITE     4 AM3 21 ASN A 361  LEU A 362  CLA A 804  CLA A 806                    
SITE     5 AM3 21 CLA A 813  CLA A 814  CLA A 825  CLA A 830                    
SITE     6 AM3 21 BCR A 849                                                     
SITE     1 AM4 12 HIS A  62  GLN A  85  LEU A 365  ILE A 402                    
SITE     2 AM4 12 PHE A 405  CLA A 804  CLA A 805  CLA A 828                    
SITE     3 AM4 12 CLA A 829  CLA A 830  BCR A 849  LHG A 853                    
SITE     1 AM5 15 LEU A  91  TRP A  92  SER A  94  GLY A  95                    
SITE     2 AM5 15 PHE A  98  HIS A  99  PHE A 103  GLN A 121                    
SITE     3 AM5 15 TRP A 124  CLA A 808  CLA A 809  LMT A 846                    
SITE     4 AM5 15 HOH A 934  CLA J1105  BCR J1108                               
SITE     1 AM6 16 TRP A  92  MET A  96  ALA A 120  GLN A 121                    
SITE     2 AM6 16 GLN A 144  ILE A 145  THR A 146  SER A 147                    
SITE     3 AM6 16 TYR A 675  CLA A 807  CLA A 809  CLA A 811                    
SITE     4 AM6 16 CLA A 828  BCR A 852  CLA J1101  BCR J1108                    
SITE     1 AM7 17 SER A  87  GLN A 121  VAL A 122  VAL A 123                    
SITE     2 AM7 17 TRP A 124  GLN A 129  LEU A 132  ILE A 143                    
SITE     3 AM7 17 CLA A 804  CLA A 807  CLA A 808  CLA A 811                    
SITE     4 AM7 17 CLA A 828  PHE B 446  ILE J  27  BCR J1108                    
SITE     5 AM7 17 LUT J1109                                                     
SITE     1 AM8 17 GLY 3  90  GLY 3  91  PHE 3  92  ILE 3  93                    
SITE     2 AM8 17 CLA 3 309  ILE A  20  VAL A  22  PHE A  83                    
SITE     3 AM8 17 LEU A 177  MET A 178  ALA A 181  PHE A 184                    
SITE     4 AM8 17 HIS A 185  ALA A 189  TRP A 195  CLA A 812                    
SITE     5 AM8 17 CLA A 813                                                     
SITE     1 AM9 19 LYS A  28  THR A  29  SER A  30  GLN A  33                    
SITE     2 AM9 19 TRP A  34  HIS A  39  LYS A  77  SER A  80                    
SITE     3 AM9 19 LEU A 179  GLY A 182  TRP A 183  TYR A 186                    
SITE     4 AM9 19 HIS A 187  CLA A 804  CLA A 808  CLA A 809                    
SITE     5 AM9 19 LHG A 853  TYR J   7  LUT J1109                               
SITE     1 AN1 14 LEU 3  81  LEU 3  83  VAL A  18  LYS A  19                    
SITE     2 AN1 14 ILE A  20  TRP A 195  ASP A 198  SER A 201                    
SITE     3 AN1 14 HIS A 205  ASN A 320  TRP A 321  CLA A 810                    
SITE     4 AN1 14 CLA A 813  CLA A 820                                          
SITE     1 AN2 16 CLA 3 309  PHE A  79  HIS A  82  PHE A  83                    
SITE     2 AN2 16 LEU A  86  MET A 178  TRP A 195  MET A 202                    
SITE     3 AN2 16 HIS A 205  HIS A 206  GLY A 209  LEU A 210                    
SITE     4 AN2 16 CLA A 805  CLA A 810  CLA A 812  CLA A 825                    
SITE     1 AN3 20 GLY A 157  ILE A 158  GLN A 163  CYS A 166                    
SITE     2 AN3 20 THR A 167  GLY A 170  PHE A 174  GLY A 214                    
SITE     3 AN3 20 SER A 217  TRP A 218  GLY A 220  HIS A 221                    
SITE     4 AN3 20 HIS A 224  VAL A 225  PRO A 245  CLA A 805                    
SITE     5 AN3 20 CLA A 815  CLA A 816  BCR A 848  BCR A 849                    
SITE     1 AN4 11 LEU 3 246  LYS 3 273  LEU A 216  SER A 217                    
SITE     2 AN4 11 HIS A 224  ILE A 249  ARG A 252  PHE A 262                    
SITE     3 AN4 11 CLA A 814  BCR A 848  BCR A 856                               
SITE     1 AN5  6 PRO 3 144  CYS A 166  LEU A 244  HIS A 246                    
SITE     2 AN5  6 CLA A 814  BCR A 848                                          
SITE     1 AN6 15 PHE A 269  TRP A 274  SER A 275  TYR A 277                    
SITE     2 AN6 15 ALA A 278  PHE A 283  HIS A 301  LEU A 304                    
SITE     3 AN6 15 GLY A 506  CLA A 818  CLA A 835  LEU K 119                    
SITE     4 AN6 15 ASN K 123  CLA K1002  BCR K1005                               
SITE     1 AN7 16 THR A 282  PHE A 283  ASP A 298  ILE A 299                    
SITE     2 AN7 16 HIS A 301  HIS A 302  ALA A 305  ILE A 306                    
SITE     3 AN7 16 LEU A 309  HIS A 375  MET A 379  THR A 511                    
SITE     4 AN7 16 CLA A 817  CLA A 819  CLA A 827  CLA A 834                    
SITE     1 AN8 18 ALA A 155  LEU A 211  GLY A 214  SER A 215                    
SITE     2 AN8 18 TRP A 218  GLN A 222  HIS A 302  HIS A 303                    
SITE     3 AN8 18 PHE A 310  LEU A 368  VAL A 372  MET A 376                    
SITE     4 AN8 18 PRO A 381  TYR A 382  CLA A 818  CLA A 827                    
SITE     5 AN8 18 CLA A 829  BCR A 849                                          
SITE     1 AN9 14 PRO 3  80  ASN A 204  HIS A 205  GLY A 209                    
SITE     2 AN9 14 LEU A 213  HIS A 315  THR A 319  TRP A 321                    
SITE     3 AN9 14 CLA A 812  BCR A 856  ALA K 101  ALA K 105                    
SITE     4 AN9 14 VAL K 108  BCR K1005                                          
SITE     1 AO1 16 LEU A 207  PHE A 310  ALA A 313  MET A 316                    
SITE     2 AO1 16 TYR A 317  ILE A 327  ILE A 330  MET A 364                    
SITE     3 AO1 16 CLA A 822  CLA A 823  CLA A 824  CLA A 825                    
SITE     4 AO1 16 CLA A 826  CLA A 827  CLA A 831  BCR A 850                    
SITE     1 AO2 12 MET A 316  HIS A 325  ILE A 330  ALA A 333                    
