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Database: PDB
Entry: 4L6V
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HEADER    ELECTRON TRANSPORT                      13-JUN-13   4L6V              
TITLE     CRYSTAL STRUCTURE OF A VIRUS LIKE PHOTOSYSTEM I FROM THE              
TITLE    2 CYANOBACTERIUM SYNECHOCYSTIS PCC 6803                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1;            
COMPND   3 CHAIN: A, a, 1;                                                      
COMPND   4 SYNONYM: PSAA;                                                       
COMPND   5 EC: 1.97.1.12;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2;            
COMPND   9 CHAIN: B, b, 2;                                                      
COMPND  10 SYNONYM: PSAB;                                                       
COMPND  11 EC: 1.97.1.12;                                                       
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: PHOTOSYSTEM I IRON-SULFUR CENTER;                          
COMPND  15 CHAIN: C, c, 3;                                                      
COMPND  16 SYNONYM: 9 KDA POLYPEPTIDE, PSI-C, PHOTOSYSTEM I SUBUNIT VII, PSAC;  
COMPND  17 EC: 1.97.1.12;                                                       
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: PHOTOSYSTEM I SUBUNIT II;                                  
COMPND  21 CHAIN: D, d, 4;                                                      
COMPND  22 EC: 1.97.1.12;                                                       
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 MOL_ID: 5;                                                           
COMPND  25 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT IV;                  
COMPND  26 CHAIN: E, e, 5;                                                      
COMPND  27 EC: 1.97.1.12;                                                       
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 MOL_ID: 6;                                                           
COMPND  30 MOLECULE: FUSION PROTEIN OF PHOTOSYSTEM I SUBUNIT III AND SUBUNIT IX;
COMPND  31 CHAIN: F, f, 6;                                                      
COMPND  32 SYNONYM: PSI SUBUNIT V, PSI-L;                                       
COMPND  33 EC: 1.97.1.12;                                                       
COMPND  34 ENGINEERED: YES;                                                     
COMPND  35 MOL_ID: 7;                                                           
COMPND  36 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT XI;                  
COMPND  37 CHAIN: L, l, 8;                                                      
COMPND  38 SYNONYM: PSI-M;                                                      
COMPND  39 EC: 1.97.1.12;                                                       
COMPND  40 ENGINEERED: YES;                                                     
COMPND  41 MOL_ID: 8;                                                           
COMPND  42 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT XII;                 
COMPND  43 CHAIN: M, m, 7;                                                      
COMPND  44 EC: 1.97.1.12;                                                       
COMPND  45 ENGINEERED: YES;                                                     
COMPND  46 MOL_ID: 9;                                                           
COMPND  47 MOLECULE: PHOTOSYSTEM I SUBUNIT III;                                 
COMPND  48 CHAIN: i, 9, I;                                                      
COMPND  49 EC: 1.97.1.12;                                                       
COMPND  50 ENGINEERED: YES;                                                     
COMPND  51 MOL_ID: 10;                                                          
COMPND  52 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT VIII;                
COMPND  53 CHAIN: K, k, 0;                                                      
COMPND  54 EC: 1.97.1.12;                                                       
COMPND  55 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE   3 ORGANISM_TAXID: 1148;                                                
SOURCE   4 GENE: PSAA, BEST7613_2234, MYO_18690;                                
SOURCE   5 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE   9 ORGANISM_TAXID: 1148;                                                
SOURCE  10 GENE: PSAB, BEST7613_2235, MYO_18700;                                
SOURCE  11 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  15 ORGANISM_TAXID: 1148;                                                
SOURCE  16 GENE: PSAC, BEST7613_5694, MYO_120930;                               
SOURCE  17 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  19 MOL_ID: 4;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  21 ORGANISM_TAXID: 1148;                                                
SOURCE  22 GENE: PSAE, BEST7613_5968, MYO_118260;                               
SOURCE  23 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  25 MOL_ID: 5;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  27 ORGANISM_TAXID: 1148;                                                
SOURCE  28 GENE: PSAF, BEST7613_2928;                                           
SOURCE  29 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  30 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  31 MOL_ID: 6;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803, BACILLUS SUBTILIS   
SOURCE  33 BEST7613;                                                            
SOURCE  34 ORGANISM_TAXID: 1148, 1204343;                                       
SOURCE  35 GENE: PSAL, BEST7613_4425, MYO_131030, PSAF,BEST7613_2928;           
SOURCE  36 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  37 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  38 MOL_ID: 7;                                                           
SOURCE  39 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  40 ORGANISM_TAXID: 1148;                                                
SOURCE  41 GENE: PSBM, PSAM, BEST7613_1787, MYO_14340;                          
SOURCE  42 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  43 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  44 MOL_ID: 8;                                                           
SOURCE  45 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  46 ORGANISM_TAXID: 1148;                                                
SOURCE  47 GENE: PSAF, BEST7613_2928;                                           
SOURCE  48 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  49 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  50 MOL_ID: 9;                                                           
SOURCE  51 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  52 ORGANISM_TAXID: 1148;                                                
SOURCE  53 GENE: PSAI, BEST7613_4424, MYO_131040;                               
SOURCE  54 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  55 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  56 MOL_ID: 10;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  58 ORGANISM_TAXID: 1148;                                                
SOURCE  59 GENE: PSAD, BEST7613_1459, MYO_11100;                                
SOURCE  60 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  61 EXPRESSION_SYSTEM_TAXID: 1148                                        
KEYWDS    PHOTOSYNTHETIC REACTION CENTER, MEMBRANE COMPLEX, PLASTOCYANIN,       
KEYWDS   2 CYTOCHROME C6, FERREDOXIN, ELECTRON TRANSPORT                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.MAZOR,D.NATAF,H.TOPORIK,N.NELSON                                    
REVDAT   3   26-JUL-17 4L6V    1       SOURCE REMARK                            
REVDAT   2   07-MAY-14 4L6V    1       JRNL                                     
REVDAT   1   05-FEB-14 4L6V    0                                                
JRNL        AUTH   Y.MAZOR,D.NATAF,H.TOPORIK,N.NELSON                           
JRNL        TITL   CRYSTAL STRUCTURES OF VIRUS-LIKE PHOTOSYSTEM I COMPLEXES     
JRNL        TITL 2 FROM THE MESOPHILIC CYANOBACTERIUM SYNECHOCYSTIS PCC 6803.   
JRNL        REF    ELIFE                         V.   3 01496 2014              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   24473073                                                     
JRNL        DOI    10.7554/ELIFE.01496                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 109176                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.255                           
REMARK   3   R VALUE            (WORKING SET) : 0.253                           
REMARK   3   FREE R VALUE                     : 0.297                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5477                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.9972 - 11.5842    0.96     3632   183  0.2385 0.2719        
REMARK   3     2 11.5842 -  9.2844    0.97     3588   185  0.1578 0.1798        
REMARK   3     3  9.2844 -  8.1375    0.98     3561   208  0.1648 0.1988        
REMARK   3     4  8.1375 -  7.4058    0.98     3557   177  0.1936 0.2336        
REMARK   3     5  7.4058 -  6.8818    0.97     3576   185  0.2137 0.2764        
REMARK   3     6  6.8818 -  6.4804    0.93     3335   166  0.2436 0.3275        
REMARK   3     7  6.4804 -  6.1588    0.96     3495   178  0.2513 0.3518        
REMARK   3     8  6.1588 -  5.8928    0.97     3560   172  0.2574 0.3121        
REMARK   3     9  5.8928 -  5.6675    0.97     3531   179  0.2503 0.3116        
REMARK   3    10  5.6675 -  5.4732    0.97     3499   200  0.2620 0.3359        
REMARK   3    11  5.4732 -  5.3030    0.97     3523   191  0.2579 0.2986        
REMARK   3    12  5.3030 -  5.1522    0.97     3509   200  0.2490 0.3212        
REMARK   3    13  5.1522 -  5.0172    0.96     3478   181  0.2448 0.2867        
REMARK   3    14  5.0172 -  4.8953    0.97     3491   174  0.2431 0.3257        
REMARK   3    15  4.8953 -  4.7845    0.97     3457   203  0.2497 0.2969        
REMARK   3    16  4.7845 -  4.6830    0.96     3482   188  0.2565 0.3034        
REMARK   3    17  4.6830 -  4.5897    0.96     3447   167  0.2741 0.3556        
REMARK   3    18  4.5897 -  4.5034    0.91     3280   203  0.2836 0.2753        
REMARK   3    19  4.5034 -  4.4232    0.90     3275   165  0.2959 0.3368        
REMARK   3    20  4.4232 -  4.3485    0.93     3355   175  0.3151 0.3367        
REMARK   3    21  4.3485 -  4.2785    0.94     3374   193  0.3280 0.3770        
REMARK   3    22  4.2785 -  4.2129    0.95     3406   185  0.3312 0.3872        
REMARK   3    23  4.2129 -  4.1511    0.95     3429   185  0.3330 0.3956        
REMARK   3    24  4.1511 -  4.0927    0.95     3473   190  0.3452 0.3823        
REMARK   3    25  4.0927 -  4.0376    0.95     3430   181  0.3632 0.4159        
REMARK   3    26  4.0376 -  3.9852    0.95     3408   173  0.3707 0.3689        
REMARK   3    27  3.9852 -  3.9355    0.95     3408   182  0.3851 0.4212        
REMARK   3    28  3.9355 -  3.8882    0.94     3369   163  0.3903 0.4424        
REMARK   3    29  3.8882 -  3.8431    0.94     3430   160  0.4048 0.4173        
REMARK   3    30  3.8431 -  3.8000    0.93     3341   185  0.4158 0.4549        
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)     : 0.670            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.960           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 202.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 127.7                          
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      :  0.004          72200                                  
REMARK   3   ANGLE     :  1.771         102458                                  
REMARK   3   CHIRALITY :  0.199           9065                                  
REMARK   3   PLANARITY :  0.012          12278                                  
REMARK   3   DIHEDRAL  : 28.623          27473                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' OR CHAIN 'B' OR CHAIN 'M' OR CHAIN 'L' OR    
REMARK   3               CHAIN 'I' OR CHAIN 'F'                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4749  -8.8416 225.6864              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2742 T22:   0.9709                                     
REMARK   3      T33:   1.1907 T12:   0.0589                                     
REMARK   3      T13:   0.1560 T23:   0.1211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5868 L22:   1.2780                                     
REMARK   3      L33:   0.7027 L12:   0.0188                                     
REMARK   3      L13:   0.1405 L23:   0.2061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1336 S12:  -0.3016 S13:  -0.2422                       
REMARK   3      S21:   0.5858 S22:   0.1341 S23:   0.2308                       
REMARK   3      S31:   0.2010 S32:  -0.1500 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'K'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  53.4254   5.2271 213.8921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2938 T22:   1.5441                                     
REMARK   3      T33:   2.1772 T12:  -0.1347                                     
REMARK   3      T13:  -0.1749 T23:  -0.1420                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0049 L22:  -0.0002                                     
REMARK   3      L33:   0.2683 L12:  -0.0081                                     
REMARK   3      L13:  -0.0357 L23:   0.0226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0289 S12:   0.4145 S13:   0.4288                       
REMARK   3      S21:  -0.1928 S22:   0.0782 S23:  -0.5038                       
REMARK   3      S31:  -0.5554 S32:   0.4157 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' OR CHAIN 'D' OR CHAIN 'E'                    
REMARK   3    ORIGIN FOR THE GROUP (A): -16.0597  30.3857 221.9165              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1857 T22:   1.0948                                     
REMARK   3      T33:   1.7564 T12:   0.0884                                     
REMARK   3      T13:   0.1255 T23:  -0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8038 L22:   1.7691                                     
REMARK   3      L33:   1.5544 L12:  -0.0988                                     
REMARK   3      L13:   0.0735 L23:  -0.1762                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0799 S12:  -0.0572 S13:   0.4991                       
REMARK   3      S21:   0.4017 S22:   0.0966 S23:   0.3449                       
REMARK   3      S31:  -0.1416 S32:  -0.3904 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' OR CHAIN 'B' OR CHAIN 'M' OR CHAIN 'L' OR    
REMARK   3               CHAIN 'I' OR CHAIN 'F'                                 
REMARK   3    ORIGIN FOR THE GROUP (A): -95.8480 -93.5217 256.1976              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6700 T22:   2.2926                                     
REMARK   3      T33:   2.2429 T12:   0.4292                                     
REMARK   3      T13:  -0.5073 T23:   0.4322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6879 L22:   1.2593                                     
REMARK   3      L33:   1.0804 L12:   0.2694                                     
REMARK   3      L13:  -0.0677 L23:  -0.1704                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0645 S12:  -0.5681 S13:  -0.4786                       
REMARK   3      S21:   0.5381 S22:  -0.1952 S23:  -0.9485                       
REMARK   3      S31:   0.4374 S32:   0.7397 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'K'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -75.5324 -90.7573 193.4481              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3450 T22:   2.5004                                     
REMARK   3      T33:   3.1146 T12:   0.2877                                     
REMARK   3      T13:   1.0128 T23:  -0.2152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0855 L22:   0.0512                                     
REMARK   3      L33:   0.1764 L12:  -0.0033                                     
REMARK   3      L13:   0.1269 L23:   0.0277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8257 S12:   0.1205 S13:   0.0420                       
REMARK   3      S21:  -0.7231 S22:   0.0044 S23:  -0.1625                       
REMARK   3      S31:  -0.4923 S32:   0.3061 S33:  -0.0005                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' OR CHAIN 'D' OR CHAIN 'E'                    
REMARK   3    ORIGIN FOR THE GROUP (A): -86.6552 -54.5966 258.0298              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8726 T22:   2.6729                                     
REMARK   3      T33:   2.5405 T12:  -0.2587                                     
REMARK   3      T13:  -0.6542 T23:  -0.0605                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3006 L22:   0.0058                                     
REMARK   3      L33:  -0.0082 L12:  -0.1869                                     
REMARK   3      L13:   0.0805 L23:  -0.0491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1288 S12:  -0.5452 S13:   0.1574                       
REMARK   3      S21:   0.6042 S22:  -0.0589 S23:  -0.5422                       
REMARK   3      S31:  -0.8250 S32:   0.6300 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN '1' OR CHAIN '2' OR CHAIN '0' OR CHAIN '8' OR    
REMARK   3               CHAIN '9' OR CHAIN '7' OR CHAIN '6'                    
REMARK   3    ORIGIN FOR THE GROUP (A):  31.1806 -74.6248 271.9616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0613 T22:   1.5202                                     
REMARK   3      T33:   1.1926 T12:  -0.2338                                     
REMARK   3      T13:   0.3210 T23:  -0.2540                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2971 L22:   1.1157                                     
REMARK   3      L33:   1.1791 L12:   0.3145                                     
REMARK   3      L13:   0.1814 L23:  -0.2065                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3584 S12:  -0.8253 S13:   0.2530                       
REMARK   3      S21:   0.9727 S22:  -0.2782 S23:   0.5028                       
REMARK   3      S31:  -0.1649 S32:  -0.0183 S33:   0.0002                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN '3' OR CHAIN '4' OR CHAIN '5'                    
REMARK   3    ORIGIN FOR THE GROUP (A):  40.4210 -35.7687 274.8920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.8682 T22:   1.7433                                     
REMARK   3      T33:   2.1402 T12:  -0.2177                                     
REMARK   3      T13:   0.3727 T23:  -0.6275                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1505 L22:   0.7044                                     