SITE     2 AO2 12 HIS A 334  CLA A 821  CLA A 823  CLA A 824                    
SITE     3 AO2 12 CLA A 834  CLA A 842  LMG A 847  BCR A 856                    
SITE     1 AO3 15 ILE A 312  HIS A 315  MET A 316  ARG A 318                    
SITE     2 AO3 15 ILE A 323  GLY A 324  HIS A 325  CLA A 821                    
SITE     3 AO3 15 CLA A 822  BCR A 856  PRO K  72  ALA K  78                    
SITE     4 AO3 15 THR K  79  CLA K1002  CLA K1003                               
SITE     1 AO4 16 ILE A 330  LEU A 331  HIS A 343  LEU A 346                    
SITE     2 AO4 16 ASN A 429  LEU A 431  CLA A 821  CLA A 822                    
SITE     3 AO4 16 CLA A 826  CLA A 831  CLA A 834  CLA A 838                    
SITE     4 AO4 16 CLA A 842  LHG A 845  BCR A 850  BCR A 851                    
SITE     1 AO5 17 SER A  75  HIS A  82  VAL A 199  MET A 202                    
SITE     2 AO5 17 LEU A 203  HIS A 206  LEU A 350  THR A 351                    
SITE     3 AO5 17 TRP A 354  GLN A 357  ILE A 360  ASN A 361                    
SITE     4 AO5 17 CLA A 805  CLA A 813  CLA A 821  CLA A 829                    
SITE     5 AO5 17 HOH A 905                                                     
SITE     1 AO6 16 ILE A 370  HIS A 374  MET A 400  ILE A 407                    
SITE     2 AO6 16 ILE A 549  THR A 552  VAL A 553  ILE A 609                    
SITE     3 AO6 16 CLA A 821  CLA A 824  CLA A 827  CLA A 836                    
SITE     4 AO6 16 CLA A 837  CLA A 838  BCR A 851  HOH A 924                    
SITE     1 AO7 16 MET A 364  ILE A 371  HIS A 374  HIS A 375                    
SITE     2 AO7 16 ALA A 378  MET A 379  SER A 512  TRP A 515                    
SITE     3 AO7 16 CLA A 818  CLA A 819  CLA A 821  CLA A 826                    
SITE     4 AO7 16 CLA A 834  CLA A 836  BCR A 851  CLA K1002                    
SITE     1 AO8 18 TRP A  92  MET A  96  THR A 146  SER A 147                    
SITE     2 AO8 18 PHE A 149  SER A 394  THR A 397  HIS A 398                    
SITE     3 AO8 18 TRP A 401  ILE A 743  TRP A 747  CLA A 806                    
SITE     4 AO8 18 CLA A 808  CLA A 809  CLA A 829  BCR A 852                    
SITE     5 AO8 18 CLA A 854  BCR J1108                                          
SITE     1 AO9 15 LEU A  93  PHE A 149  ILE A 152  LEU A 211                    
SITE     2 AO9 15 THR A 369  MET A 376  TYR A 382  LEU A 395                    
SITE     3 AO9 15 HIS A 398  HIS A 399  CLA A 806  CLA A 819                    
SITE     4 AO9 15 CLA A 825  CLA A 828  BCR A 849                               
SITE     1 AP1 20 HIS A  58  ALA A  59  HIS A  62  ASP A  63                    
SITE     2 AP1 20 LEU A 358  LEU A 362  PHE A 405  GLY A 409                    
SITE     3 AP1 20 ALA A 412  HIS A 413  ILE A 416  ARG A 420                    
SITE     4 AP1 20 PHE A 577  ARG A 578  TRP A 595  CLA A 804                    
SITE     5 AP1 20 CLA A 805  CLA A 806  LHG A 853  HOH A 921                    
SITE     1 AP2 17 PHE A 338  THR A 339  ARG A 434  VAL A 435                    
SITE     2 AP2 17 ARG A 437  HIS A 438  HIS A 445  CLA A 821                    
SITE     3 AP2 17 CLA A 824  CLA A 838  CLA A 842  LHG A 845                    
SITE     4 AP2 17 VAL L  57  THR L  71  PRO L  72  LEU L  78                    
SITE     5 AP2 17 CLA L 301                                                     
SITE     1 AP3 15 TRP A 448  ILE A 451  PHE A 452  PHE A 455                    
SITE     2 AP3 15 HIS A 456  CLA A 833  CLA A 837  CLA A 855                    
SITE     3 AP3 15 BCR B 802  CLA B 838  CLA B 839  PQN B 841                    
SITE     4 AP3 15 BCR I 101  BCR I 102  BCR L 302                               
SITE     1 AP4 19 PHE A 455  GLY A 459  LEU A 460  ILE A 462                    
SITE     2 AP4 19 HIS A 463  THR A 466  MET A 467  ARG A 472                    
SITE     3 AP4 19 CLA A 832  CLA B 804  CLA B 810  CLA B 811                    
SITE     4 AP4 19 BCR I 101  PRO L 113  ALA L 117  PRO L 119                    
SITE     5 AP4 19 ARG L 121  BCR L 302  CLA L 304                               
SITE     1 AP5 15 TRP A 491  HIS A 496  ALA A 499  THR A 503                    
SITE     2 AP5 15 ALA A 504  THR A 511  CLA A 818  CLA A 822                    
SITE     3 AP5 15 CLA A 824  CLA A 827  CLA A 835  CLA A 836                    
SITE     4 AP5 15 CLA A 842  BCR A 851  CLA K1002                               
SITE     1 AP6  9 PHE A 283  THR A 503  ALA A 504  PRO A 505                    
SITE     2 AP6  9 GLY A 506  CLA A 817  CLA A 834  BCR A 851                    
SITE     3 AP6  9 CLA K1002                                                     
SITE     1 AP7 16 HIS A 374  TYR A 377  PHE A 488  ALA A 489                    
SITE     2 AP7 16 ILE A 492  GLN A 493  TRP A 515  HIS A 542                    
SITE     3 AP7 16 HIS A 545  HIS A 615  PHE A 616  CLA A 826                    
SITE     4 AP7 16 CLA A 827  CLA A 834  CLA A 837  CLA A 838                    
SITE     1 AP8 17 TRP A 448  PHE A 452  LEU A 453  PRO A 486                    
SITE     2 AP8 17 VAL A 487  PHE A 488  ALA A 489  PHE A 539                    
SITE     3 AP8 17 HIS A 542  HIS A 543  HIS A 550  CLA A 826                    
SITE     4 AP8 17 CLA A 832  CLA A 836  CLA A 838  CLA L 301                    
SITE     5 AP8 17 CLA L 304                                                     
SITE     1 AP9 13 LEU A 446  TRP A 448  VAL A 449  ALA A 546                    
SITE     2 AP9 13 HIS A 550  CLA A 824  CLA A 826  CLA A 831                    