REMARK   3      L33:   0.7824 L12:   0.1350                                     
REMARK   3      L13:  -0.0648 L23:  -0.0247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2455 S12:  -0.5045 S13:   0.8684                       
REMARK   3      S21:   0.6797 S22:  -0.0724 S23:   0.1044                       
REMARK   3      S31:  -0.7941 S32:  -0.0089 S33:  -0.0000                       
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 4L6V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080255.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, SCALA                         
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113221                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.23800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4KT0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30MM TRICINE-NAOH, 90MM NACL, 90MM       
REMARK 280  MGCL2, 100MM GLYCINE, 0.005% NONYL BETA MALTOSIDE., PH 8, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       66.84000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, L, M, K, I          
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: a, b, c, d, e, f, i, l, m, k          
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2, 3, 4, 5, 6, 9, 8, 7, 0          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLY B   731                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     VAL D   141                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLN E    70                                                      
REMARK 465     ALA E    71                                                      
REMARK 465     ALA E    72                                                      
REMARK 465     ALA E    73                                                      
REMARK 465     LYS E    74                                                      
REMARK 465     MET L     1                                                      
REMARK 465     ALA L     2                                                      
REMARK 465     GLU L     3                                                      
REMARK 465     SER L     4                                                      
REMARK 465     ASN L     5                                                      
REMARK 465     GLN L     6                                                      
REMARK 465     MET a     1                                                      
REMARK 465     THR a     2                                                      
REMARK 465     ILE a     3                                                      
REMARK 465     SER a     4                                                      
REMARK 465     PRO a     5                                                      
REMARK 465     PRO a     6                                                      
REMARK 465     GLU a     7                                                      
REMARK 465     ARG a     8                                                      
REMARK 465     GLU a     9                                                      
REMARK 465     ALA a    10                                                      
REMARK 465     LYS a    11                                                      
REMARK 465     ALA a    12                                                      
REMARK 465     MET b     1                                                      
REMARK 465     ALA b     2                                                      
REMARK 465     GLY b   731                                                      
REMARK 465     MET c     1                                                      
REMARK 465     MET d     1                                                      
REMARK 465     THR d     2                                                      
REMARK 465     VAL d   141                                                      
REMARK 465     MET e     1                                                      
REMARK 465     GLN e    70                                                      
REMARK 465     ALA e    71                                                      
REMARK 465     ALA e    72                                                      
REMARK 465     ALA e    73                                                      
REMARK 465     LYS e    74                                                      
REMARK 465     GLU i    39                                                      
REMARK 465     GLY i    40                                                      
REMARK 465     MET l     1                                                      
REMARK 465     ALA l     2                                                      
REMARK 465     GLU l     3                                                      
REMARK 465     SER l     4                                                      
REMARK 465     ASN l     5                                                      
REMARK 465     GLN l     6                                                      
REMARK 465     MET 1     1                                                      
REMARK 465     THR 1     2                                                      
REMARK 465     ILE 1     3                                                      
REMARK 465     SER 1     4                                                      
REMARK 465     PRO 1     5                                                      
REMARK 465     PRO 1     6                                                      
REMARK 465     GLU 1     7                                                      
REMARK 465     ARG 1     8                                                      
REMARK 465     GLU 1     9                                                      
REMARK 465     ALA 1    10                                                      
REMARK 465     LYS 1    11                                                      
REMARK 465     ALA 1    12                                                      
REMARK 465     MET 2     1                                                      
REMARK 465     ALA 2     2                                                      
REMARK 465     GLY 2   731                                                      
REMARK 465     MET 3     1                                                      
REMARK 465     MET 4     1                                                      
REMARK 465     THR 4     2                                                      
REMARK 465     VAL 4   141                                                      
REMARK 465     MET 5     1                                                      
REMARK 465     GLN 5    70                                                      
REMARK 465     ALA 5    71                                                      
REMARK 465     ALA 5    72                                                      
REMARK 465     ALA 5    73                                                      
REMARK 465     LYS 5    74                                                      
REMARK 465     GLU 9    39                                                      
REMARK 465     GLY 9    40                                                      
REMARK 465     MET 8     1                                                      
REMARK 465     ALA 8     2                                                      
REMARK 465     GLU 8     3                                                      
REMARK 465     SER 8     4                                                      
REMARK 465     ASN 8     5                                                      
REMARK 465     GLN 8     6                                                      
REMARK 465     MET K     1                                                      
REMARK 465     THR K     2                                                      
REMARK 465     ALA K     3                                                      
REMARK 465     ILE K     4                                                      
REMARK 465     ALA K     5                                                      
REMARK 465     ARG K     6                                                      
REMARK 465     GLU K     7                                                      
REMARK 465     ARG K     8                                                      
REMARK 465     GLY K     9                                                      
REMARK 465     ARG K    10                                                      
REMARK 465     SER K    11                                                      
REMARK 465     LYS K    12                                                      
REMARK 465     ARG K    13                                                      
REMARK 465     GLY K    14                                                      
REMARK 465     ILE K    15                                                      
REMARK 465     ALA K    16                                                      
REMARK 465     LEU K    17                                                      
REMARK 465     HIS K    18                                                      
REMARK 465     ARG K    19                                                      
REMARK 465     LEU K    20                                                      
REMARK 465     GLU K    21                                                      
REMARK 465     TYR K    22                                                      
REMARK 465     LEU K    23                                                      
REMARK 465     LYS K    24                                                      
REMARK 465     GLU K    25                                                      
REMARK 465     ASN K    26                                                      
REMARK 465     GLN K    27                                                      
REMARK 465     VAL K    28                                                      
REMARK 465     PHE K    29                                                      
REMARK 465     GLU K    30                                                      
REMARK 465     ILE K    31                                                      
REMARK 465     ILE K    32                                                      
REMARK 465     PHE K    33                                                      
REMARK 465     GLY K    34                                                      
REMARK 465     GLU K    35                                                      
REMARK 465     PRO K    36                                                      
REMARK 465     LEU K    37                                                      
REMARK 465     SER K    38                                                      
REMARK 465     MET K    39                                                      
REMARK 465     PHE K    40                                                      
REMARK 465     ASN K    41                                                      
REMARK 465     THR K    42                                                      
REMARK 465     ALA K    43                                                      
REMARK 465     LEU K    44                                                      
REMARK 465     LEU K    45                                                      
REMARK 465     LEU K    46                                                      
REMARK 465     ALA K    47                                                      
REMARK 465     LEU K   128                                                      
REMARK 465     GLU I    39                                                      
REMARK 465     GLY I    40                                                      
REMARK 465     MET k     1                                                      
REMARK 465     THR k     2                                                      
REMARK 465     ALA k     3                                                      
REMARK 465     ILE k     4                                                      
REMARK 465     ALA k     5                                                      
REMARK 465     ARG k     6                                                      
REMARK 465     GLU k     7                                                      
REMARK 465     ARG k     8                                                      
REMARK 465     GLY k     9                                                      
REMARK 465     ARG k    10                                                      
REMARK 465     SER k    11                                                      
REMARK 465     LYS k    12                                                      
REMARK 465     ARG k    13                                                      
REMARK 465     GLY k    14                                                      
REMARK 465     ILE k    15                                                      
REMARK 465     ALA k    16                                                      
REMARK 465     LEU k    17                                                      
REMARK 465     HIS k    18                                                      
REMARK 465     ARG k    19                                                      
REMARK 465     LEU k    20                                                      
REMARK 465     GLU k    21                                                      
REMARK 465     TYR k    22                                                      
REMARK 465     LEU k    23                                                      
REMARK 465     LYS k    24                                                      
REMARK 465     GLU k    25                                                      
REMARK 465     ASN k    26                                                      
REMARK 465     GLN k    27                                                      
REMARK 465     VAL k    28                                                      
REMARK 465     PHE k    29                                                      
REMARK 465     GLU k    30                                                      
REMARK 465     ILE k    31                                                      
REMARK 465     ILE k    32                                                      
REMARK 465     PHE k    33                                                      
REMARK 465     GLY k    34                                                      
REMARK 465     GLU k    35                                                      
REMARK 465     PRO k    36                                                      
REMARK 465     LEU k    37                                                      
REMARK 465     SER k    38                                                      
REMARK 465     MET k    39                                                      
REMARK 465     PHE k    40                                                      
REMARK 465     ASN k    41                                                      
REMARK 465     THR k    42                                                      
REMARK 465     ALA k    43                                                      
REMARK 465     LEU k    44                                                      
REMARK 465     LEU k    45                                                      
REMARK 465     LEU k    46                                                      
REMARK 465     ALA k    47                                                      
REMARK 465     LEU k   128                                                      
REMARK 465     MET 0     1                                                      
REMARK 465     THR 0     2                                                      
REMARK 465     ALA 0     3                                                      
REMARK 465     ILE 0     4                                                      
REMARK 465     ALA 0     5                                                      
REMARK 465     ARG 0     6                                                      
REMARK 465     GLU 0     7                                                      
REMARK 465     ARG 0     8                                                      
REMARK 465     GLY 0     9                                                      
REMARK 465     ARG 0    10                                                      
REMARK 465     SER 0    11                                                      
REMARK 465     LYS 0    12                                                      
REMARK 465     ARG 0    13                                                      
REMARK 465     GLY 0    14                                                      
REMARK 465     ILE 0    15                                                      
REMARK 465     ALA 0    16                                                      
REMARK 465     LEU 0    17                                                      
REMARK 465     HIS 0    18                                                      
REMARK 465     ARG 0    19                                                      
REMARK 465     LEU 0    20                                                      
REMARK 465     GLU 0    21                                                      
REMARK 465     TYR 0    22                                                      
REMARK 465     LEU 0    23                                                      
REMARK 465     LYS 0    24                                                      
REMARK 465     GLU 0    25                                                      
REMARK 465     ASN 0    26                                                      
REMARK 465     GLN 0    27                                                      
REMARK 465     VAL 0    28                                                      
REMARK 465     PHE 0    29                                                      
REMARK 465     GLU 0    30                                                      
REMARK 465     ILE 0    31                                                      
REMARK 465     ILE 0    32                                                      
REMARK 465     PHE 0    33                                                      
REMARK 465     GLY 0    34                                                      
REMARK 465     GLU 0    35                                                      
REMARK 465     PRO 0    36                                                      
REMARK 465     LEU 0    37                                                      
REMARK 465     SER 0    38                                                      
REMARK 465     MET 0    39                                                      
REMARK 465     PHE 0    40                                                      
REMARK 465     ASN 0    41                                                      
REMARK 465     THR 0    42                                                      
REMARK 465     ALA 0    43                                                      
REMARK 465     LEU 0    44                                                      