SITE     3 AP9 13 CLA A 836  CLA A 837  LHG A 845  BCR A 851                    
SITE     4 AP9 13 CLA L 301                                                     
SITE     1 AQ1 18 ILE A 707  ALA A 710  HIS A 711  LEU A 714                    
SITE     2 AQ1 18 VAL A 716  CLA A 840  PQN A 844  SER B 420                    
SITE     3 AQ1 18 SER B 423  TRP B 424  LEU B 427  CLA B 831                    
SITE     4 AQ1 18 BCR B 856  VAL F 177  GLY F 178  TYR F 181                    
SITE     5 AQ1 18 CLA F 302  CLA J1102                                          
SITE     1 AQ2 20 THR A  51  ILE A  54  TRP A  55  VAL A 708                    
SITE     2 AQ2 20 HIS A 711  VAL A 716  PRO A 718  PRO A 722                    
SITE     3 AQ2 20 CLA A 839  PQN A 844  HOH A 919  TYR F 181                    
SITE     4 AQ2 20 LEU F 182  GLU F 195  ALA F 203  ALA J  11                    
SITE     5 AQ2 20 SER J  15  TRP J  18  CLA J1101  CLA J1102                    
SITE     1 AQ3 13 PHE A 688  GLN A 729  VAL A 733  THR A 736                    
SITE     2 AQ3 13 HIS A 737  LEU A 740  CLA A 802  PQN A 844                    
SITE     3 AQ3 13 BCR A 852  LHG A 853  BCR B 856  PHE J  19                    
SITE     4 AQ3 13 CLA J1101                                                     
SITE     1 AQ4 11 HIS A 334  LYS A 335  PRO A 337  PHE A 338                    
SITE     2 AQ4 11 CLA A 822  CLA A 824  CLA A 831  CLA A 834                    
SITE     3 AQ4 11 LHG A 845  LMG A 847  BCR A 850                               
SITE     1 AQ5  9 CYS A 581  GLY A 583  PRO A 584  CYS A 590                    
SITE     2 AQ5  9 ARG A 731  CYS B 559  GLY B 561  CYS B 568                    
SITE     3 AQ5  9 TRP B 667                                                     
SITE     1 AQ6 12 MET A 691  PHE A 692  SER A 695  ARG A 697                    
SITE     2 AQ6 12 TRP A 700  ALA A 724  LEU A 725  CLA A 839                    
SITE     3 AQ6 12 CLA A 840  CLA A 841  BCR B 856  CLA J1101                    
SITE     1 AQ7 13 HIS A 334  LYS A 335  GLY A 336  PRO A 337                    
SITE     2 AQ7 13 PHE A 338  THR A 339  HIS A 343  CLA A 824                    
SITE     3 AQ7 13 CLA A 831  CLA A 838  CLA A 842  BCR A 850                    
SITE     4 AQ7 13 CLA L 301                                                     
SITE     1 AQ8  9 ARG A 102  PHE A 103  VAL A 122  VAL A 123                    
SITE     2 AQ8  9 TRP A 124  PRO A 125  CLA A 807  HOH A 906                    
SITE     3 AQ8  9 LUT J1109                                                     
SITE     1 AQ9  2 CLA A 822  CLA A 842                                          
SITE     1 AR1  8 GLY A 170  ALA A 171  PHE A 174  SER A 217                    
SITE     2 AR1  8 CLA A 814  CLA A 815  CLA A 816  BCR A 849                    
SITE     1 AR2  9 GLY A 209  LEU A 213  GLY A 214  CLA A 805                    
SITE     2 AR2  9 CLA A 806  CLA A 814  CLA A 819  CLA A 829                    
SITE     3 AR2  9 BCR A 848                                                     
SITE     1 AR3 10 LEU A 350  ALA A 356  SER A 359  ILE A 360                    
SITE     2 AR3 10 ALA A 414  PHE A 417  CLA A 821  CLA A 824                    
SITE     3 AR3 10 CLA A 842  LHG A 845                                          
SITE     1 AR4  9 MET A 364  SER A 367  CLA A 824  CLA A 826                    
SITE     2 AR4  9 CLA A 827  CLA A 834  CLA A 835  CLA A 838                    
SITE     3 AR4  9 CLA K1002                                                     
SITE     1 AR5  8 PHE A 684  LEU A 740  TRP A 747  CLA A 808                    
SITE     2 AR5  8 CLA A 828  CLA A 841  CLA B 832  BCR B 856                    
SITE     1 AR6 17 TRP A  55  ASN A  56  ALA A  59  ASP A  60                    
SITE     2 AR6 17 PHE A 405  ARG A 578  TRP A 595  SER A 726                    
SITE     3 AR6 17 VAL A 728  GLN A 729  ALA A 732  THR A 736                    
SITE     4 AR6 17 CLA A 806  CLA A 811  CLA A 830  CLA A 841                    
SITE     5 AR6 17 HOH A 903                                                     
SITE     1 AR7 18 LEU A 677  LEU A 680  GLY A 681  HIS A 683                    
SITE     2 AR7 18 PHE A 684  TRP A 686  ALA A 687  CL0 A 801                    
SITE     3 AR7 18 CLA A 802  CLA A 828  ASP B 441  PHE B 581                    
SITE     4 AR7 18 TRP B 582  ASN B 585  LEU B 616  TRP B 657                    
SITE     5 AR7 18 CLA B 803  HOH B 904                                          
SITE     1 AR8 18 SER A 444  ASN A 447  TRP A 448  ILE A 451                    
SITE     2 AR8 18 CLA A 832  LEU B 678  ALA B 681  HIS B 682                    
SITE     3 AR8 18 THR B 685  ALA B 688  BCR B 802  CLA B 838                    
SITE     4 AR8 18 CLA B 839  BCR I 102  LEU L 141  CLA L 301                    
SITE     5 AR8 18 BCR L 302  CLA L 304                                          
SITE     1 AR9 15 LEU A 216  PHE A 269  LEU A 304  LEU A 311                    
SITE     2 AR9 15 HIS A 315  CLA A 815  CLA A 820  CLA A 822                    
SITE     3 AR9 15 CLA A 823  MET K  62  PRO K  72  ALA K 105                    
SITE     4 AR9 15 VAL K 108  VAL K 109  BCR K1005                               
SITE     1 AS1  9 GLN 1 202  SER 1 203  ALA 1 204  PRO 1 206                    
SITE     2 AS1  9 CLA 1 516  ASN B 482  PRO B 484  LMG B 845                    
SITE     3 AS1  9 LMG G 210                                                     
SITE     1 AS2  9 ILE A 451  CLA A 803  CLA A 832  CLA A 855                    