REMARK 465     LEU 0    45                                                      
REMARK 465     LEU 0    46                                                      
REMARK 465     ALA 0    47                                                      
REMARK 465     LEU 0   128                                                      
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     GLN A 258    CG   CD   OE1  NE2                                  
REMARK 470     THR A 265    OG1  CG2                                            
REMARK 470     LEU A 266    CG   CD1  CD2                                       
REMARK 470     ASN A 267    CG   OD1  ND2                                       
REMARK 470     ASP A 273    CG   OD1  OD2                                       
REMARK 470     LYS E  30    CG   CD   CE   NZ                                   
REMARK 470     MET F   1    CG   SD   CE                                        
REMARK 470     ASP F   2    CG   OD1  OD2                                       
REMARK 470     LEU F   4    CG   CD1  CD2                                       
REMARK 470     LYS F   5    CG   CD   CE   NZ                                   
REMARK 470     PHE F   7    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU F   8    CG   CD1  CD2                                       
REMARK 470     SER F   9    OG                                                  
REMARK 470     THR F  10    OG1  CG2                                            
REMARK 470     VAL F  13    CG1  CG2                                            
REMARK 470     MET F  14    CG   SD   CE                                        
REMARK 470     ILE F  15    CG1  CG2  CD1                                       
REMARK 470     MET F  16    CG   SD   CE                                        
REMARK 470     LEU F  18    CG   CD1  CD2                                       
REMARK 470     LEU F  19    CG   CD1  CD2                                       
REMARK 470     THR F  20    OG1  CG2                                            
REMARK 470     PHE F  21    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR F  22    OG1  CG2                                            
REMARK 470     ILE F  25    CG1  CG2  CD1                                       
REMARK 470     LEU F  26    CG   CD1  CD2                                       
REMARK 470     ILE F  27    CG1  CG2  CD1                                       
REMARK 470     GLU F  28    CG   CD   OE1  OE2                                  
REMARK 470     PHE F  29    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN F  30    CG   OD1  ND2                                       
REMARK 470     ASP F  35    CG   OD1  OD2                                       
REMARK 470     LEU F  36    CG   CD1  CD2                                       
REMARK 470     LEU F  37    CG   CD1  CD2                                       
REMARK 470     PHE F  38    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS F  39    CG   ND1  CD2  CE1  NE2                             
REMARK 470     CYS F  41    SG                                                  
REMARK 470     SER F  42    OG                                                  
REMARK 470     CYS F  43    SG                                                  
REMARK 470     ASP F  46    CG   OD1  OD2                                       
REMARK 470     PHE F  47    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU F  48    CG   CD1  CD2                                       
REMARK 470     ILE F  49    CG1  CG2  CD1                                       
REMARK 470     SER F  51    OG                                                  
REMARK 470     ILE F  52    CG1  CG2  CD1                                       
REMARK 470     PHE F  54    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU F  55    CG   CD1  CD2                                       
REMARK 470     ILE F  57    CG1  CG2  CD1                                       
REMARK 470     TRP F  60    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP F  60    CZ3  CH2                                            
REMARK 470     ILE F  61    CG1  CG2  CD1                                       
REMARK 470     VAL F  64    CG1  CG2                                            
REMARK 470     ARG F  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR F  68    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU F  69    CG   CD1  CD2                                       
REMARK 470     ILE F  70    CG1  CG2  CD1                                       
REMARK 470     GLU F  71    CG   CD   OE1  OE2                                  
REMARK 470     ILE F  72    CG1  CG2  CD1                                       
REMARK 470     ARG F  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F  74    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  76    CG   CD   CE   NZ                                   
REMARK 470     ASN F  77    CG   OD1  ND2                                       
REMARK 470     GLU F  79    CG   CD   OE1  OE2                                  
REMARK 470     MET F  80    CG   SD   CE                                        
REMARK 470     GLN F  81    CG   CD   OE1  NE2                                  
REMARK 470     GLU F  82    CG   CD   OE1  OE2                                  
REMARK 470     VAL F  84    CG1  CG2                                            
REMARK 470     ILE F  85    CG1  CG2  CD1                                       
REMARK 470     ASN F  86    CG   OD1  ND2                                       
REMARK 470     VAL F  87    CG1  CG2                                            
REMARK 470     LEU F  89    CG   CD1  CD2                                       
REMARK 470     ILE F  91    CG1  CG2  CD1                                       
REMARK 470     LYS F  92    CG   CD   CE   NZ                                   
REMARK 470     LYS F  93    CG   CD   CE   NZ                                   
REMARK 470     MET F  94    CG   SD   CE                                        
REMARK 470     LEU F  95    CG   CD1  CD2                                       
REMARK 470     LEU F  99    CG   CD1  CD2                                       
REMARK 470     TRP F 100    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP F 100    CZ3  CH2                                            
REMARK 470     LEU F 102    CG   CD1  CD2                                       
REMARK 470     VAL F 105    CG1  CG2                                            
REMARK 470     GLU F 107    CG   CD   OE1  OE2                                  
REMARK 470     TYR F 108    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR F 109    OG1  CG2                                            
REMARK 470     SER F 110    OG                                                  
REMARK 470     LYS F 112    CG   CD   CE   NZ                                   
REMARK 470     LEU F 113    CG   CD1  CD2                                       
REMARK 470     VAL F 114    CG1  CG2                                            
REMARK 470     MET F 115    CG   SD   CE                                        
REMARK 470     LYS F 116    CG   CD   CE   NZ                                   
REMARK 470     ASP F 117    CG   OD1  OD2                                       
REMARK 470     SER F 118    OG                                                  
REMARK 470     GLU F 119    CG   CD   OE1  OE2                                  
REMARK 470     ILE F 120    CG1  CG2  CD1                                       
REMARK 470     THR F 122    OG1  CG2                                            
REMARK 470     SER F 123    OG                                                  
REMARK 470     ARG F 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET M   1    CG   SD   CE                                        
REMARK 470     GLN a 258    CG   CD   OE1  NE2                                  
REMARK 470     THR a 265    OG1  CG2                                            
REMARK 470     LEU a 266    CG   CD1  CD2                                       
REMARK 470     ASN a 267    CG   OD1  ND2                                       
REMARK 470     ASP a 273    CG   OD1  OD2                                       
REMARK 470     LYS e  30    CG   CD   CE   NZ                                   
REMARK 470     MET f   1    CG   SD   CE                                        
REMARK 470     ASP f   2    CG   OD1  OD2                                       
REMARK 470     LEU f   4    CG   CD1  CD2                                       
REMARK 470     LYS f   5    CG   CD   CE   NZ                                   
REMARK 470     PHE f   7    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU f   8    CG   CD1  CD2                                       
REMARK 470     SER f   9    OG                                                  
REMARK 470     THR f  10    OG1  CG2                                            
REMARK 470     VAL f  13    CG1  CG2                                            
REMARK 470     MET f  14    CG   SD   CE                                        
REMARK 470     ILE f  15    CG1  CG2  CD1                                       
REMARK 470     MET f  16    CG   SD   CE                                        
REMARK 470     LEU f  18    CG   CD1  CD2                                       
REMARK 470     LEU f  19    CG   CD1  CD2                                       
REMARK 470     THR f  20    OG1  CG2                                            
REMARK 470     PHE f  21    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR f  22    OG1  CG2                                            
REMARK 470     ILE f  25    CG1  CG2  CD1                                       
REMARK 470     LEU f  26    CG   CD1  CD2                                       
REMARK 470     ILE f  27    CG1  CG2  CD1                                       
REMARK 470     GLU f  28    CG   CD   OE1  OE2                                  
REMARK 470     PHE f  29    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN f  30    CG   OD1  ND2                                       
REMARK 470     ASP f  35    CG   OD1  OD2                                       
REMARK 470     LEU f  36    CG   CD1  CD2                                       
REMARK 470     HIS f  39    CG   ND1  CD2  CE1  NE2                             
REMARK 470     CYS f  41    SG                                                  
REMARK 470     SER f  42    OG                                                  
REMARK 470     CYS f  43    SG                                                  
REMARK 470     ASP f  46    CG   OD1  OD2                                       
REMARK 470     PHE f  47    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU f  48    CG   CD1  CD2                                       
REMARK 470     ILE f  49    CG1  CG2  CD1                                       
REMARK 470     SER f  51    OG                                                  
REMARK 470     ILE f  52    CG1  CG2  CD1                                       
REMARK 470     PHE f  54    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU f  55    CG   CD1  CD2                                       
REMARK 470     ILE f  57    CG1  CG2  CD1                                       
REMARK 470     TRP f  60    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP f  60    CZ3  CH2                                            
REMARK 470     ILE f  61    CG1  CG2  CD1                                       
REMARK 470     VAL f  64    CG1  CG2                                            
REMARK 470     ARG f  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR f  68    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU f  69    CG   CD1  CD2                                       
REMARK 470     ILE f  70    CG1  CG2  CD1                                       
REMARK 470     GLU f  71    CG   CD   OE1  OE2                                  
REMARK 470     ILE f  72    CG1  CG2  CD1                                       
REMARK 470     ARG f  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU f  74    CG   CD   OE1  OE2                                  
REMARK 470     LYS f  76    CG   CD   CE   NZ                                   
REMARK 470     ASN f  77    CG   OD1  ND2                                       
REMARK 470     GLU f  79    CG   CD   OE1  OE2                                  
REMARK 470     MET f  80    CG   SD   CE                                        
REMARK 470     GLN f  81    CG   CD   OE1  NE2                                  
REMARK 470     GLU f  82    CG   CD   OE1  OE2                                  
REMARK 470     VAL f  84    CG1  CG2                                            
REMARK 470     ILE f  85    CG1  CG2  CD1                                       
REMARK 470     ASN f  86    CG   OD1  ND2                                       
REMARK 470     VAL f  87    CG1  CG2                                            
REMARK 470     LEU f  89    CG   CD1  CD2                                       
REMARK 470     ILE f  91    CG1  CG2  CD1                                       
REMARK 470     LYS f  92    CG   CD   CE   NZ                                   
REMARK 470     LYS f  93    CG   CD   CE   NZ                                   
REMARK 470     MET f  94    CG   SD   CE                                        
REMARK 470     LEU f  95    CG   CD1  CD2                                       
REMARK 470     LEU f  99    CG   CD1  CD2                                       
REMARK 470     TRP f 100    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP f 100    CZ3  CH2                                            
REMARK 470     LEU f 102    CG   CD1  CD2                                       
REMARK 470     VAL f 105    CG1  CG2                                            
REMARK 470     GLU f 107    CG   CD   OE1  OE2                                  
REMARK 470     TYR f 108    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR f 109    OG1  CG2                                            
REMARK 470     SER f 110    OG                                                  
REMARK 470     LYS f 112    CG   CD   CE   NZ                                   
REMARK 470     LEU f 113    CG   CD1  CD2                                       
REMARK 470     VAL f 114    CG1  CG2                                            
REMARK 470     MET f 115    CG   SD   CE                                        
REMARK 470     LYS f 116    CG   CD   CE   NZ                                   
REMARK 470     ASP f 117    CG   OD1  OD2                                       
REMARK 470     SER f 118    OG                                                  
REMARK 470     GLU f 119    CG   CD   OE1  OE2                                  
REMARK 470     ILE f 120    CG1  CG2  CD1                                       
REMARK 470     THR f 122    OG1  CG2                                            
REMARK 470     SER f 123    OG                                                  
REMARK 470     ARG f 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET m   1    CG   SD   CE                                        
REMARK 470     GLN 1 258    CG   CD   OE1  NE2                                  
REMARK 470     THR 1 265    OG1  CG2                                            
REMARK 470     LEU 1 266    CG   CD1  CD2                                       
REMARK 470     ASN 1 267    CG   OD1  ND2                                       
REMARK 470     ASP 1 273    CG   OD1  OD2                                       
REMARK 470     LYS 5  30    CG   CD   CE   NZ                                   
REMARK 470     MET 6   1    CG   SD   CE                                        
REMARK 470     ASP 6   2    CG   OD1  OD2                                       
REMARK 470     LEU 6   4    CG   CD1  CD2                                       
REMARK 470     LYS 6   5    CG   CD   CE   NZ                                   
REMARK 470     PHE 6   7    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU 6   8    CG   CD1  CD2                                       
REMARK 470     SER 6   9    OG                                                  
REMARK 470     THR 6  10    OG1  CG2                                            
REMARK 470     VAL 6  13    CG1  CG2                                            
REMARK 470     MET 6  14    CG   SD   CE                                        
REMARK 470     ILE 6  15    CG1  CG2  CD1                                       
REMARK 470     MET 6  16    CG   SD   CE                                        
REMARK 470     LEU 6  18    CG   CD1  CD2                                       
REMARK 470     LEU 6  19    CG   CD1  CD2                                       
REMARK 470     THR 6  20    OG1  CG2                                            
REMARK 470     PHE 6  21    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR 6  22    OG1  CG2                                            
REMARK 470     ILE 6  25    CG1  CG2  CD1                                       
REMARK 470     LEU 6  26    CG   CD1  CD2                                       
REMARK 470     ILE 6  27    CG1  CG2  CD1                                       
REMARK 470     GLU 6  28    CG   CD   OE1  OE2                                  
REMARK 470     PHE 6  29    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN 6  30    CG   OD1  ND2                                       
REMARK 470     ASP 6  35    CG   OD1  OD2                                       
REMARK 470     LEU 6  36    CG   CD1  CD2                                       
REMARK 470     HIS 6  39    CG   ND1  CD2  CE1  NE2                             
REMARK 470     CYS 6  41    SG                                                  
REMARK 470     SER 6  42    OG                                                  
REMARK 470     CYS 6  43    SG                                                  
REMARK 470     ASP 6  46    CG   OD1  OD2                                       
REMARK 470     PHE 6  47    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU 6  48    CG   CD1  CD2                                       
REMARK 470     ILE 6  49    CG1  CG2  CD1                                       
REMARK 470     SER 6  51    OG                                                  
REMARK 470     ILE 6  52    CG1  CG2  CD1                                       
REMARK 470     PHE 6  54    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU 6  55    CG   CD1  CD2                                       
REMARK 470     ILE 6  57    CG1  CG2  CD1                                       
REMARK 470     TRP 6  60    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP 6  60    CZ3  CH2                                            
REMARK 470     ILE 6  61    CG1  CG2  CD1                                       
REMARK 470     VAL 6  64    CG1  CG2                                            
REMARK 470     ARG 6  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR 6  68    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU 6  69    CG   CD1  CD2                                       
REMARK 470     ILE 6  70    CG1  CG2  CD1                                       
REMARK 470     GLU 6  71    CG   CD   OE1  OE2                                  
REMARK 470     ILE 6  72    CG1  CG2  CD1                                       
REMARK 470     ARG 6  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU 6  74    CG   CD   OE1  OE2                                  
REMARK 470     LYS 6  76    CG   CD   CE   NZ                                   
REMARK 470     ASN 6  77    CG   OD1  ND2                                       
REMARK 470     GLU 6  79    CG   CD   OE1  OE2                                  
REMARK 470     MET 6  80    CG   SD   CE                                        
REMARK 470     GLN 6  81    CG   CD   OE1  NE2                                  
REMARK 470     GLU 6  82    CG   CD   OE1  OE2                                  
REMARK 470     VAL 6  84    CG1  CG2                                            
REMARK 470     ILE 6  85    CG1  CG2  CD1                                       
REMARK 470     ASN 6  86    CG   OD1  ND2                                       
REMARK 470     VAL 6  87    CG1  CG2                                            
REMARK 470     LEU 6  89    CG   CD1  CD2                                       
REMARK 470     ILE 6  91    CG1  CG2  CD1                                       
REMARK 470     LYS 6  92    CG   CD   CE   NZ                                   
REMARK 470     LYS 6  93    CG   CD   CE   NZ                                   
REMARK 470     MET 6  94    CG   SD   CE                                        
REMARK 470     LEU 6  95    CG   CD1  CD2                                       
REMARK 470     LEU 6  99    CG   CD1  CD2                                       
REMARK 470     TRP 6 100    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP 6 100    CZ3  CH2                                            
REMARK 470     LEU 6 102    CG   CD1  CD2                                       
REMARK 470     VAL 6 105    CG1  CG2                                            
REMARK 470     GLU 6 107    CG   CD   OE1  OE2                                  
REMARK 470     TYR 6 108    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR 6 109    OG1  CG2                                            
REMARK 470     SER 6 110    OG                                                  
REMARK 470     LYS 6 112    CG   CD   CE   NZ                                   
REMARK 470     LEU 6 113    CG   CD1  CD2                                       
REMARK 470     VAL 6 114    CG1  CG2                                            
REMARK 470     MET 6 115    CG   SD   CE                                        
REMARK 470     LYS 6 116    CG   CD   CE   NZ                                   
REMARK 470     ASP 6 117    CG   OD1  OD2                                       
REMARK 470     SER 6 118    OG                                                  
REMARK 470     GLU 6 119    CG   CD   OE1  OE2                                  
REMARK 470     ILE 6 120    CG1  CG2  CD1                                       
REMARK 470     THR 6 122    OG1  CG2                                            
REMARK 470     SER 6 123    OG                                                  
REMARK 470     ARG 6 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET 7   1    CG   SD   CE                                        
REMARK 470     GLN K  48    CG   CD   OE1  NE2                                  
REMARK 470     SER K  50    OG                                                  
REMARK 470     THR K  52    OG1  CG2                                            
REMARK 470     THR K  53    OG1  CG2                                            
REMARK 470     TRP K  56    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP K  56    CZ3  CH2                                            
REMARK 470     ILE K  79    CG1  CG2  CD1                                       
REMARK 470     GLN K  80    CG   CD   OE1  NE2                                  
REMARK 470     LYS K  81    CG   CD   CE   NZ                                   
REMARK 470     THR K  82    OG1  CG2                                            
REMARK 470     LYS K  84    CG   CD   CE   NZ                                   
REMARK 470     LYS K  86    CG   CD   CE   NZ                                   
REMARK 470     ASP K  87    CG   OD1  OD2                                       
REMARK 470     LEU K  88    CG   CD1  CD2                                       
REMARK 470     LEU K  90    CG   CD1  CD2                                       
REMARK 470     GLN K  92    CG   CD   OE1  NE2                                  
REMARK 470     LEU K  93    CG   CD1  CD2                                       
REMARK 470     SER K  95    OG                                                  
REMARK 470     LYS K  96    CG   CD   CE   NZ                                   
REMARK 470     LYS K  97    CG   CD   CE   NZ                                   
REMARK 470     THR K  98    OG1  CG2                                            
REMARK 470     PHE K  99    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU K 101    CG   CD1  CD2                                       
REMARK 470     GLU K 103    CG   CD   OE1  OE2                                  
REMARK 470     GLN k  48    CG   CD   OE1  NE2                                  
REMARK 470     SER k  50    OG                                                  
REMARK 470     THR k  52    OG1  CG2                                            
REMARK 470     THR k  53    OG1  CG2                                            
REMARK 470     TRP k  56    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP k  56    CZ3  CH2                                            
REMARK 470     ILE k  79    CG1  CG2  CD1                                       
REMARK 470     GLN k  80    CG   CD   OE1  NE2                                  
REMARK 470     LYS k  81    CG   CD   CE   NZ                                   
REMARK 470     THR k  82    OG1  CG2                                            
REMARK 470     LYS k  84    CG   CD   CE   NZ                                   
REMARK 470     LYS k  86    CG   CD   CE   NZ                                   
REMARK 470     ASP k  87    CG   OD1  OD2                                       
REMARK 470     LEU k  88    CG   CD1  CD2                                       
REMARK 470     LEU k  90    CG   CD1  CD2                                       
REMARK 470     GLN k  92    CG   CD   OE1  NE2                                  
REMARK 470     LEU k  93    CG   CD1  CD2                                       
REMARK 470     SER k  95    OG                                                  
REMARK 470     LYS k  96    CG   CD   CE   NZ                                   
REMARK 470     LYS k  97    CG   CD   CE   NZ                                   
REMARK 470     THR k  98    OG1  CG2                                            
REMARK 470     PHE k  99    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU k 101    CG   CD1  CD2                                       
REMARK 470     GLU k 103    CG   CD   OE1  OE2                                  
REMARK 470     GLN 0  48    CG   CD   OE1  NE2                                  
REMARK 470     SER 0  50    OG                                                  
REMARK 470     THR 0  52    OG1  CG2                                            
REMARK 470     THR 0  53    OG1  CG2                                            
REMARK 470     TRP 0  56    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP 0  56    CZ3  CH2                                            
REMARK 470     ILE 0  79    CG1  CG2  CD1                                       
REMARK 470     GLN 0  80    CG   CD   OE1  NE2                                  
REMARK 470     LYS 0  81    CG   CD   CE   NZ                                   
REMARK 470     THR 0  82    OG1  CG2                                            
REMARK 470     LYS 0  84    CG   CD   CE   NZ                                   
REMARK 470     LYS 0  86    CG   CD   CE   NZ                                   
REMARK 470     ASP 0  87    CG   OD1  OD2                                       
REMARK 470     LEU 0  88    CG   CD1  CD2                                       
REMARK 470     LEU 0  90    CG   CD1  CD2                                       
REMARK 470     GLN 0  92    CG   CD   OE1  NE2                                  
REMARK 470     LEU 0  93    CG   CD1  CD2                                       
REMARK 470     SER 0  95    OG                                                  
REMARK 470     LYS 0  96    CG   CD   CE   NZ                                   
REMARK 470     LYS 0  97    CG   CD   CE   NZ                                   
REMARK 470     THR 0  98    OG1  CG2                                            
REMARK 470     PHE 0  99    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU 0 101    CG   CD1  CD2                                       
REMARK 470     GLU 0 103    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS 3    21    FE2   SF4 3  3002              0.59            
REMARK 500   SG   CYS C    21    FE2   SF4 C  3002              0.60            
REMARK 500   SG   CYS c    21    FE2   SF4 c  3002              0.65            
REMARK 500   SG   CYS C    48    FE4   SF4 C  3002              0.75            
REMARK 500   SG   CYS C    11    FE3   SF4 C  3003              0.82            
REMARK 500   SG   CYS 3    48    FE4   SF4 3  3002              0.87            
REMARK 500   SG   CYS 3    11    FE3   SF4 3  3003              0.88            
REMARK 500   SG   CYS c    58    FE1   SF4 c  3003              0.94            
REMARK 500   SG   CYS c    11    FE3   SF4 c  3003              0.96            
REMARK 500   SG   CYS c    48    FE4   SF4 c  3002              1.05            
REMARK 500   SG   CYS C    58    FE1   SF4 C  3003              1.08            
REMARK 500   SG   CYS c    14    FE2   SF4 c  3003              1.10            
REMARK 500   SG   CYS C    54    FE3   SF4 C  3002              1.22            
REMARK 500   SG   CYS 3    58    FE1   SF4 3  3003              1.23            
REMARK 500   SG   CYS 3    14    FE2   SF4 3  3003              1.29            
REMARK 500   SG   CYS C    14    FE2   SF4 C  3003              1.31            
REMARK 500   SG   CYS 3    51    FE1   SF4 3  3002              1.45            
REMARK 500   SG   CYS 2   565    FE3   SF4 1  3001              1.57            
REMARK 500   SG   CYS B   565    FE3   SF4 A  3001              1.58            
REMARK 500   SG   CYS c    51    FE1   SF4 c  3002              1.63            
REMARK 500   SG   CYS 3    17    FE4   SF4 3  3003              1.71            
REMARK 500   SG   CYS A   583    FE2   SF4 A  3001              1.75            
REMARK 500   SG   CYS a   574    FE4   SF4 a  3001              1.90            
REMARK 500   SG   CYS C    58     S3   SF4 C  3003              2.05            
REMARK 500   CG   HIS a    56     CBB  CLA a  1103              2.07            
REMARK 500   CB   CYS B   565    FE3   SF4 A  3001              2.12            
REMARK 500   SG   CYS C    11     S2   SF4 C  3003              2.17            
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    GLN A 115      101.79     62.39                                   
REMARK 500    TYR A 180      -17.79   -148.61                                   
REMARK 500    VAL A 182      -59.08   -125.59                                   
REMARK 500    ALA A 232      143.88     72.67                                   
REMARK 500    TYR A 253       87.14     62.38                                   
REMARK 500    SER A 255       33.13    -77.64                                   
REMARK 500    THR A 261      -30.13    103.53                                   
REMARK 500    TRP A 268      -63.29     62.01                                   
REMARK 500    LEU A 275       76.76   -112.79                                   
REMARK 500    PHE A 277       43.87   -141.13                                   
REMARK 500    THR A 313     -147.99   -140.86                                   
REMARK 500    TYR A 378       18.81     59.64                                   
REMARK 500    HIS A 432       30.18   -140.55                                   
REMARK 500    SER A 451      -65.79   -123.41                                   
REMARK 500    ALA A 475     -134.46    -92.87                                   
REMARK 500    ALA A 496      -83.49   -149.62                                   
REMARK 500    ALA A 517     -116.14     56.11                                   
REMARK 500    CYS A 574     -175.41   -173.14                                   
REMARK 500    VAL A 617      -69.31   -138.71                                   
REMARK 500    LEU A 733      -71.92    -62.58                                   
REMARK 500    PHE B   5     -177.51    -63.41                                   
REMARK 500    PRO B   6       85.36     17.33                                   
REMARK 500    ASN B  73       47.48    -96.03                                   
REMARK 500    ASP B  80       61.05   -151.80                                   
REMARK 500    VAL B 197      -64.81   -129.68                                   
REMARK 500    ASN B 211       15.79   -141.40                                   
REMARK 500    LEU B 222      -51.75     73.93                                   
REMARK 500    ALA B 235      -77.29    -63.85                                   
REMARK 500    PHE B 257       51.47   -143.54                                   
REMARK 500    THR B 293     -153.19   -146.43                                   
REMARK 500    PRO B 455       63.73    -65.20                                   
REMARK 500    LEU B 475     -107.61     56.97                                   
REMARK 500    THR B 485       34.18    -98.72                                   
REMARK 500    ALA B 488      -85.18     45.90                                   
REMARK 500    ALA B 489      -68.64     55.28                                   
REMARK 500    MET B 544       75.00   -154.32                                   
REMARK 500    CYS B 556     -148.02   -179.97                                   
REMARK 500    ASP B 557       32.93   -150.65                                   
REMARK 500    ASN B 602       65.94   -108.47                                   
REMARK 500    PRO B 634       -6.16    -58.90                                   
REMARK 500    ILE B 662      -61.78    -92.08                                   
REMARK 500    LEU B 684      -31.50     70.14                                   
REMARK 500    ARG D  24      -61.24   -105.72                                   
REMARK 500    GLU D  25      -67.77    -96.69                                   
REMARK 500    THR D  74      -16.59   -140.59                                   
REMARK 500    LYS D  79      104.24    -59.72                                   
REMARK 500    LEU D  97      -58.62   -133.83                                   
REMARK 500    PRO D  99       68.56     18.36                                   
REMARK 500    ALA D 100      -70.33    -48.16                                   
REMARK 500    ARG D 120      148.15   -173.75                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     238 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE B    5     PRO B    6                 -136.44                    
REMARK 500 HIS D   98     PRO D   99                 -138.82                    
REMARK 500 PHE b    5     PRO b    6                 -136.34                    
REMARK 500 HIS d   98     PRO d   99                 -139.93                    
REMARK 500 PHE 2    5     PRO 2    6                 -135.84                    
REMARK 500 HIS 4   98     PRO 4   99                 -139.38                    
REMARK 500 SER k  125     GLY k  126                 -145.38                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PRO F  40        -10.27                                           
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     CLA A 1801                                                       
REMARK 610     CLA A 1237                                                       
REMARK 610     CLA A 1105                                                       
REMARK 610     CLA A 1108                                                       
REMARK 610     CLA A 1110                                                       
REMARK 610     CLA A 1111                                                       
REMARK 610     CLA A 1112                                                       
REMARK 610     CLA A 1113                                                       
REMARK 610     CLA A 1115                                                       
REMARK 610     CLA A 1116                                                       
REMARK 610     CLA A 1118                                                       
REMARK 610     CLA A 1122                                                       
REMARK 610     CLA A 1124                                                       
REMARK 610     CLA A 1125                                                       
REMARK 610     CLA A 1130                                                       
REMARK 610     CLA A 1138                                                       
REMARK 610     CLA A 1139                                                       
REMARK 610     CLA A 1114                                                       
REMARK 610     CLA A 1120                                                       
REMARK 610     CLA A 1121                                                       
REMARK 610     CLA A 1129                                                       
REMARK 610     CLA A 1133                                                       
REMARK 610     CLA A 1134                                                       
REMARK 610     CLA A 1135                                                       
REMARK 610     CLA A 1136                                                       
REMARK 610     CLA B 1201                                                       
REMARK 610     CLA B 1205                                                       
REMARK 610     CLA B 1208                                                       
REMARK 610     CLA B 1209                                                       
REMARK 610     CLA B 1212                                                       
REMARK 610     CLA B 1214                                                       
REMARK 610     CLA B 1217                                                       
REMARK 610     CLA B 1218                                                       
REMARK 610     CLA B 1219                                                       