SITE     2 AS2  9 TRP B 648  CLA B 804  CLA B 809  CLA B 810                    
SITE     3 AS2  9 CLA B 839                                                     
SITE     1 AS3 19 LEU A 653  LEU A 657  TRP A 658  CL0 A 801                    
SITE     2 AS3 19 CLA A 803  CLA A 854  ALA B 522  TRP B 589                    
SITE     3 AS3 19 PHE B 592  TRP B 619  SER B 628  ILE B 632                    
SITE     4 AS3 19 PHE B 650  HIS B 654  TRP B 657  TYR B 717                    
SITE     5 AS3 19 THR B 720  TYR B 721  PHE B 724                               
SITE     1 AS4 24 ASN A 447  CYS A 450  ILE A 451  GLY A 454                    
SITE     2 AS4 24 PHE A 455  PHE A 547  LEU A 554  ILE A 555                    
SITE     3 AS4 24 PHE A 603  TRP A 604  CLA A 803  CLA A 833                    
SITE     4 AS4 24 ALA B 658  THR B 659  PHE B 661  MET B 662                    
SITE     5 AS4 24 ILE B 665  SER B 666  TYR B 670  TRP B 671                    
SITE     6 AS4 24 LEU B 674  BCR B 802  CLA B 839  BCR I 101                    
SITE     1 AS5 10 PHE B   5  PHE B   8  ALA B  28  HIS B  29                    
SITE     2 AS5 10 SER B  49  CLA B 806  CLA B 807  LHG B 843                    
SITE     3 AS5 10 DGD B 854  BCR I 102                                          
SITE     1 AS6 22 HIS B  29  PHE B  31  TYR B  43  ILE B  46                    
SITE     2 AS6 22 SER B  49  HIS B  50  GLN B  53  LEU B  54                    
SITE     3 AS6 22 ARG B 174  HIS B 178  ILE B 330  HIS B 331                    
SITE     4 AS6 22 LEU B 334  ALA B 337  LEU B 338  CLA B 805                    
SITE     5 AS6 22 CLA B 807  CLA B 814  CLA B 824  CLA B 829                    
SITE     6 AS6 22 BCR B 850  HOH B 950                                          
SITE     1 AS7 10 HIS B  29  GLN B  53  ILE B  57  TRP B  60                    
SITE     2 AS7 10 ILE B 382  CLA B 805  CLA B 806  CLA B 827                    
SITE     3 AS7 10 CLA B 828  CLA B 829                                          
SITE     1 AS8 14 LEU B  59  GLY B  63  PHE B  66  HIS B  67                    
SITE     2 AS8 14 TRP B  70  GLN B  71  ALA B  90  CLA B 809                    
SITE     3 AS8 14 CLA B 810  LEU I   4  PRO I   5  PHE I   8                    
SITE     4 AS8 14 VAL I  12  BCR I 101                                          
SITE     1 AS9 14 ASN B  64  ALA B  88  HIS B  89  ASN B 114                    
SITE     2 AS9 14 ILE B 115  ALA B 116  TYR B 117  SER B 118                    
SITE     3 AS9 14 TRP B 646  BCR B 802  CLA B 808  CLA B 810                    
SITE     4 AS9 14 CLA B 827  BCR I 101                                          
SITE     1 AT1 26 THR A 466  ALA A 469  LEU A 470  CLA A 803                    
SITE     2 AT1 26 CLA A 833  HIS B  89  ALA B  90  ILE B  91                    
SITE     3 AT1 26 TRP B  92  ASP B  93  HIS B  95  PHE B  96                    
SITE     4 AT1 26 ASN B 114  SER B 644  VAL B 645  TRP B 648                    
SITE     5 AT1 26 BCR B 802  CLA B 808  CLA B 809  CLA B 811                    
SITE     6 AT1 26 CLA B 839  DGD B 854  PHE I  16  MET I  21                    
SITE     7 AT1 26 BCR I 101  BCR I 102                                          
SITE     1 AT2 14 CLA A 803  CLA A 833  PRO B  94  HIS B  95                    
SITE     2 AT2 14 CLA B 810  GLY H 107  LEU H 123  GLY I  13                    
SITE     3 AT2 14 LEU I  14  LEU I  15  BCR I 101  PRO L 119                    
SITE     4 AT2 14 LEU L 132  BCR L 302                                          
SITE     1 AT3 13 PHE B  51  ALA B 152  LEU B 155  HIS B 156                    
SITE     2 AT3 13 LYS B 160  TRP B 161  TRP B 167  CLA B 813                    
SITE     3 AT3 13 CLA B 814  CLA B 815  LMT B 846  ARG G 107                    
SITE     4 AT3 13 LMT G 208                                                     
SITE     1 AT4 15 TRP B 167  ASN B 170  SER B 173  HIS B 177                    
SITE     2 AT4 15 THR B 293  ASN B 294  PHE B 295  CLA B 812                    
SITE     3 AT4 15 CLA B 814  CLA B 821  BCR B 850  ASP G 105                    
SITE     4 AT4 15 ARG G 107  TYR G 111  LMT G 208                               
SITE     1 AT5 21 PHE B  47  HIS B  50  PHE B  51  LEU B  54                    
SITE     2 AT5 21 TRP B 123  TRP B 167  PHE B 168  ASN B 170                    
SITE     3 AT5 21 ARG B 174  HIS B 177  HIS B 178  GLY B 181                    
SITE     4 AT5 21 LEU B 182  PHE B 183  CLA B 806  CLA B 812                    
SITE     5 AT5 21 CLA B 813  CLA B 819  CLA B 824  CLA B 828                    
SITE     6 AT5 21 BCR B 850                                                     
SITE     1 AT6 19 GLY B 128  LEU B 129  GLY B 138  PHE B 141                    
SITE     2 AT6 19 ILE B 148  SER B 149  SER B 186  ALA B 189                    
SITE     3 AT6 19 TRP B 190  HIS B 193  HIS B 196  VAL B 197                    
SITE     4 AT6 19 ARG B 208  TRP B 209  PHE B 212  CLA B 812                    
SITE     5 AT6 19 CLA B 816  BCR B 850  BCR B 851                               
SITE     1 AT7 14 ALA B 189  ALA B 191  GLY B 192  HIS B 196                    
SITE     2 AT7 14 PHE B 212  VAL B 215  LEU B 216  PRO B 217                    
SITE     3 AT7 14 GLY B 221  LEU B 222  CLA B 815  BCR B 849                    
SITE     4 AT7 14 BCR B 851  LMT B 855                                          
SITE     1 AT8 16 TRP B 230  ASN B 231  LEU B 255  LEU B 257                    
SITE     2 AT8 16 HIS B 275  LEU B 278  ALA B 279  ILE B 282                    
SITE     3 AT8 16 ILE B 492  CLA B 818  ILE G 137  ALA G 144                    