REMARK 610     CLA B 1220                                                       
REMARK 610     CLA B 1221                                                       
REMARK 610     CLA B 1222                                                       
REMARK 610     CLA B 1224                                                       
REMARK 610     CLA B 1227                                                       
REMARK 610     CLA B 1228                                                       
REMARK 610     CLA B 1230                                                       
REMARK 610     CLA B 1231                                                       
REMARK 610     CLA B 1232                                                       
REMARK 610     CLA B 1234                                                       
REMARK 610     CLA B 1235                                                       
REMARK 610     CLA B 1236                                                       
REMARK 610     CLA B 1240                                                       
REMARK 610     CLA B 1211                                                       
REMARK 610     CLA B 1239                                                       
REMARK 610     CLA L 1502                                                       
REMARK 610     CLA a 1801                                                       
REMARK 610     CLA a 1237                                                       
REMARK 610     CLA a 1105                                                       
REMARK 610     CLA a 1108                                                       
REMARK 610     CLA a 1110                                                       
REMARK 610     CLA a 1111                                                       
REMARK 610     CLA a 1112                                                       
REMARK 610     CLA a 1113                                                       
REMARK 610     CLA a 1115                                                       
REMARK 610     CLA a 1116                                                       
REMARK 610     CLA a 1118                                                       
REMARK 610     CLA a 1122                                                       
REMARK 610     CLA a 1124                                                       
REMARK 610     CLA a 1125                                                       
REMARK 610     CLA a 1130                                                       
REMARK 610     CLA a 1138                                                       
REMARK 610     CLA a 1139                                                       
REMARK 610     CLA a 1114                                                       
REMARK 610     CLA a 1120                                                       
REMARK 610     CLA a 1121                                                       
REMARK 610     CLA a 1129                                                       
REMARK 610     CLA a 1133                                                       
REMARK 610     CLA a 1134                                                       
REMARK 610     CLA a 1135                                                       
REMARK 610     CLA a 1136                                                       
REMARK 610     CLA b 1201                                                       
REMARK 610     CLA b 1205                                                       
REMARK 610     CLA b 1208                                                       
REMARK 610     CLA b 1209                                                       
REMARK 610     CLA b 1212                                                       
REMARK 610     CLA b 1214                                                       
REMARK 610     CLA b 1217                                                       
REMARK 610     CLA b 1218                                                       
REMARK 610     CLA b 1219                                                       
REMARK 610     CLA b 1220                                                       
REMARK 610     CLA b 1221                                                       
REMARK 610     CLA b 1222                                                       
REMARK 610     CLA b 1224                                                       
REMARK 610     CLA b 1227                                                       
REMARK 610     CLA b 1228                                                       
REMARK 610     CLA b 1230                                                       
REMARK 610     CLA b 1231                                                       
REMARK 610     CLA b 1232                                                       
REMARK 610     CLA b 1234                                                       
REMARK 610     CLA b 1235                                                       
REMARK 610     CLA b 1236                                                       
REMARK 610     CLA b 1240                                                       
REMARK 610     CLA b 1211                                                       
REMARK 610     CLA b 1239                                                       
REMARK 610     CLA l 1502                                                       
REMARK 610     CLA 1 1801                                                       
REMARK 610     CLA 1 1237                                                       
REMARK 610     CLA 1 1105                                                       
REMARK 610     CLA 1 1108                                                       
REMARK 610     CLA 1 1110                                                       
REMARK 610     CLA 1 1111                                                       
REMARK 610     CLA 1 1112                                                       
REMARK 610     CLA 1 1113                                                       
REMARK 610     CLA 1 1115                                                       
REMARK 610     CLA 1 1116                                                       
REMARK 610     CLA 1 1118                                                       
REMARK 610     CLA 1 1122                                                       
REMARK 610     CLA 1 1124                                                       
REMARK 610     CLA 1 1125                                                       
REMARK 610     CLA 1 1130                                                       
REMARK 610     CLA 1 1138                                                       
REMARK 610     CLA 1 1139                                                       
REMARK 610     CLA 1 1114                                                       
REMARK 610     CLA 1 1120                                                       
REMARK 610     CLA 1 1121                                                       
REMARK 610     CLA 1 1129                                                       
REMARK 610     CLA 1 1133                                                       
REMARK 610     CLA 1 1134                                                       
REMARK 610     CLA 1 1135                                                       
REMARK 610     CLA 1 1136                                                       
REMARK 610     CLA 2 1201                                                       
REMARK 610     CLA 2 1205                                                       
REMARK 610     CLA 2 1208                                                       
REMARK 610     CLA 2 1209                                                       
REMARK 610     CLA 2 1212                                                       
REMARK 610     CLA 2 1214                                                       
REMARK 610     CLA 2 1217                                                       
REMARK 610     CLA 2 1218                                                       
REMARK 610     CLA 2 1219                                                       
REMARK 610     CLA 2 1220                                                       
REMARK 610     CLA 2 1221                                                       
REMARK 610     CLA 2 1222                                                       
REMARK 610     CLA 2 1224                                                       
REMARK 610     CLA 2 1227                                                       
REMARK 610     CLA 2 1228                                                       
REMARK 610     CLA 2 1230                                                       
REMARK 610     CLA 2 1231                                                       
REMARK 610     CLA 2 1232                                                       
REMARK 610     CLA 2 1234                                                       
REMARK 610     CLA 2 1235                                                       
REMARK 610     CLA 2 1236                                                       
REMARK 610     CLA 2 1240                                                       
REMARK 610     CLA 2 1211                                                       
REMARK 610     CLA 2 1239                                                       
REMARK 610     CLA 8 1502                                                       
REMARK 610     CLA K 1402                                                       
REMARK 610     CLA k 1402                                                       
REMARK 610     CLA 0 1402                                                       
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                             SF4 13001  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 1 574   SG                                                     
REMARK 620 2 SF4 13001   S1  106.7                                              
REMARK 620 3 SF4 13001   S2  147.0  67.9                                        
REMARK 620 4 SF4 13001   S3   78.8  68.7  68.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3003  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  17   SG                                                     
REMARK 620 2 SF4 C3003   S1  131.1                                              
REMARK 620 3 SF4 C3003   S2  152.7  67.8                                        
REMARK 620 4 SF4 C3003   S3  132.8  68.7  68.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 a3001  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS b 565   SG                                                     
REMARK 620 2 SF4 a3001   S1   84.0                                              
REMARK 620 3 SF4 a3001   S2  108.3  67.9                                        
REMARK 620 4 SF4 a3001   S4  150.9  67.5  67.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A3001  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 556   SG                                                     
REMARK 620 2 SF4 A3001   S2   90.2                                              
REMARK 620 3 SF4 A3001   S3  156.7  68.8                                        
REMARK 620 4 SF4 A3001   S4   94.8  67.7  68.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 13001  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 2 556   SG                                                     
REMARK 620 2 SF4 13001   S2   94.1                                              
REMARK 620 3 SF4 13001   S3  161.4  68.8                                        
REMARK 620 4 SF4 13001   S4   98.9  67.8  68.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3002  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  51   SG                                                     
REMARK 620 2 SF4 C3002   S2  148.4                                              
REMARK 620 3 SF4 C3002   S3  143.1  68.0                                        
REMARK 620 4 SF4 C3002   S4  120.6  68.1  68.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 33002  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 3  54   SG                                                     
REMARK 620 2 SF4 33002   S1  102.4                                              
REMARK 620 3 SF4 33002   S2  148.5  67.8                                        
REMARK 620 4 SF4 33002   S4   80.5  68.3  68.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A3001  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 574   SG                                                     
REMARK 620 2 SF4 A3001   S1  103.7                                              
REMARK 620 3 SF4 A3001   S2  151.9  67.9                                        
REMARK 620 4 SF4 A3001   S3   83.1  68.7  68.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 c3003  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS c  17   SG                                                     
REMARK 620 2 SF4 c3003   S1  124.9                                              
REMARK 620 3 SF4 c3003   S2  149.2  67.8                                        
REMARK 620 4 SF4 c3003   S3  140.5  68.7  68.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 a3001  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS a 583   SG                                                     
REMARK 620 2 SF4 a3001   S1  170.0                                              
REMARK 620 3 SF4 a3001   S3  103.8  68.7                                        
REMARK 620 4 SF4 a3001   S4  103.9  67.5  68.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 13001  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 1 583   SG                                                     
REMARK 620 2 SF4 13001   S1  169.1                                              
REMARK 620 3 SF4 13001   S3  100.8  68.7                                        
REMARK 620 4 SF4 13001   S4  106.4  67.5  68.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 a3001  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS b 556   SG                                                     
REMARK 620 2 SF4 a3001   S2   99.3                                              
REMARK 620 3 SF4 a3001   S3  166.8  68.8                                        
REMARK 620 4 SF4 a3001   S4  102.2  67.8  68.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 c3002  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS c  54   SG                                                     
REMARK 620 2 SF4 c3002   S1   98.4                                              
REMARK 620 3 SF4 c3002   S2  145.9  67.8                                        
REMARK 620 4 SF4 c3002   S4   77.9  68.3  68.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a1106  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN a 115   OE1                                                    
REMARK 620 2 CLA a1106   NA   86.3                                              
REMARK 620 3 CLA a1106   NB  107.8  87.9                                        
REMARK 620 4 CLA a1106   NC  107.4 164.4  94.9                                  
REMARK 620 5 CLA a1106   ND   88.2  90.8 163.8  82.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1106  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 115   OE1                                                    
REMARK 620 2 CLA A1106   NA   86.0                                              
REMARK 620 3 CLA A1106   NB  100.8  86.9                                        
REMARK 620 4 CLA A1106   NC  108.7 164.4  95.3                                  
REMARK 620 5 CLA A1106   ND   96.4  91.4 162.5  81.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 11106  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN 1 115   OE1                                                    
REMARK 620 2 CLA 11106   NA   88.4                                              
REMARK 620 3 CLA 11106   NB  111.9  87.7                                        
REMARK 620 4 CLA 11106   NC  105.7 163.6  94.6                                  
REMARK 620 5 CLA 11106   ND   85.1  91.0 162.9  82.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA l1501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU l  52   OE2                                                    
REMARK 620 2 CLA l1501   NA   98.1                                              
REMARK 620 3 CLA l1501   NB  110.4  87.7                                        
REMARK 620 4 CLA l1501   NC   96.1 163.9  94.6                                  
REMARK 620 5 CLA l1501   ND   86.5  91.1 163.1  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1240  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LHG B5004   O5                                                     
REMARK 620 2 CLA B1240   NA  104.0                                              
REMARK 620 3 CLA B1240   NB  105.1  87.9                                        
REMARK 620 4 CLA B1240   NC   90.6 164.1  94.5                                  
REMARK 620 5 CLA B1240   ND   90.8  91.1 163.8  82.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  93   OD2                                                    
REMARK 620 2 CLA B1206   NA   92.8                                              
REMARK 620 3 CLA B1206   NB   93.0  87.6                                        
REMARK 620 4 CLA B1206   NC  103.0 163.9  94.6                                  
REMARK 620 5 CLA B1206   ND  103.6  91.6 163.4  81.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 21206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP 2  93   OD2                                                    
REMARK 620 2 CLA 21206   NA   96.0                                              
REMARK 620 3 CLA 21206   NB   90.9  87.7                                        
REMARK 620 4 CLA 21206   NC   99.5 164.3  94.4                                  
REMARK 620 5 CLA 21206   ND  106.1  91.5 162.9  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a1109  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CLA a1102   O1A                                                    
REMARK 620 2 CLA a1109   NA   74.1                                              
REMARK 620 3 CLA a1109   NB   78.0  87.2                                        
REMARK 620 4 CLA a1109   NC   91.5 164.7  94.9                                  
REMARK 620 5 CLA a1109   ND   83.8  91.1 161.5  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1107  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 123   OE1                                                    
REMARK 620 2 CLA A1107   NA   80.9                                              
REMARK 620 3 CLA A1107   NB   75.2  88.1                                        
REMARK 620 4 CLA A1107   NC   83.6 162.9  94.8                                  
REMARK 620 5 CLA A1107   ND   87.9  91.1 162.9  81.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1801  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LHG A5003   O5                                                     
REMARK 620 2 CLA A1801   NA   97.3                                              
REMARK 620 3 CLA A1801   NB  108.6  87.0                                        