SITE     4 AT8 16 ASN G 148  CLA G 204  BCR G 205  HOH G 303                    
SITE     1 AT9 16 THR B 256  GLY B 259  LEU B 268  ASP B 272                    
SITE     2 AT9 16 HIS B 275  HIS B 276  ILE B 280  LEU B 283                    
SITE     3 AT9 16 HIS B 351  LEU B 355  CLA B 817  CLA B 819                    
SITE     4 AT9 16 CLA B 824  CLA B 826  CLA B 833  CLA B 834                    
SITE     1 AU1 19 TRP B 123  ILE B 127  PHE B 183  SER B 186                    
SITE     2 AU1 19 SER B 187  TRP B 190  HIS B 276  HIS B 277                    
SITE     3 AU1 19 ILE B 280  VAL B 348  MET B 352  ALA B 357                    
SITE     4 AU1 19 TYR B 358  CLA B 814  CLA B 818  CLA B 820                    
SITE     5 AU1 19 CLA B 824  CLA B 826  CLA B 828                               
SITE     1 AU2 13 LEU B 179  PHE B 284  MET B 290  TYR B 291                    
SITE     2 AU2 13 ILE B 304  CLA B 819  CLA B 822  CLA B 823                    
SITE     3 AU2 13 CLA B 824  CLA B 826  BCR B 853  HOH B 914                    
SITE     4 AU2 13 CLA G 201                                                     
SITE     1 AU3 14 ASN B 176  HIS B 177  SER B 180  VAL B 185                    
SITE     2 AU3 14 HIS B 289  THR B 293  PHE B 295  ILE B 297                    
SITE     3 AU3 14 CLA B 813  BCR B 849  BCR B 850  LEU G 129                    
SITE     4 AU3 14 SER G 133  BCR G 205                                          
SITE     1 AU4 14 CLA 1 508  LHG 1 520  ILE B 286  MET B 290                    
SITE     2 AU4 14 HIS B 299  TYR B 303  ILE B 304  HIS B 308                    
SITE     3 AU4 14 CLA B 820  CLA B 840  BCR B 852  GLN G  90                    
SITE     4 AU4 14 ILE G 137  CLA G 201                                          
SITE     1 AU5 11 ILE B 304  LEU B 305  HIS B 308  HIS B 319                    
SITE     2 AU5 11 ILE B 326  MET B 411  CLA B 820  CLA B 824                    
SITE     3 AU5 11 CLA B 830  CLA B 840  BCR B 852                               
SITE     1 AU6 19 ALA B 171  ARG B 174  LEU B 175  HIS B 178                    
SITE     2 AU6 19 PHE B 183  ILE B 301  LEU B 305  TYR B 323                    
SITE     3 AU6 19 LEU B 336  ALA B 337  SER B 340  ILE B 344                    
SITE     4 AU6 19 CLA B 806  CLA B 814  CLA B 818  CLA B 819                    
SITE     5 AU6 19 CLA B 820  CLA B 823  HOH B 957                               
SITE     1 AU7 18 VAL B 343  SER B 346  LEU B 347  GLN B 350                    
SITE     2 AU7 18 GLN B 376  PHE B 387  LEU B 527  THR B 530                    
SITE     3 AU7 18 THR B 531  ILE B 587  CLA B 826  CLA B 830                    
SITE     4 AU7 18 CLA B 835  CLA B 836  CLA B 837  BCR B 853                    
SITE     5 AU7 18 HOH B 953  LMG F 304                                          
SITE     1 AU8 15 SER B 340  VAL B 343  LEU B 347  HIS B 351                    
SITE     2 AU8 15 SER B 354  LEU B 508  CLA B 818  CLA B 819                    
SITE     3 AU8 15 CLA B 820  CLA B 825  CLA B 833  CLA B 835                    
SITE     4 AU8 15 CLA B 837  BCR B 852  BCR B 853                               
SITE     1 AU9 15 TRP B  60  ASN B  64  TYR B 117  SER B 118                    
SITE     2 AU9 15 ALA B 370  THR B 373  HIS B 374  TYR B 377                    
SITE     3 AU9 15 ILE B 378  ILE B 718  ALA B 722  ILE B 726                    
SITE     4 AU9 15 CLA B 807  CLA B 809  CLA B 828                               
SITE     1 AV1 16 THR B  61  GLY B 119  TRP B 123  ALA B 189                    
SITE     2 AV1 16 LEU B 341  THR B 345  VAL B 348  MET B 352                    
SITE     3 AV1 16 TYR B 358  HIS B 374  HIS B 375  CLA B 807                    
SITE     4 AV1 16 CLA B 814  CLA B 819  CLA B 827  BCR B 850                    
SITE     1 AV2 18 ILE B  25  ALA B  26  HIS B  29  ASP B  30                    
SITE     2 AV2 18 LEU B 334  PHE B 381  THR B 384  GLY B 385                    
SITE     3 AV2 18 HIS B 389  ILE B 392  ARG B 396  TYR B 555                    
SITE     4 AV2 18 TRP B 573  PHE B 576  CLA B 806  CLA B 807                    
SITE     5 AV2 18 CLA B 839  DGD B 854                                          
SITE     1 AV3 15 ARG B 314  LEU B 315  VAL B 407  ARG B 410                    
SITE     2 AV3 15 MET B 411  HIS B 414  HIS B 421  CLA B 823                    
SITE     3 AV3 15 CLA B 825  CLA B 831  CLA B 837  CLA B 840                    
SITE     4 AV3 15 LHG B 842  LMG B 844  LMG F 304                               
SITE     1 AV4 13 TRP A 709  ALA A 710  LYS A 713  CLA A 839                    
SITE     2 AV4 13 ALA B 417  HIS B 421  CLA B 830  CLA B 836                    
SITE     3 AV4 13 CLA B 837  LMG B 844  VAL F 227  CLA F 303                    
SITE     4 AV4 13 BCR F 306                                                     
SITE     1 AV5 16 VAL A 127  BCR A 852  GLY B 435  VAL B 438                    
SITE     2 AV5 16 HIS B 439  MET B 443  LYS B 451  ILE B 453                    
SITE     3 AV5 16 BCR B 856  CLA F 302  ASN J  30  ASP J  35                    
SITE     4 AV5 16 ALA J  36  CLA J1102  DGD J1106  BCR J1108                    
SITE     1 AV6 13 TRP B 462  HIS B 467  LEU B 477  LEU B 478                    
SITE     2 AV6 13 TRP B 493  TRP B 497  PHE B 509  CLA B 818                    
SITE     3 AV6 13 CLA B 826  CLA B 834  CLA B 835  BCR B 853                    
SITE     4 AV6 13 HOH B 903                                                     
SITE     1 AV7 13 LEU B 477  ALA B 485  ALA B 488  GLY B 489                    
SITE     2 AV7 13 TRP B 493  CLA B 818  CLA B 833  BCR B 853                    
SITE     3 AV7 13 HOH B 903  TYR G 150  CLA G 204  LMG G 210                    
SITE     4 AV7 13 HOH G 301                                                     
SITE     1 AV8 21 GLN B 350  TYR B 372  GLN B 376  PHE B 459                    
SITE     2 AV8 21 ALA B 460  ILE B 463  GLN B 464  PHE B 509                    
SITE     3 AV8 21 LEU B 510  HIS B 520  ILE B 523  VAL B 590                    
SITE     4 AV8 21 TYR B 593  TRP B 594  LYS B 597  CLA B 825                    
SITE     5 AV8 21 CLA B 826  CLA B 833  CLA B 836  CLA F 303                    
SITE     6 AV8 21 LMG F 304                                                     
SITE     1 AV9 17 PHE B 428  LEU B 429  GLU B 456  PRO B 457                    
SITE     2 AV9 17 ILE B 458  PHE B 459  ALA B 460  PHE B 517                    
SITE     3 AV9 17 HIS B 520  HIS B 521  CLA B 825  CLA B 831                    
SITE     4 AV9 17 CLA B 835  CLA B 837  VAL F 150  PHE F 160                    
SITE     5 AV9 17 CLA F 302                                                     
SITE     1 AW1 11 LEU B 422  ALA B 524  LEU B 527  HIS B 528                    
SITE     2 AW1 11 CLA B 825  CLA B 826  CLA B 830  CLA B 831                    
SITE     3 AW1 11 CLA B 836  CLA B 840  BCR B 853                               
SITE     1 AW2 22 CLA A 832  CLA A 855  THR B  18  TRP B  22                    
SITE     2 AW2 22 HIS B 682  ILE B 691  ARG B 692  TRP B 693                    
SITE     3 AW2 22 ARG B 694  PRO B 697  VAL B 698  CLA B 839                    
SITE     4 AW2 22 PQN B 841  HOH B 924  HOH B 944  LEU I  14                    
SITE     5 AW2 22 ALA I  18  PHE I  25  GLU I  29  BCR I 101                    
SITE     6 AW2 22 BCR I 102  TYR L 148                                          
SITE     1 AW3 21 CLA A 832  CLA A 855  PHE B 652  LEU B 655                    
SITE     2 AW3 21 VAL B 656  THR B 659  PHE B 663  VAL B 711                    
SITE     3 AW3 21 HIS B 712  BCR B 802  CLA B 804  CLA B 810                    
SITE     4 AW3 21 CLA B 829  CLA B 838  PQN B 841  DGD B 854                    
SITE     5 AW3 21 ALA I  18  MET I  21  BCR I 102  ILE L 143                    
SITE     6 AW3 21 CYS L 144                                                     
SITE     1 AW4 18 LEU 1  66  ASN 1  72  PHE 1  76  CLA 1 508                    
SITE     2 AW4 18 LHG 1 520  ALA B 307  HIS B 308  ILE B 309                    
SITE     3 AW4 18 PRO B 310  PRO B 311  ARG B 314  CLA B 822                    
SITE     4 AW4 18 CLA B 823  CLA B 830  CLA B 837  LHG B 842                    
SITE     5 AW4 18 BCR B 852  HOH B 913                                          
SITE     1 AW5 14 CLA A 832  MET B 662  PHE B 663  SER B 666                    
SITE     2 AW5 14 TRP B 667  ARG B 668  TRP B 671  ALA B 699                    
SITE     3 AW5 14 LEU B 700  ALA B 705  CLA B 838  CLA B 839                    
SITE     4 AW5 14 DGD B 854  BCR I 102                                          
SITE     1 AW6  5 LEU 1  66  PRO B 311  CLA B 830  CLA B 840                    
SITE     2 AW6  5 HOH B 913                                                     
SITE     1 AW7  8 ARG B   7  PHE B   8  HIS B  34  ASP B  35                    
SITE     2 AW7  8 ASN B  45  ALA B  48  ILE B  56  CLA B 805                    
SITE     1 AW8  8 GLY B 312  GLY B 313  ARG B 314  ARG B 410                    
SITE     2 AW8  8 CLA B 830  CLA B 831  HOH B 915  LMG F 305                    
SITE     1 AW9  6 CLA 1 516  ASP B 475  SER B 480  DGD B 801                    
SITE     2 AW9  6 LMT B 847  LMG F 304                                          
SITE     1 AX1  3 TRP B 161  CLA B 812  LMT G 208                               
SITE     1 AX2  8 TRP B 462  GLY B 473  PHE B 474  VAL B 476                    
SITE     2 AX2  8 LMG B 845  ARG F 155  CLA F 303  LMG F 304                    
SITE     1 AX3  4 ILE B 501  GLU B 503  ASN B 506  LEU B 508                    
SITE     1 AX4 12 LEU B 188  LEU B 225  LEU B 278  LEU B 285                    
SITE     2 AX4 12 HIS B 289  CLA B 816  CLA B 821  GLN G  83                    
SITE     3 AX4 12 TRP G 131  ILE G 134  CLA G 201  BCR G 205                    
SITE     1 AX5  9 LEU B  54  GLY B 181  SER B 186  CLA B 806                    
SITE     2 AX5  9 CLA B 813  CLA B 814  CLA B 815  CLA B 821                    
SITE     3 AX5  9 CLA B 828                                                     
SITE     1 AX6  8 LEU B  65  TRP B 124  GLY B 138  PHE B 141                    
SITE     2 AX6  8 LEU B 142  TRP B 209  CLA B 815  CLA B 816                    
SITE     1 AX7  7 CLA 1 508  VAL B 535  CLA B 822  CLA B 823                    
SITE     2 AX7  7 CLA B 826  CLA B 840  BCR B 853                               
SITE     1 AX8 15 PHE B 332  LEU B 336  VAL B 343  MET B 383                    
SITE     2 AX8 15 PHE B 387  GLY B 390  PHE B 393  PHE B 394                    
SITE     3 AX8 15 CLA B 820  CLA B 825  CLA B 826  CLA B 833                    
SITE     4 AX8 15 CLA B 834  CLA B 837  BCR B 852                               
SITE     1 AX9 19 SER B   9  LEU B  12  TRP B  22  PHE B  23                    
SITE     2 AX9 19 ILE B  25  ALA B  26  THR B  27  SER B  33                    
SITE     3 AX9 19 ASP B  35  SER B 556  GLN B 704  LEU B 707                    
SITE     4 AX9 19 CLA B 805  CLA B 810  CLA B 829  CLA B 839                    
SITE     5 AX9 19 PQN B 841  TRP C  70  HIS C  71                               