REMARK 620 4 CLA A1801   NC   97.5 163.5  95.1                                  
REMARK 620 5 CLA A1801   ND   88.8  91.4 162.6  81.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a1801  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LHG a5003   O5                                                     
REMARK 620 2 CLA a1801   NA   71.3                                              
REMARK 620 3 CLA a1801   NB   93.6  87.3                                        
REMARK 620 4 CLA a1801   NC  124.6 163.6  94.7                                  
REMARK 620 5 CLA a1801   ND  102.7  91.2 162.2  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 11801  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LHG 15003   O5                                                     
REMARK 620 2 CLA 11801   NA   87.9                                              
REMARK 620 3 CLA 11801   NB  103.5  87.7                                        
REMARK 620 4 CLA 11801   NC  106.8 164.1  94.4                                  
REMARK 620 5 CLA 11801   ND   93.8  91.2 162.6  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA L1501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU L  52   OE2                                                    
REMARK 620 2 CLA L1501   NA  107.5                                              
REMARK 620 3 CLA L1501   NB  111.1  87.5                                        
REMARK 620 4 CLA L1501   NC   87.7 162.9  94.4                                  
REMARK 620 5 CLA L1501   ND   85.4  91.3 163.0  81.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP b  93   OD2                                                    
REMARK 620 2 CLA b1206   NA   98.0                                              
REMARK 620 3 CLA b1206   NB   97.6  87.6                                        
REMARK 620 4 CLA b1206   NC   97.1 164.3  94.6                                  
REMARK 620 5 CLA b1206   ND   99.6  91.3 162.8  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a1107  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN a 123   OE1                                                    
REMARK 620 2 CLA a1107   NA   83.7                                              
REMARK 620 3 CLA a1107   NB   81.1  88.7                                        
REMARK 620 4 CLA a1107   NC   81.1 163.7  94.6                                  
REMARK 620 5 CLA a1107   ND   82.4  90.8 163.4  81.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1109  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CLA A1102   O1A                                                    
REMARK 620 2 CLA A1109   NA   72.6                                              
REMARK 620 3 CLA A1109   NB   82.3  87.6                                        
REMARK 620 4 CLA A1109   NC   92.9 164.9  94.8                                  
REMARK 620 5 CLA A1109   ND   80.5  90.9 162.4  82.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1134  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 497   O                                                      
REMARK 620 2 CLA A1134   NA   78.7                                              
REMARK 620 3 CLA A1134   NB   86.2  88.0                                        
REMARK 620 4 CLA A1134   NC   85.4 163.6  95.0                                  
REMARK 620 5 CLA A1134   ND   77.0  91.2 163.0  81.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 21240  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LHG 25004   O5                                                     
REMARK 620 2 CLA 21240   NA  125.8                                              
REMARK 620 3 CLA 21240   NB   95.4  87.4                                        
REMARK 620 4 CLA 21240   NC   70.4 163.4  94.8                                  
REMARK 620 5 CLA 21240   ND   99.1  91.4 162.8  81.7                            
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 CLA A 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQN A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 5003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1237                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1108                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1109                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1111                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1112                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1113                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1115                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1116                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1117                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1118                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1119                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1122                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1123                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1124                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1125                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1126                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1127                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1128                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1131                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1137                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1138                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1139                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1140                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1114                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1120                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1121                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1129                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1132                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1133                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1134                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1135                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1136                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQN B 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG B 5004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1215                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1217                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1220                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1221                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1222                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1223                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1224                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1225                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1226                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1227                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1228                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1229                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1230                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1231                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1232                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1234                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1235                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1236                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1240                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1238                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1239                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR F 4018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR F 4020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR F 4013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR L 4019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR L 4022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR M 4021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQN a 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 a 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 4003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 4007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 4008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG a 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG a 5003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1237                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1108                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1109                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1111                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1112                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1113                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1115                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1116                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1117                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1118                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1119                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1122                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1123                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1124                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1125                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1126                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1127                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1128                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1131                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1137                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1138                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1139                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1140                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1114                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1120                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1121                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1129                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1132                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1133                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1134                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1135                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 1136                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQN b 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 4004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 4009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 4010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 4011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 4014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 4017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG b 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG b 5004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1215                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1217                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1220                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1221                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1222                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1223                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1224                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1225                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1226                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1227                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1228                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1229                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1230                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1231                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1232                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1234                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: YC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1235                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: YC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1236                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: YC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1240                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: YC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: YC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: YC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1238                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: YC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 1239                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: YC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 c 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: YC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 c 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR f 4018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR f 4020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR f 4013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA l 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA l 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA l 1503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR l 4019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR l 4022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR m 4021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQN 1 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 1 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 1 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 1 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 1 4003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 1 4007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 1 4008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG 1 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG 1 5003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1237                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1108                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1109                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1111                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1112                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1113                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1115                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1116                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1117                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1118                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1119                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1122                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1123                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1124                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1125                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1126                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1127                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ED1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1128                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ED2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ED3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1131                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ED4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1137                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ED5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1138                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ED6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1139                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ED7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1140                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ED8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ED9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1114                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1120                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1121                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1129                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1132                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1133                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1134                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1135                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1136                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQN 2 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 2 4004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 2 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 2 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 2 4009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 2 4010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 2 4011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 2 4014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 2 4017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG 2 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG 2 5004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ID1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ID2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ID3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ID4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ID5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ID6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ID7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ID8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ID9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1215                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1217                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1220                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1221                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1222                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1223                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1224                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1225                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1226                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1227                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1228                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1229                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1230                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1231                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1232                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1234                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1235                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1236                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1240                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1238                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 1239                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 3 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 3 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 6 4018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 6 4020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 6 4013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 8 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 8 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 8 1503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 8 4019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 8 4022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 7 4021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ND1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ND2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 1402                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ND3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA k 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ND4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA k 1402                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ND5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 0 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ND6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 0 1402                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JB0   RELATED DB: PDB                                   