SITE     1 AY1  6 GLY B 221  LEU B 222  GLY B 223  PHE B 226                    
SITE     2 AY1  6 CLA B 816  CLA G 202                                          
SITE     1 AY2 11 CLA A 839  CLA A 841  PQN A 844  BCR A 852                    
SITE     2 AY2 11 PHE B 431  CLA B 832  PRO F 163  PHE F 167                    
SITE     3 AY2 11 ILE F 170  CLA F 302  CLA J1102                               
SITE     1 AY3 10 CYS C  21  PRO C  22  THR C  23  CYS C  48                    
SITE     2 AY3 10 VAL C  49  GLY C  50  CYS C  51  LYS C  52                    
SITE     3 AY3 10 CYS C  54  VAL C  67                                          
SITE     1 AY4  8 CYS C  11  ILE C  12  CYS C  14  THR C  15                    
SITE     2 AY4  8 CYS C  17  CYS C  58  THR C  60  VAL C  65                    
SITE     1 AY5 10 SER 1 203  ALA 1 204  VAL 1 229  LEU 1 230                    
SITE     2 AY5 10 CLA 1 516  LMG 1 518  CLA 4 315  CLA 4 318                    
SITE     3 AY5 10 LMG 4 321  TYR F 218                                          
SITE     1 AY6 14 CLA A 839  TRP B 424  LEU B 427  PHE B 428                    
SITE     2 AY6 14 HIS B 432  CLA B 832  CLA B 836  BCR B 856                    
SITE     3 AY6 14 PHE F 160  GLY F 164  PHE F 167  ALA F 171                    
SITE     4 AY6 14 BCR F 306  BCR J1108                                          
SITE     1 AY7 15 ILE B 458  PHE B 459  TRP B 462  PHE B 474                    
SITE     2 AY7 15 CLA B 831  CLA B 835  LMT B 847  SER F 151                    
SITE     3 AY7 15 GLY F 152  ASP F 153  GLN F 154  TRP F 157                    
SITE     4 AY7 15 ILE F 165  LMG F 304  LMG F 305                               
SITE     1 AY8 11 CLA 1 516  CLA 4 318  CLA B 825  CLA B 830                    
SITE     2 AY8 11 CLA B 835  LMG B 845  LMT B 847  ASP F 153                    
SITE     3 AY8 11 GLN F 154  ARG F 155  CLA F 303                               
SITE     1 AY9  5 LMG 4 321  LMG B 844  LEU F 221  LEU F 222                    
SITE     2 AY9  5 CLA F 303                                                     
SITE     1 AZ1  7 CLA B 831  VAL F 150  PHE F 160  GLY F 175                    
SITE     2 AZ1  7 TRP F 176  TRP F 213  CLA F 302                               
SITE     1 AZ2 18 GLU 1 138  CHL 1 514  LHG 1 520  ILE B 286                    
SITE     2 AZ2 18 HIS B 289  MET B 290  ILE B 297  GLY B 298                    
SITE     3 AZ2 18 HIS B 299  CLA B 820  CLA B 822  BCR B 849                    
SITE     4 AZ2 18 PHE G  79  PHE G  82  GLN G  83  ASN G  86                    
SITE     5 AZ2 18 VAL G  87  GLN G  90                                          
SITE     1 AZ3 12 PHE B 226  LMT B 855  SER G  61  ILE G  64                    
SITE     2 AZ3 12 SER G  65  THR G  68  GLY G  69  LEU G 129                    
SITE     3 AZ3 12 HIS G 136  TYR G 140  BCR G 205  LMT G 209                    
SITE     1 AZ4  9 ARG G  76  PHE G  77  SER G 117  ASN G 118                    
SITE     2 AZ4  9 ASP G 119  PRO G 120  ILE G 125  VAL G 128                    
SITE     3 AZ4  9 BCR G 205                                                     
SITE     1 AZ5 16 ALA 1 112  ALA 1 113  LEU 1 131  LEU 1 135                    
SITE     2 AZ5 16 CHL 1 512  LHG 1 520  CLA B 817  CLA B 834                    
SITE     3 AZ5 16 TYR G 141  THR G 145  ASN G 148  TYR G 150                    
SITE     4 AZ5 16 PRO G 152  LMG G 206  HOH G 301  HOH G 302                    
SITE     1 AZ6 11 CLA B 817  CLA B 821  BCR B 849  THR G  68                    
SITE     2 AZ6 11 LEU G  72  LEU G 129  GLY G 132  SER G 133                    
SITE     3 AZ6 11 HIS G 136  CLA G 202  CLA G 203                               
SITE     1 AZ7 13 ALA 1 112  LEU 1 114  PRO 1 115  PRO 1 132                    
SITE     2 AZ7 13 LEU 1 135  PHE 1 139  CHL 1 512  VAL G 138                    
SITE     3 AZ7 13 TYR G 141  ILE G 142  THR G 145  CLA G 204                    
SITE     4 AZ7 13 DGD G 207                                                     
SITE     1 AZ8  9 PRO 1 115  THR 1 133  VAL 1 136  PHE 1 139                    
SITE     2 AZ8  9 VAL G  63  SER G  67  LEU G  70  SER G 146                    
SITE     3 AZ8  9 LMG G 206                                                     
SITE     1 AZ9  4 CLA B 812  CLA B 813  LMT B 846  ARG G 107                    
SITE     1 BC1  4 ASN G  59  PRO G  60  SER G  61  CLA G 202                    
SITE     1 BC2  7 CHL 1 512  ASN B 482  DGD B 801  CLA B 834                    
SITE     2 BC2  7 PRO G 152  LYS G 153  PHE G 154                               
SITE     1 BC3  9 ASN H  79  LEU H  81  GLN H  82  PHE H  85                    
SITE     2 BC3  9 TRP L  81  LEU L 104  CLA L 303  BCR L 306                    
SITE     3 BC3  9 BCR L 307                                                     
SITE     1 BC4 13 CLA A 803  CLA A 832  CLA A 833  CLA B 804                    
SITE     2 BC4 13 CLA B 808  CLA B 809  CLA B 810  CLA B 811                    
SITE     3 BC4 13 CLA B 838  VAL I  12  LEU I  14  PRO I  17                    
SITE     4 BC4 13 BCR L 302                                                     
SITE     1 BC5 17 CLA A 832  CLA A 855  CLA B 805  CLA B 810                    
SITE     2 BC5 17 CLA B 838  CLA B 839  PQN B 841  MET I  21                    
SITE     3 BC5 17 LEU I  24  PHE I  25  HIS L 106  LEU L 141                    
SITE     4 BC5 17 CYS L 144  LEU L 145  TYR L 148  PHE L 189                    
SITE     5 BC5 17 CLA L 304                                                     