REMARK 900 PHOTOSYNTHETIC REACTION CENTER AND CORE ANTENNA SYSTEM FROM          
REMARK 900 CYANOBACTERIA                                                        
REMARK 900 RELATED ID: 3LW5   RELATED DB: PDB                                   
REMARK 900 IMPROVED MODEL OF PLANT PHOTOSYSTEM I                                
REMARK 900 RELATED ID: 4KT0   RELATED DB: PDB                                   
DBREF  4L6V A    1   751  UNP    L8AHT3   L8AHT3_9SYNC     1    751             
DBREF  4L6V B    1   731  UNP    L8AIC0   L8AIC0_9SYNC     1    731             
DBREF  4L6V C    1    81  UNP    L8AST2   L8AST2_9SYNC     1     81             
DBREF  4L6V D    1   141  UNP    L8AFM8   L8AFM8_9SYNC     1    141             
DBREF  4L6V E    1    74  UNP    L8ASH8   L8ASH8_9SYNC     1     74             
DBREF  4L6V F   44   125  UNP    L8AII8   L8AII8_9SYNC   103    184             
DBREF  4L6V L    1   157  UNP    L8APN7   L8APN7_9SYNC     1    157             
DBREF  4L6V M    1    31  UNP    L8ADF9   L8ADF9_9SYNC     1     31             
DBREF  4L6V a    1   751  UNP    L8AHT3   L8AHT3_9SYNC     1    751             
DBREF  4L6V b    1   731  UNP    L8AIC0   L8AIC0_9SYNC     1    731             
DBREF  4L6V c    1    81  UNP    L8AST2   L8AST2_9SYNC     1     81             
DBREF  4L6V d    1   141  UNP    L8AFM8   L8AFM8_9SYNC     1    141             
DBREF  4L6V e    1    74  UNP    L8ASH8   L8ASH8_9SYNC     1     74             
DBREF  4L6V f   44   125  UNP    L8AII8   L8AII8_9SYNC   103    184             
DBREF  4L6V i    1    40  UNP    L8AP84   L8AP84_9SYNC     1     40             
DBREF  4L6V l    1   157  UNP    L8APN7   L8APN7_9SYNC     1    157             
DBREF  4L6V m    1    31  UNP    L8ADF9   L8ADF9_9SYNC     1     31             
DBREF  4L6V 1    1   751  UNP    L8AHT3   L8AHT3_9SYNC     1    751             
DBREF  4L6V 2    1   731  UNP    L8AIC0   L8AIC0_9SYNC     1    731             
DBREF  4L6V 3    1    81  UNP    L8AST2   L8AST2_9SYNC     1     81             
DBREF  4L6V 4    1   141  UNP    L8AFM8   L8AFM8_9SYNC     1    141             
DBREF  4L6V 5    1    74  UNP    L8ASH8   L8ASH8_9SYNC     1     74             
DBREF  4L6V 6   44   125  UNP    L8AII8   L8AII8_9SYNC   103    184             
DBREF  4L6V 9    1    40  UNP    L8AP84   L8AP84_9SYNC     1     40             
DBREF  4L6V 8    1   157  UNP    L8APN7   L8APN7_9SYNC     1    157             
DBREF  4L6V 7    1    31  UNP    L8ADF9   L8ADF9_9SYNC     1     31             
DBREF  4L6V K    1   128  UNP    L8APJ0   L8APJ0_9SYNC     1    128             
DBREF  4L6V I    1    40  UNP    L8AP84   L8AP84_9SYNC     1     40             
DBREF  4L6V k    1   128  UNP    L8APJ0   L8APJ0_9SYNC     1    128             
DBREF  4L6V 0    1   128  UNP    L8APJ0   L8APJ0_9SYNC     1    128             
DBREF  4L6V F    1    40  UNP    Q55329   PSAJ_SYNY3       1     40             
DBREF  4L6V f    1    40  UNP    Q55329   PSAJ_SYNY3       1     40             
DBREF  4L6V 6    1    40  UNP    Q55329   PSAJ_SYNY3       1     40             
SEQADV 4L6V CYS F   41  UNP  L8AII8              LINKER                         
SEQADV 4L6V SER F   42  UNP  L8AII8              LINKER                         
SEQADV 4L6V CYS F   43  UNP  L8AII8              LINKER                         
SEQADV 4L6V ILE F   53  UNP  L8AII8    LEU   112 ENGINEERED MUTATION            
SEQADV 4L6V CYS f   41  UNP  L8AII8              LINKER                         
SEQADV 4L6V SER f   42  UNP  L8AII8              LINKER                         
SEQADV 4L6V CYS f   43  UNP  L8AII8              LINKER                         
SEQADV 4L6V ILE f   53  UNP  L8AII8    LEU   112 ENGINEERED MUTATION            
SEQADV 4L6V CYS 6   41  UNP  L8AII8              LINKER                         
SEQADV 4L6V SER 6   42  UNP  L8AII8              LINKER                         
SEQADV 4L6V CYS 6   43  UNP  L8AII8              LINKER                         
SEQADV 4L6V ILE 6   53  UNP  L8AII8    LEU   112 ENGINEERED MUTATION            
SEQRES   1 A  751  MET THR ILE SER PRO PRO GLU ARG GLU ALA LYS ALA LYS          
SEQRES   2 A  751  VAL SER VAL ASP ASN ASN PRO VAL PRO THR SER PHE GLU          
SEQRES   3 A  751  LYS TRP GLY LYS PRO GLY HIS PHE ASP ARG THR LEU ALA          
SEQRES   4 A  751  ARG GLY PRO LYS THR THR THR TRP ILE TRP ASN LEU HIS          
SEQRES   5 A  751  ALA ASN ALA HIS ASP PHE ASP SER GLN THR SER ASP LEU          
SEQRES   6 A  751  GLU ASP VAL SER ARG LYS ILE PHE SER ALA HIS PHE GLY          
SEQRES   7 A  751  HIS LEU ALA VAL VAL PHE VAL TRP LEU SER GLY MET TYR          
SEQRES   8 A  751  PHE HIS GLY ALA LYS PHE SER ASN TYR GLU GLY TRP LEU          
SEQRES   9 A  751  ALA ASP PRO THR HIS ILE LYS PRO SER ALA GLN VAL VAL          
SEQRES  10 A  751  TRP PRO ILE VAL GLY GLN GLY ILE LEU ASN GLY ASP VAL          
SEQRES  11 A  751  GLY GLY GLY PHE HIS GLY ILE GLN ILE THR SER GLY LEU          
SEQRES  12 A  751  PHE TYR LEU TRP ARG ALA SER GLY PHE THR ASP SER TYR          
SEQRES  13 A  751  GLN LEU TYR CYS THR ALA ILE GLY GLY LEU VAL MET ALA          
SEQRES  14 A  751  ALA LEU MET LEU PHE ALA GLY TRP PHE HIS TYR HIS VAL          
SEQRES  15 A  751  LYS ALA PRO LYS LEU GLU TRP PHE GLN ASN VAL GLU SER          
SEQRES  16 A  751  MET MET ASN HIS HIS LEU ALA GLY LEU LEU GLY LEU GLY          
SEQRES  17 A  751  SER LEU GLY TRP ALA GLY HIS GLN ILE HIS VAL SER MET          
SEQRES  18 A  751  PRO ILE ASN LYS LEU LEU ASP ALA GLY VAL ALA PRO LYS          
SEQRES  19 A  751  ASP ILE PRO LEU PRO HIS GLU PHE ILE LEU GLU PRO SER          
SEQRES  20 A  751  LYS MET ALA GLU LEU TYR PRO SER PHE ALA GLN GLY LEU          
SEQRES  21 A  751  THR PRO PHE PHE THR LEU ASN TRP GLY VAL TYR SER ASP          
SEQRES  22 A  751  PHE LEU THR PHE LYS GLY GLY LEU ASN PRO VAL THR GLY          
SEQRES  23 A  751  GLY LEU TRP LEU SER ASP THR ALA HIS HIS HIS LEU ALA          
SEQRES  24 A  751  ILE ALA VAL LEU PHE ILE ILE ALA GLY HIS MET TYR ARG          
SEQRES  25 A  751  THR ASN TRP GLY ILE GLY HIS SER MET LYS GLU ILE LEU          
SEQRES  26 A  751  GLU ALA HIS LYS GLY PRO PHE THR GLY GLU GLY HIS LYS          
SEQRES  27 A  751  GLY LEU TYR GLU ILE LEU THR THR SER TRP HIS ALA GLN          
SEQRES  28 A  751  LEU ALA ILE ASN LEU ALA LEU LEU GLY SER LEU THR ILE          
SEQRES  29 A  751  ILE VAL ALA GLN HIS MET TYR ALA MET PRO PRO TYR PRO          
SEQRES  30 A  751  TYR GLN ALA ILE ASP TYR ALA THR GLN LEU SER LEU PHE          
SEQRES  31 A  751  THR HIS HIS MET TRP ILE GLY GLY PHE LEU ILE VAL GLY          
SEQRES  32 A  751  ALA GLY ALA HIS GLY ALA ILE PHE MET VAL ARG ASP TYR          
SEQRES  33 A  751  ASP PRO ALA LYS ASN VAL ASN ASN LEU LEU ASP ARG MET          
SEQRES  34 A  751  LEU ARG HIS ARG ASP ALA ILE ILE SER HIS LEU ASN TRP          
SEQRES  35 A  751  VAL CYS ILE PHE LEU GLY PHE HIS SER PHE GLY LEU TYR          
SEQRES  36 A  751  ILE HIS ASN ASP THR MET ARG ALA LEU GLY ARG PRO GLN          
SEQRES  37 A  751  ASP MET PHE SER ASP THR ALA ILE GLN LEU GLN PRO ILE          
SEQRES  38 A  751  PHE ALA GLN TRP VAL GLN HIS LEU HIS THR LEU ALA PRO          
SEQRES  39 A  751  GLY ALA THR ALA PRO ASN ALA LEU ALA THR ALA SER TYR          
SEQRES  40 A  751  ALA PHE GLY GLY GLU THR ILE ALA VAL ALA GLY LYS VAL          
SEQRES  41 A  751  ALA MET MET PRO ILE THR LEU GLY THR ALA ASP PHE MET          
SEQRES  42 A  751  VAL HIS HIS ILE HIS ALA PHE THR ILE HIS VAL THR ALA          
SEQRES  43 A  751  LEU ILE LEU LEU LYS GLY VAL LEU TYR ALA ARG SER SER          
SEQRES  44 A  751  ARG LEU VAL PRO ASP LYS ALA ASN LEU GLY PHE ARG PHE          
SEQRES  45 A  751  PRO CYS ASP GLY PRO GLY ARG GLY GLY THR CYS GLN VAL          
SEQRES  46 A  751  SER GLY TRP ASP HIS VAL PHE LEU GLY LEU PHE TRP MET          
SEQRES  47 A  751  TYR ASN SER LEU SER ILE VAL ILE PHE HIS PHE SER TRP          
SEQRES  48 A  751  LYS MET GLN SER ASP VAL TRP GLY THR VAL SER PRO ASP          
SEQRES  49 A  751  GLY SER VAL THR HIS VAL THR LEU GLY ASN PHE ALA GLN          
SEQRES  50 A  751  SER ALA ILE THR ILE ASN GLY TRP LEU ARG ASP PHE LEU          
SEQRES  51 A  751  TRP ALA GLN ALA ALA ASN VAL ILE ASN SER TYR GLY SER          
SEQRES  52 A  751  ALA LEU SER ALA TYR GLY ILE MET PHE LEU ALA GLY HIS          
SEQRES  53 A  751  PHE VAL PHE ALA PHE SER LEU MET PHE LEU PHE SER GLY          
SEQRES  54 A  751  ARG GLY TYR TRP GLN GLU LEU ILE GLU SER ILE VAL TRP          
SEQRES  55 A  751  ALA HIS ASN LYS LEU ASN VAL ALA PRO ALA ILE GLN PRO          
SEQRES  56 A  751  ARG ALA LEU SER ILE ILE GLN GLY ARG ALA VAL GLY VAL          
SEQRES  57 A  751  ALA HIS TYR LEU LEU GLY GLY ILE VAL THR THR TRP ALA          
SEQRES  58 A  751  PHE PHE LEU ALA ARG SER LEU SER ILE GLY                      
SEQRES   1 B  731  MET ALA THR LYS PHE PRO LYS PHE SER GLN ASP LEU ALA          
SEQRES   2 B  731  GLN ASP PRO THR THR ARG ARG ILE TRP TYR GLY ILE ALA          
SEQRES   3 B  731  THR ALA HIS ASP PHE GLU THR HIS ASP GLY MET THR GLU          
SEQRES   4 B  731  GLU ASN LEU TYR GLN LYS ILE PHE ALA SER HIS PHE GLY          
SEQRES   5 B  731  HIS ILE ALA ILE ILE PHE LEU TRP THR SER GLY THR LEU          
SEQRES   6 B  731  PHE HIS VAL ALA TRP GLN GLY ASN PHE GLU GLN TRP ILE          
SEQRES   7 B  731  LYS ASP PRO LEU ASN ILE ARG PRO ILE ALA HIS ALA ILE          
SEQRES   8 B  731  TRP ASP PRO HIS PHE GLY GLU GLY ALA VAL ASN ALA PHE          
SEQRES   9 B  731  THR GLN ALA GLY ALA SER ASN PRO VAL ASN ILE ALA TYR          
SEQRES  10 B  731  SER GLY VAL TYR HIS TRP PHE TYR THR ILE GLY MET THR          
SEQRES  11 B  731  THR ASN GLN GLU LEU TYR SER GLY ALA VAL PHE LEU LEU          
SEQRES  12 B  731  VAL LEU ALA SER LEU PHE LEU PHE ALA GLY TRP LEU HIS          
SEQRES  13 B  731  LEU GLN PRO LYS PHE ARG PRO SER LEU ALA TRP PHE LYS          
SEQRES  14 B  731  ASN ALA GLU SER ARG LEU ASN HIS HIS LEU ALA GLY LEU          
SEQRES  15 B  731  PHE GLY VAL SER SER LEU ALA TRP ALA GLY HIS LEU VAL          
SEQRES  16 B  731  HIS VAL ALA ILE PRO GLU ALA ARG GLY GLN HIS VAL GLY          
SEQRES  17 B  731  TRP ASP ASN PHE LEU SER THR PRO PRO HIS PRO ALA GLY          
SEQRES  18 B  731  LEU MET PRO PHE PHE THR GLY ASN TRP GLY VAL TYR ALA          
SEQRES  19 B  731  ALA ASP PRO ASP THR ALA GLY HIS ILE PHE GLY THR SER          
SEQRES  20 B  731  GLU GLY ALA GLY THR ALA ILE LEU THR PHE LEU GLY GLY          
SEQRES  21 B  731  PHE HIS PRO GLN THR GLU SER LEU TRP LEU THR ASP ILE          
SEQRES  22 B  731  ALA HIS HIS HIS LEU ALA ILE ALA VAL ILE PHE ILE ILE          
SEQRES  23 B  731  ALA GLY HIS MET TYR ARG THR ASN TRP GLY ILE GLY HIS          
SEQRES  24 B  731  SER ILE LYS GLU ILE LEU ASN ALA HIS LYS GLY PRO LEU          
SEQRES  25 B  731  THR GLY ALA GLY HIS THR ASN LEU TYR ASP THR ILE ASN          
SEQRES  26 B  731  ASN SER LEU HIS PHE GLN LEU GLY LEU ALA LEU ALA SER          
SEQRES  27 B  731  LEU GLY VAL ILE THR SER LEU VAL ALA GLN HIS MET TYR          
SEQRES  28 B  731  SER LEU PRO SER TYR ALA PHE ILE ALA GLN ASP HIS THR          
SEQRES  29 B  731  THR GLN ALA ALA LEU TYR THR HIS HIS GLN TYR ILE ALA          
SEQRES  30 B  731  GLY PHE LEU MET VAL GLY ALA PHE ALA HIS GLY ALA ILE          
SEQRES  31 B  731  PHE PHE VAL ARG ASP TYR ASP PRO VAL ALA ASN LYS ASP          
SEQRES  32 B  731  ASN VAL LEU ALA ARG MET LEU GLU HIS LYS GLU ALA LEU          
SEQRES  33 B  731  ILE SER HIS LEU SER TRP VAL SER LEU PHE LEU GLY PHE          
SEQRES  34 B  731  HIS THR LEU GLY LEU TYR VAL HIS ASN ASP VAL VAL VAL          
SEQRES  35 B  731  ALA PHE GLY THR PRO GLU LYS GLN ILE LEU ILE GLU PRO          
SEQRES  36 B  731  VAL PHE ALA GLN TRP ILE GLN ALA THR SER GLY LYS ALA          
SEQRES  37 B  731  LEU TYR GLY PHE ASP VAL LEU LEU SER ASN PRO ASP SER          
SEQRES  38 B  731  ILE ALA SER THR THR GLY ALA ALA TRP LEU PRO GLY TRP          
SEQRES  39 B  731  LEU ASP ALA ILE ASN SER GLY THR ASN SER LEU PHE LEU          
SEQRES  40 B  731  THR ILE GLY PRO GLY ASP PHE LEU VAL HIS HIS ALA ILE          
SEQRES  41 B  731  ALA LEU GLY LEU HIS THR THR ALA LEU ILE LEU ILE LYS          
SEQRES  42 B  731  GLY ALA LEU ASP ALA ARG GLY SER LYS LEU MET PRO ASP          
SEQRES  43 B  731  LYS LYS ASP PHE GLY TYR SER PHE PRO CYS ASP GLY PRO          
SEQRES  44 B  731  GLY ARG GLY GLY THR CYS ASP ILE SER ALA TRP ASP ALA          
SEQRES  45 B  731  PHE TYR LEU ALA MET PHE TRP MET LEU ASN THR LEU GLY          
SEQRES  46 B  731  TRP LEU THR PHE TYR TRP HIS TRP LYS HIS LEU GLY VAL          
SEQRES  47 B  731  TRP SER GLY ASN VAL ALA GLN PHE ASN GLU ASN SER THR          
SEQRES  48 B  731  TYR LEU MET GLY TRP PHE ARG ASP TYR LEU TRP ALA ASN          
SEQRES  49 B  731  SER ALA GLN LEU ILE ASN GLY TYR ASN PRO TYR GLY VAL          
SEQRES  50 B  731  ASN ASN LEU SER VAL TRP ALA TRP MET PHE LEU PHE GLY          
SEQRES  51 B  731  HIS LEU VAL TRP ALA THR GLY PHE MET PHE LEU ILE SER          
SEQRES  52 B  731  TRP ARG GLY TYR TRP GLN GLU LEU ILE GLU THR ILE VAL          
SEQRES  53 B  731  TRP ALA HIS GLU ARG THR PRO LEU ALA ASN LEU VAL ARG          
SEQRES  54 B  731  TRP LYS ASP LYS PRO VAL ALA LEU SER ILE VAL GLN ALA          
SEQRES  55 B  731  ARG LEU VAL GLY LEU ALA HIS PHE THR VAL GLY TYR VAL          
SEQRES  56 B  731  LEU THR TYR ALA ALA PHE LEU ILE ALA SER THR ALA GLY          
SEQRES  57 B  731  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 LEU ASP VAL LEU          
SEQRES   3 C   81  GLU MET VAL PRO TRP ASP GLY CYS LYS ALA ALA GLN ILE          
SEQRES   4 C   81  ALA SER SER PRO ARG THR GLU ASP CYS VAL GLY CYS LYS          
SEQRES   5 C   81  ARG CYS GLU THR ALA CYS PRO THR ASP PHE LEU SER ILE          
SEQRES   6 C   81  ARG VAL TYR LEU GLY ALA GLU THR THR ARG SER MET GLY          
SEQRES   7 C   81  LEU ALA TYR                                                  
SEQRES   1 D  141  MET THR GLU LEU SER GLY GLN PRO PRO LYS PHE GLY GLY          
SEQRES   2 D  141  SER THR GLY GLY LEU LEU SER LYS ALA ASN ARG GLU GLU          
SEQRES   3 D  141  LYS TYR ALA ILE THR TRP THR SER ALA SER GLU GLN VAL          
SEQRES   4 D  141  PHE GLU MET PRO THR GLY GLY ALA ALA ILE MET ASN GLU          
SEQRES   5 D  141  GLY GLU ASN LEU LEU TYR LEU ALA ARG LYS GLU GLN CYS          
SEQRES   6 D  141  LEU ALA LEU GLY THR GLN LEU ARG THR LYS PHE LYS PRO          
SEQRES   7 D  141  LYS ILE GLN ASP TYR LYS ILE TYR ARG VAL TYR PRO SER          
SEQRES   8 D  141  GLY GLU VAL GLN TYR LEU HIS PRO ALA ASP GLY VAL PHE          
SEQRES   9 D  141  PRO GLU LYS VAL ASN GLU GLY ARG GLU ALA GLN GLY THR          
SEQRES  10 D  141  LYS THR ARG ARG ILE GLY GLN ASN PRO GLU PRO VAL THR          
SEQRES  11 D  141  ILE LYS PHE SER GLY LYS ALA PRO TYR GLU VAL                  
SEQRES   1 E   74  MET ALA LEU ASN ARG GLY ASP LYS VAL ARG ILE LYS ARG          
SEQRES   2 E   74  THR GLU SER TYR TRP TYR GLY ASP VAL GLY THR VAL ALA          
SEQRES   3 E   74  SER VAL GLU LYS SER GLY ILE LEU TYR PRO VAL ILE VAL          
SEQRES   4 E   74  ARG PHE ASP ARG VAL ASN TYR ASN GLY PHE SER GLY SER          
SEQRES   5 E   74  ALA SER GLY VAL ASN THR ASN ASN PHE ALA GLU ASN GLU          
SEQRES   6 E   74  LEU GLU LEU VAL GLN ALA ALA ALA LYS                          
SEQRES   1 F  125  MET ASP GLY LEU LYS SER PHE LEU SER THR ALA PRO VAL          
SEQRES   2 F  125  MET ILE MET ALA LEU LEU THR PHE THR ALA GLY ILE LEU          
SEQRES   3 F  125  ILE GLU PHE ASN ALA PHE TYR PRO ASP LEU LEU PHE HIS          
SEQRES   4 F  125  PRO CYS SER CYS ALA GLY ASP PHE LEU ILE PRO SER ILE          
SEQRES   5 F  125  ILE PHE LEU TYR ILE ALA GLY TRP ILE GLY TRP VAL GLY          
SEQRES   6 F  125  ARG SER TYR LEU ILE GLU ILE ARG GLU SER LYS ASN PRO          
SEQRES   7 F  125  GLU MET GLN GLU VAL VAL ILE ASN VAL PRO LEU ALA ILE          
SEQRES   8 F  125  LYS LYS MET LEU GLY GLY PHE LEU TRP PRO LEU ALA ALA          
SEQRES   9 F  125  VAL GLY GLU TYR THR SER GLY LYS LEU VAL MET LYS ASP          
SEQRES  10 F  125  SER GLU ILE PRO THR SER PRO ARG                              
SEQRES   1 L  157  MET ALA GLU SER ASN GLN VAL VAL GLN ALA TYR ASN GLY          
SEQRES   2 L  157  ASP PRO PHE VAL GLY HIS LEU SER THR PRO ILE SER ASP          
SEQRES   3 L  157  SER ALA PHE THR ARG THR PHE ILE GLY ASN LEU PRO ALA          
SEQRES   4 L  157  TYR ARG LYS GLY LEU SER PRO ILE LEU ARG GLY LEU GLU          
SEQRES   5 L  157  VAL GLY MET ALA HIS GLY TYR PHE LEU ILE GLY PRO TRP          