SITE     1 BC6 16 PRO A  37  LEU A  57  HIS A  58  CLA A 802                    
SITE     2 BC6 16 CLA A 804  CLA A 808  CLA A 840  CLA A 841                    
SITE     3 BC6 16 PQN A 844  ALA J  11  PRO J  12  THR J  16                    
SITE     4 BC6 16 PHE J  19  ALA J  20  BCR J1108  LUT J1109                    
SITE     1 BC7 13 CLA A 839  CLA A 840  CLA B 832  BCR B 856                    
SITE     2 BC7 13 TRP F 173  ILE F 174  VAL F 177  VAL F 207                    
SITE     3 BC7 13 TRP J  18  PHE J  19  LEU J  22  HOH J1201                    
SITE     4 BC7 13 HOH J1203                                                     
SITE     1 BC8 10 LMG 2 518  ILE F 198  ASP F 199  VAL F 200                    
SITE     2 BC8 10 PRO F 201  THR F 204  ARG J   2  LYS J   5                    
SITE     3 BC8 10 THR J   6  SER J   9                                          
SITE     1 BC9  5 ARG F 128  ASN F 132  PHE J  33  DGD J1106                    
SITE     2 BC9  5 LMT J1107                                                     
SITE     1 BD1  7 LMG 2 519  CLA A 807  GLU J  28  ARG J  31                    
SITE     2 BD1  7 PHE J  32  LMT J1107  LUT J1109                               
SITE     1 BD2 19 PHE B 428  HIS B 432  HIS B 521  CLA B 832                    
SITE     2 BD2 19 ARG F 128  ASN F 132  LYS F 135  PHE F 160                    
SITE     3 BD2 19 PRO F 163  ILE J  29  PHE J  33  PRO J  34                    
SITE     4 BD2 19 ALA J  36  LEU J  37  THR J  38  PHE J  39                    
SITE     5 BD2 19 PRO J  40  PHE J  41  LMG J1104                               
SITE     1 BD3  4 ARG F 128  ARG J  31  LMG J1104  CLA J1105                    
SITE     1 BD4 11 ILE A  88  LEU A  91  CLA A 807  CLA A 808                    
SITE     2 BD4 11 CLA A 809  CLA A 828  CLA B 832  CLA F 302                    
SITE     3 BD4 11 LEU J  26  ASN J  30  CLA J1101                               
SITE     1 BD5 13 ILE A 126  CLA A 804  CLA A 809  CLA A 811                    
SITE     2 BD5 13 LMT A 846  TYR J   7  PRO J  12  THR J  16                    
SITE     3 BD5 13 ALA J  20  GLU J  28  ARG J  31  CLA J1101                    
SITE     4 BD5 13 CLA J1105                                                     
SITE     1 BD6  9 PHE A 269  PHE A 270  LEU A 272  ASN K  52                    
SITE     2 BD6  9 MET K  55  VAL K  56  THR K  59  HIS K 111                    
SITE     3 BD6  9 BCR K1005                                                     
SITE     1 BD7 11 CLA A 817  CLA A 823  CLA A 827  CLA A 834                    
SITE     2 BD7 11 CLA A 835  BCR A 851  ILE K 112  ILE K 113                    
SITE     3 BD7 11 GLY K 116  VAL K 117  ILE K 124                               
SITE     1 BD8  5 CLA A 823  LEU K  61  MET K  62  ALA K  65                    
SITE     2 BD8  5 LEU K  70                                                     
SITE     1 BD9  5 ARG K  67  GLY K  93  ASP K  94  THR K 103                    
SITE     2 BD9  5 BCR K1005                                                     
SITE     1 BE1 11 CLA A 817  CLA A 820  BCR A 856  LEU K  63                    
SITE     2 BE1 11 LEU K 104  GLY K 107  VAL K 108  HIS K 111                    
SITE     3 BE1 11 ILE K 112  CLA K1001  CLA K1004                               
SITE     1 BE2 18 HIS A 445  TRP A 448  CLA A 831  CLA A 837                    
SITE     2 BE2 18 CLA A 838  LHG A 845  CLA A 855  ALA B 681                    
SITE     3 BE2 18 ARG B 684  THR B 685  PRO B 686  LEU L  69                    
SITE     4 BE2 18 THR L  71  VAL L  73  THR L  74  LEU L  83                    
SITE     5 BE2 18 BCR L 302  CLA L 304                                          
SITE     1 BE3  8 CLA A 832  CLA A 833  CLA A 855  CLA B 811                    
SITE     2 BE3  8 BCR I 101  ALA L 133  CLA L 301  CLA L 304                    
SITE     1 BE4 13 PRO H  77  TYR H  78  GLN H  82  PHE H  86                    
SITE     2 BE4 13 CLA H1000  TYR L  82  ASN L  85  ARG L  90                    
SITE     3 BE4 13 GLU L 101  LEU L 104  ALA L 105  CLA L 304                    
SITE     4 BE4 13 BCR L 306                                                     
SITE     1 BE5 19 CLA A 833  CLA A 837  CLA A 855  PRO B 686                    
SITE     2 BE5 19 LEU B 687  ALA B 688  BCR I 102  TYR L  82                    
SITE     3 BE5 19 LEU L  86  PRO L  87  GLY L  88  GLU L 101                    
SITE     4 BE5 19 VAL L 102  HIS L 106  LEU L 109  CLA L 301                    
SITE     5 BE5 19 BCR L 302  CLA L 303  BCR L 306                               
SITE     1 BE6 10 PHE L 108  LEU L 109  GLY L 112  PRO L 113                    
SITE     2 BE6 10 LYS L 116  LEU L 203  LEU L 207  LEU L 209                    
SITE     3 BE6 10 BCR L 307  HOH L 401                                          
SITE     1 BE7 10 CLA H1000  LEU L 104  ALA L 105  PHE L 108                    
SITE     2 BE7 10 SER L 195  ILE L 198  TRP L 199  CLA L 303                    
SITE     3 BE7 10 CLA L 304  BCR L 307                                          
SITE     1 BE8  7 LEU H  81  PHE H  85  CLA H1000  TRP L 199                    
SITE     2 BE8  7 LEU L 203  CLA L 305  BCR L 306                               
CRYST1  189.611  200.994  212.943  90.00  90.00  90.00 P 21 21 21    4          
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      0.005274  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004975  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004696        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system