SEQRES   6 L  157  THR LEU LEU GLY PRO LEU ARG ASP SER GLU TYR GLN TYR          
SEQRES   7 L  157  ILE GLY GLY LEU ILE GLY ALA LEU ALA LEU ILE LEU VAL          
SEQRES   8 L  157  ALA THR ALA ALA LEU SER SER TYR GLY LEU VAL THR PHE          
SEQRES   9 L  157  GLN GLY GLU GLN GLY SER GLY ASP THR LEU GLN THR ALA          
SEQRES  10 L  157  ASP GLY TRP SER GLN PHE ALA ALA GLY PHE PHE VAL GLY          
SEQRES  11 L  157  GLY MET GLY GLY ALA PHE VAL ALA TYR PHE LEU LEU GLU          
SEQRES  12 L  157  ASN LEU SER VAL VAL ASP GLY ILE PHE ARG GLY LEU PHE          
SEQRES  13 L  157  ASN                                                          
SEQRES   1 M   31  MET ALA LEU SER ASP THR GLN ILE LEU ALA ALA LEU VAL          
SEQRES   2 M   31  VAL ALA LEU LEU PRO ALA PHE LEU ALA PHE ARG LEU SER          
SEQRES   3 M   31  THR GLU LEU TYR LYS                                          
SEQRES   1 a  751  MET THR ILE SER PRO PRO GLU ARG GLU ALA LYS ALA LYS          
SEQRES   2 a  751  VAL SER VAL ASP ASN ASN PRO VAL PRO THR SER PHE GLU          
SEQRES   3 a  751  LYS TRP GLY LYS PRO GLY HIS PHE ASP ARG THR LEU ALA          
SEQRES   4 a  751  ARG GLY PRO LYS THR THR THR TRP ILE TRP ASN LEU HIS          
SEQRES   5 a  751  ALA ASN ALA HIS ASP PHE ASP SER GLN THR SER ASP LEU          
SEQRES   6 a  751  GLU ASP VAL SER ARG LYS ILE PHE SER ALA HIS PHE GLY          
SEQRES   7 a  751  HIS LEU ALA VAL VAL PHE VAL TRP LEU SER GLY MET TYR          
SEQRES   8 a  751  PHE HIS GLY ALA LYS PHE SER ASN TYR GLU GLY TRP LEU          
SEQRES   9 a  751  ALA ASP PRO THR HIS ILE LYS PRO SER ALA GLN VAL VAL          
SEQRES  10 a  751  TRP PRO ILE VAL GLY GLN GLY ILE LEU ASN GLY ASP VAL          
SEQRES  11 a  751  GLY GLY GLY PHE HIS GLY ILE GLN ILE THR SER GLY LEU          
SEQRES  12 a  751  PHE TYR LEU TRP ARG ALA SER GLY PHE THR ASP SER TYR          
SEQRES  13 a  751  GLN LEU TYR CYS THR ALA ILE GLY GLY LEU VAL MET ALA          
SEQRES  14 a  751  ALA LEU MET LEU PHE ALA GLY TRP PHE HIS TYR HIS VAL          
SEQRES  15 a  751  LYS ALA PRO LYS LEU GLU TRP PHE GLN ASN VAL GLU SER          
SEQRES  16 a  751  MET MET ASN HIS HIS LEU ALA GLY LEU LEU GLY LEU GLY          
SEQRES  17 a  751  SER LEU GLY TRP ALA GLY HIS GLN ILE HIS VAL SER MET          
SEQRES  18 a  751  PRO ILE ASN LYS LEU LEU ASP ALA GLY VAL ALA PRO LYS          
SEQRES  19 a  751  ASP ILE PRO LEU PRO HIS GLU PHE ILE LEU GLU PRO SER          
SEQRES  20 a  751  LYS MET ALA GLU LEU TYR PRO SER PHE ALA GLN GLY LEU          
SEQRES  21 a  751  THR PRO PHE PHE THR LEU ASN TRP GLY VAL TYR SER ASP          
SEQRES  22 a  751  PHE LEU THR PHE LYS GLY GLY LEU ASN PRO VAL THR GLY          
SEQRES  23 a  751  GLY LEU TRP LEU SER ASP THR ALA HIS HIS HIS LEU ALA          
SEQRES  24 a  751  ILE ALA VAL LEU PHE ILE ILE ALA GLY HIS MET TYR ARG          
SEQRES  25 a  751  THR ASN TRP GLY ILE GLY HIS SER MET LYS GLU ILE LEU          
SEQRES  26 a  751  GLU ALA HIS LYS GLY PRO PHE THR GLY GLU GLY HIS LYS          
SEQRES  27 a  751  GLY LEU TYR GLU ILE LEU THR THR SER TRP HIS ALA GLN          
SEQRES  28 a  751  LEU ALA ILE ASN LEU ALA LEU LEU GLY SER LEU THR ILE          
SEQRES  29 a  751  ILE VAL ALA GLN HIS MET TYR ALA MET PRO PRO TYR PRO          
SEQRES  30 a  751  TYR GLN ALA ILE ASP TYR ALA THR GLN LEU SER LEU PHE          
SEQRES  31 a  751  THR HIS HIS MET TRP ILE GLY GLY PHE LEU ILE VAL GLY          
SEQRES  32 a  751  ALA GLY ALA HIS GLY ALA ILE PHE MET VAL ARG ASP TYR          
SEQRES  33 a  751  ASP PRO ALA LYS ASN VAL ASN ASN LEU LEU ASP ARG MET          
SEQRES  34 a  751  LEU ARG HIS ARG ASP ALA ILE ILE SER HIS LEU ASN TRP          
SEQRES  35 a  751  VAL CYS ILE PHE LEU GLY PHE HIS SER PHE GLY LEU TYR          
SEQRES  36 a  751  ILE HIS ASN ASP THR MET ARG ALA LEU GLY ARG PRO GLN          
SEQRES  37 a  751  ASP MET PHE SER ASP THR ALA ILE GLN LEU GLN PRO ILE          
SEQRES  38 a  751  PHE ALA GLN TRP VAL GLN HIS LEU HIS THR LEU ALA PRO          
SEQRES  39 a  751  GLY ALA THR ALA PRO ASN ALA LEU ALA THR ALA SER TYR          
SEQRES  40 a  751  ALA PHE GLY GLY GLU THR ILE ALA VAL ALA GLY LYS VAL          
SEQRES  41 a  751  ALA MET MET PRO ILE THR LEU GLY THR ALA ASP PHE MET          
SEQRES  42 a  751  VAL HIS HIS ILE HIS ALA PHE THR ILE HIS VAL THR ALA          
SEQRES  43 a  751  LEU ILE LEU LEU LYS GLY VAL LEU TYR ALA ARG SER SER          
SEQRES  44 a  751  ARG LEU VAL PRO ASP LYS ALA ASN LEU GLY PHE ARG PHE          
SEQRES  45 a  751  PRO CYS ASP GLY PRO GLY ARG GLY GLY THR CYS GLN VAL          
SEQRES  46 a  751  SER GLY TRP ASP HIS VAL PHE LEU GLY LEU PHE TRP MET          
SEQRES  47 a  751  TYR ASN SER LEU SER ILE VAL ILE PHE HIS PHE SER TRP          
SEQRES  48 a  751  LYS MET GLN SER ASP VAL TRP GLY THR VAL SER PRO ASP          
SEQRES  49 a  751  GLY SER VAL THR HIS VAL THR LEU GLY ASN PHE ALA GLN          
SEQRES  50 a  751  SER ALA ILE THR ILE ASN GLY TRP LEU ARG ASP PHE LEU          
SEQRES  51 a  751  TRP ALA GLN ALA ALA ASN VAL ILE ASN SER TYR GLY SER          
SEQRES  52 a  751  ALA LEU SER ALA TYR GLY ILE MET PHE LEU ALA GLY HIS          
SEQRES  53 a  751  PHE VAL PHE ALA PHE SER LEU MET PHE LEU PHE SER GLY          
SEQRES  54 a  751  ARG GLY TYR TRP GLN GLU LEU ILE GLU SER ILE VAL TRP          
SEQRES  55 a  751  ALA HIS ASN LYS LEU ASN VAL ALA PRO ALA ILE GLN PRO          
SEQRES  56 a  751  ARG ALA LEU SER ILE ILE GLN GLY ARG ALA VAL GLY VAL          
SEQRES  57 a  751  ALA HIS TYR LEU LEU GLY GLY ILE VAL THR THR TRP ALA          
SEQRES  58 a  751  PHE PHE LEU ALA ARG SER LEU SER ILE GLY                      
SEQRES   1 b  731  MET ALA THR LYS PHE PRO LYS PHE SER GLN ASP LEU ALA          
SEQRES   2 b  731  GLN ASP PRO THR THR ARG ARG ILE TRP TYR GLY ILE ALA          
SEQRES   3 b  731  THR ALA HIS ASP PHE GLU THR HIS ASP GLY MET THR GLU          
SEQRES   4 b  731  GLU ASN LEU TYR GLN LYS ILE PHE ALA SER HIS PHE GLY          
SEQRES   5 b  731  HIS ILE ALA ILE ILE PHE LEU TRP THR SER GLY THR LEU          
SEQRES   6 b  731  PHE HIS VAL ALA TRP GLN GLY ASN PHE GLU GLN TRP ILE          
SEQRES   7 b  731  LYS ASP PRO LEU ASN ILE ARG PRO ILE ALA HIS ALA ILE          
SEQRES   8 b  731  TRP ASP PRO HIS PHE GLY GLU GLY ALA VAL ASN ALA PHE          
SEQRES   9 b  731  THR GLN ALA GLY ALA SER ASN PRO VAL ASN ILE ALA TYR          
SEQRES  10 b  731  SER GLY VAL TYR HIS TRP PHE TYR THR ILE GLY MET THR          
SEQRES  11 b  731  THR ASN GLN GLU LEU TYR SER GLY ALA VAL PHE LEU LEU          
SEQRES  12 b  731  VAL LEU ALA SER LEU PHE LEU PHE ALA GLY TRP LEU HIS          
SEQRES  13 b  731  LEU GLN PRO LYS PHE ARG PRO SER LEU ALA TRP PHE LYS          
SEQRES  14 b  731  ASN ALA GLU SER ARG LEU ASN HIS HIS LEU ALA GLY LEU          
SEQRES  15 b  731  PHE GLY VAL SER SER LEU ALA TRP ALA GLY HIS LEU VAL          
SEQRES  16 b  731  HIS VAL ALA ILE PRO GLU ALA ARG GLY GLN HIS VAL GLY          
SEQRES  17 b  731  TRP ASP ASN PHE LEU SER THR PRO PRO HIS PRO ALA GLY          
SEQRES  18 b  731  LEU MET PRO PHE PHE THR GLY ASN TRP GLY VAL TYR ALA          
SEQRES  19 b  731  ALA ASP PRO ASP THR ALA GLY HIS ILE PHE GLY THR SER          
SEQRES  20 b  731  GLU GLY ALA GLY THR ALA ILE LEU THR PHE LEU GLY GLY          
SEQRES  21 b  731  PHE HIS PRO GLN THR GLU SER LEU TRP LEU THR ASP ILE          
SEQRES  22 b  731  ALA HIS HIS HIS LEU ALA ILE ALA VAL ILE PHE ILE ILE          
SEQRES  23 b  731  ALA GLY HIS MET TYR ARG THR ASN TRP GLY ILE GLY HIS          
SEQRES  24 b  731  SER ILE LYS GLU ILE LEU ASN ALA HIS LYS GLY PRO LEU          
SEQRES  25 b  731  THR GLY ALA GLY HIS THR ASN LEU TYR ASP THR ILE ASN          
SEQRES  26 b  731  ASN SER LEU HIS PHE GLN LEU GLY LEU ALA LEU ALA SER          
SEQRES  27 b  731  LEU GLY VAL ILE THR SER LEU VAL ALA GLN HIS MET TYR          
SEQRES  28 b  731  SER LEU PRO SER TYR ALA PHE ILE ALA GLN ASP HIS THR          
SEQRES  29 b  731  THR GLN ALA ALA LEU TYR THR HIS HIS GLN TYR ILE ALA          
SEQRES  30 b  731  GLY PHE LEU MET VAL GLY ALA PHE ALA HIS GLY ALA ILE          
SEQRES  31 b  731  PHE PHE VAL ARG ASP TYR ASP PRO VAL ALA ASN LYS ASP          
SEQRES  32 b  731  ASN VAL LEU ALA ARG MET LEU GLU HIS LYS GLU ALA LEU          
SEQRES  33 b  731  ILE SER HIS LEU SER TRP VAL SER LEU PHE LEU GLY PHE          
SEQRES  34 b  731  HIS THR LEU GLY LEU TYR VAL HIS ASN ASP VAL VAL VAL          
SEQRES  35 b  731  ALA PHE GLY THR PRO GLU LYS GLN ILE LEU ILE GLU PRO          
SEQRES  36 b  731  VAL PHE ALA GLN TRP ILE GLN ALA THR SER GLY LYS ALA          
SEQRES  37 b  731  LEU TYR GLY PHE ASP VAL LEU LEU SER ASN PRO ASP SER          
SEQRES  38 b  731  ILE ALA SER THR THR GLY ALA ALA TRP LEU PRO GLY TRP          
SEQRES  39 b  731  LEU ASP ALA ILE ASN SER GLY THR ASN SER LEU PHE LEU          
SEQRES  40 b  731  THR ILE GLY PRO GLY ASP PHE LEU VAL HIS HIS ALA ILE          
SEQRES  41 b  731  ALA LEU GLY LEU HIS THR THR ALA LEU ILE LEU ILE LYS          
SEQRES  42 b  731  GLY ALA LEU ASP ALA ARG GLY SER LYS LEU MET PRO ASP          
SEQRES  43 b  731  LYS LYS ASP PHE GLY TYR SER PHE PRO CYS ASP GLY PRO          
SEQRES  44 b  731  GLY ARG GLY GLY THR CYS ASP ILE SER ALA TRP ASP ALA          
SEQRES  45 b  731  PHE TYR LEU ALA MET PHE TRP MET LEU ASN THR LEU GLY          
SEQRES  46 b  731  TRP LEU THR PHE TYR TRP HIS TRP LYS HIS LEU GLY VAL          
SEQRES  47 b  731  TRP SER GLY ASN VAL ALA GLN PHE ASN GLU ASN SER THR          
SEQRES  48 b  731  TYR LEU MET GLY TRP PHE ARG ASP TYR LEU TRP ALA ASN          
SEQRES  49 b  731  SER ALA GLN LEU ILE ASN GLY TYR ASN PRO TYR GLY VAL          
SEQRES  50 b  731  ASN ASN LEU SER VAL TRP ALA TRP MET PHE LEU PHE GLY          
SEQRES  51 b  731  HIS LEU VAL TRP ALA THR GLY PHE MET PHE LEU ILE SER          
SEQRES  52 b  731  TRP ARG GLY TYR TRP GLN GLU LEU ILE GLU THR ILE VAL          
SEQRES  53 b  731  TRP ALA HIS GLU ARG THR PRO LEU ALA ASN LEU VAL ARG          
SEQRES  54 b  731  TRP LYS ASP LYS PRO VAL ALA LEU SER ILE VAL GLN ALA          
SEQRES  55 b  731  ARG LEU VAL GLY LEU ALA HIS PHE THR VAL GLY TYR VAL          
SEQRES  56 b  731  LEU THR TYR ALA ALA PHE LEU ILE ALA SER THR ALA GLY          
SEQRES  57 b  731  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 LEU ASP VAL LEU          
SEQRES   3 c   81  GLU MET VAL PRO TRP ASP GLY CYS LYS ALA ALA GLN ILE          
SEQRES   4 c   81  ALA SER SER PRO ARG THR GLU ASP CYS VAL GLY CYS LYS          
SEQRES   5 c   81  ARG CYS GLU THR ALA CYS PRO THR ASP PHE LEU SER ILE          
SEQRES   6 c   81  ARG VAL TYR LEU GLY ALA GLU THR THR ARG SER MET GLY          
SEQRES   7 c   81  LEU ALA TYR                                                  
SEQRES   1 d  141  MET THR GLU LEU SER GLY GLN PRO PRO LYS PHE GLY GLY          
SEQRES   2 d  141  SER THR GLY GLY LEU LEU SER LYS ALA ASN ARG GLU GLU          
SEQRES   3 d  141  LYS TYR ALA ILE THR TRP THR SER ALA SER GLU GLN VAL          
SEQRES   4 d  141  PHE GLU MET PRO THR GLY GLY ALA ALA ILE MET ASN GLU          
SEQRES   5 d  141  GLY GLU ASN LEU LEU TYR LEU ALA ARG LYS GLU GLN CYS          
SEQRES   6 d  141  LEU ALA LEU GLY THR GLN LEU ARG THR LYS PHE LYS PRO          
SEQRES   7 d  141  LYS ILE GLN ASP TYR LYS ILE TYR ARG VAL TYR PRO SER          
SEQRES   8 d  141  GLY GLU VAL GLN TYR LEU HIS PRO ALA ASP GLY VAL PHE          
SEQRES   9 d  141  PRO GLU LYS VAL ASN GLU GLY ARG GLU ALA GLN GLY THR          
SEQRES  10 d  141  LYS THR ARG ARG ILE GLY GLN ASN PRO GLU PRO VAL THR          
SEQRES  11 d  141  ILE LYS PHE SER GLY LYS ALA PRO TYR GLU VAL                  
SEQRES   1 e   74  MET ALA LEU ASN ARG GLY ASP LYS VAL ARG ILE LYS ARG          
SEQRES   2 e   74  THR GLU SER TYR TRP TYR GLY ASP VAL GLY THR VAL ALA          
SEQRES   3 e   74  SER VAL GLU LYS SER GLY ILE LEU TYR PRO VAL ILE VAL          
SEQRES   4 e   74  ARG PHE ASP ARG VAL ASN TYR ASN GLY PHE SER GLY SER          
SEQRES   5 e   74  ALA SER GLY VAL ASN THR ASN ASN PHE ALA GLU ASN GLU          
SEQRES   6 e   74  LEU GLU LEU VAL GLN ALA ALA ALA LYS                          
SEQRES   1 f  125  MET ASP GLY LEU LYS SER PHE LEU SER THR ALA PRO VAL          
SEQRES   2 f  125  MET ILE MET ALA LEU LEU THR PHE THR ALA GLY ILE LEU          
SEQRES   3 f  125  ILE GLU PHE ASN ALA PHE TYR PRO ASP LEU LEU PHE HIS          
SEQRES   4 f  125  PRO CYS SER CYS ALA GLY ASP PHE LEU ILE PRO SER ILE          
SEQRES   5 f  125  ILE PHE LEU TYR ILE ALA GLY TRP ILE GLY TRP VAL GLY          
SEQRES   6 f  125  ARG SER TYR LEU ILE GLU ILE ARG GLU SER LYS ASN PRO          
SEQRES   7 f  125  GLU MET GLN GLU VAL VAL ILE ASN VAL PRO LEU ALA ILE          
SEQRES   8 f  125  LYS LYS MET LEU GLY GLY PHE LEU TRP PRO LEU ALA ALA          
SEQRES   9 f  125  VAL GLY GLU TYR THR SER GLY LYS LEU VAL MET LYS ASP          
SEQRES  10 f  125  SER GLU ILE PRO THR SER PRO ARG                              
SEQRES   1 i   40  MET ASP GLY SER TYR ALA ALA SER TYR LEU PRO TRP ILE          
SEQRES   2 i   40  LEU ILE PRO MET VAL GLY TRP LEU PHE PRO ALA VAL THR          
SEQRES   3 i   40  MET GLY LEU LEU PHE ILE HIS ILE GLU SER GLU GLY GLU          
SEQRES   4 i   40  GLY                                                          
SEQRES   1 l  157  MET ALA GLU SER ASN GLN VAL VAL GLN ALA TYR ASN GLY          
SEQRES   2 l  157  ASP PRO PHE VAL GLY HIS LEU SER THR PRO ILE SER ASP          
SEQRES   3 l  157  SER ALA PHE THR ARG THR PHE ILE GLY ASN LEU PRO ALA          
SEQRES   4 l  157  TYR ARG LYS GLY LEU SER PRO ILE LEU ARG GLY LEU GLU          
SEQRES   5 l  157  VAL GLY MET ALA HIS GLY TYR PHE LEU ILE GLY PRO TRP          
SEQRES   6 l  157  THR LEU LEU GLY PRO LEU ARG ASP SER GLU TYR GLN TYR          
SEQRES   7 l  157  ILE GLY GLY LEU ILE GLY ALA LEU ALA LEU ILE LEU VAL          
SEQRES   8 l  157  ALA THR ALA ALA LEU SER SER TYR GLY LEU VAL THR PHE          
SEQRES   9 l  157  GLN GLY GLU GLN GLY SER GLY ASP THR LEU GLN THR ALA          
SEQRES  10 l  157  ASP GLY TRP SER GLN PHE ALA ALA GLY PHE PHE VAL GLY          
SEQRES  11 l  157  GLY MET GLY GLY ALA PHE VAL ALA TYR PHE LEU LEU GLU          
SEQRES  12 l  157  ASN LEU SER VAL VAL ASP GLY ILE PHE ARG GLY LEU PHE          
SEQRES  13 l  157  ASN                                                          
SEQRES   1 m   31  MET ALA LEU SER ASP THR GLN ILE LEU ALA ALA LEU VAL          
SEQRES   2 m   31  VAL ALA LEU LEU PRO ALA PHE LEU ALA PHE ARG LEU SER          
SEQRES   3 m   31  THR GLU LEU TYR LYS                                          
SEQRES   1 1  751  MET THR ILE SER PRO PRO GLU ARG GLU ALA LYS ALA LYS          
SEQRES   2 1  751  VAL SER VAL ASP ASN ASN PRO VAL PRO THR SER PHE GLU          
SEQRES   3 1  751  LYS TRP GLY LYS PRO GLY HIS PHE ASP ARG THR LEU ALA          
SEQRES   4 1  751  ARG GLY PRO LYS THR THR THR TRP ILE TRP ASN LEU HIS          
SEQRES   5 1  751  ALA ASN ALA HIS ASP PHE ASP SER GLN THR SER ASP LEU          
SEQRES   6 1  751  GLU ASP VAL SER ARG LYS ILE PHE SER ALA HIS PHE GLY          
SEQRES   7 1  751  HIS LEU ALA VAL VAL PHE VAL TRP LEU SER GLY MET TYR          
SEQRES   8 1  751  PHE HIS GLY ALA LYS PHE SER ASN TYR GLU GLY TRP LEU          
SEQRES   9 1  751  ALA ASP PRO THR HIS ILE LYS PRO SER ALA GLN VAL VAL          
SEQRES  10 1  751  TRP PRO ILE VAL GLY GLN GLY ILE LEU ASN GLY ASP VAL          
SEQRES  11 1  751  GLY GLY GLY PHE HIS GLY ILE GLN ILE THR SER GLY LEU          
SEQRES  12 1  751  PHE TYR LEU TRP ARG ALA SER GLY PHE THR ASP SER TYR          
SEQRES  13 1  751  GLN LEU TYR CYS THR ALA ILE GLY GLY LEU VAL MET ALA          
SEQRES  14 1  751  ALA LEU MET LEU PHE ALA GLY TRP PHE HIS TYR HIS VAL          
SEQRES  15 1  751  LYS ALA PRO LYS LEU GLU TRP PHE GLN ASN VAL GLU SER          
SEQRES  16 1  751  MET MET ASN HIS HIS LEU ALA GLY LEU LEU GLY LEU GLY          
SEQRES  17 1  751  SER LEU GLY TRP ALA GLY HIS GLN ILE HIS VAL SER MET          
SEQRES  18 1  751  PRO ILE ASN LYS LEU LEU ASP ALA GLY VAL ALA PRO LYS          
SEQRES  19 1  751  ASP ILE PRO LEU PRO HIS GLU PHE ILE LEU GLU PRO SER          
SEQRES  20 1  751  LYS MET ALA GLU LEU TYR PRO SER PHE ALA GLN GLY LEU          
SEQRES  21 1  751  THR PRO PHE PHE THR LEU ASN TRP GLY VAL TYR SER ASP          
SEQRES  22 1  751  PHE LEU THR PHE LYS GLY GLY LEU ASN PRO VAL THR GLY          
SEQRES  23 1  751  GLY LEU TRP LEU SER ASP THR ALA HIS HIS HIS LEU ALA          
SEQRES  24 1  751  ILE ALA VAL LEU PHE ILE ILE ALA GLY HIS MET TYR ARG          
SEQRES  25 1  751  THR ASN TRP GLY ILE GLY HIS SER MET LYS GLU ILE LEU          
SEQRES  26 1  751  GLU ALA HIS LYS GLY PRO PHE THR GLY GLU GLY HIS LYS          
SEQRES  27 1  751  GLY LEU TYR GLU ILE LEU THR THR SER TRP HIS ALA GLN          
SEQRES  28 1  751  LEU ALA ILE ASN LEU ALA LEU LEU GLY SER LEU THR ILE          
SEQRES  29 1  751  ILE VAL ALA GLN HIS MET TYR ALA MET PRO PRO TYR PRO          
SEQRES  30 1  751  TYR GLN ALA ILE ASP TYR ALA THR GLN LEU SER LEU PHE          
SEQRES  31 1  751  THR HIS HIS MET TRP ILE GLY GLY PHE LEU ILE VAL GLY          
SEQRES  32 1  751  ALA GLY ALA HIS GLY ALA ILE PHE MET VAL ARG ASP TYR          
SEQRES  33 1  751  ASP PRO ALA LYS ASN VAL ASN ASN LEU LEU ASP ARG MET          
SEQRES  34 1  751  LEU ARG HIS ARG ASP ALA ILE ILE SER HIS LEU ASN TRP          
SEQRES  35 1  751  VAL CYS ILE PHE LEU GLY PHE HIS SER PHE GLY LEU TYR          
SEQRES  36 1  751  ILE HIS ASN ASP THR MET ARG ALA LEU GLY ARG PRO GLN          
SEQRES  37 1  751  ASP MET PHE SER ASP THR ALA ILE GLN LEU GLN PRO ILE          
SEQRES  38 1  751  PHE ALA GLN TRP VAL GLN HIS LEU HIS THR LEU ALA PRO          
SEQRES  39 1  751  GLY ALA THR ALA PRO ASN ALA LEU ALA THR ALA SER TYR          
SEQRES  40 1  751  ALA PHE GLY GLY GLU THR ILE ALA VAL ALA GLY LYS VAL          
SEQRES  41 1  751  ALA MET MET PRO ILE THR LEU GLY THR ALA ASP PHE MET          
SEQRES  42 1  751  VAL HIS HIS ILE HIS ALA PHE THR ILE HIS VAL THR ALA          
SEQRES  43 1  751  LEU ILE LEU LEU LYS GLY VAL LEU TYR ALA ARG SER SER          
SEQRES  44 1  751  ARG LEU VAL PRO ASP LYS ALA ASN LEU GLY PHE ARG PHE          
SEQRES  45 1  751  PRO CYS ASP GLY PRO GLY ARG GLY GLY THR CYS GLN VAL          
SEQRES  46 1  751  SER GLY TRP ASP HIS VAL PHE LEU GLY LEU PHE TRP MET          
SEQRES  47 1  751  TYR ASN SER LEU SER ILE VAL ILE PHE HIS PHE SER TRP          
SEQRES  48 1  751  LYS MET GLN SER ASP VAL TRP GLY THR VAL SER PRO ASP          
SEQRES  49 1  751  GLY SER VAL THR HIS VAL THR LEU GLY ASN PHE ALA GLN          
SEQRES  50 1  751  SER ALA ILE THR ILE ASN GLY TRP LEU ARG ASP PHE LEU          
SEQRES  51 1  751  TRP ALA GLN ALA ALA ASN VAL ILE ASN SER TYR GLY SER          
SEQRES  52 1  751  ALA LEU SER ALA TYR GLY ILE MET PHE LEU ALA GLY HIS          
SEQRES  53 1  751  PHE VAL PHE ALA PHE SER LEU MET PHE LEU PHE SER GLY          
SEQRES  54 1  751  ARG GLY TYR TRP GLN GLU LEU ILE GLU SER ILE VAL TRP          
SEQRES  55 1  751  ALA HIS ASN LYS LEU ASN VAL ALA PRO ALA ILE GLN PRO          
SEQRES  56 1  751  ARG ALA LEU SER ILE ILE GLN GLY ARG ALA VAL GLY VAL          
SEQRES  57 1  751  ALA HIS TYR LEU LEU GLY GLY ILE VAL THR THR TRP ALA          
SEQRES  58 1  751  PHE PHE LEU ALA ARG SER LEU SER ILE GLY                      
SEQRES   1 2  731  MET ALA THR LYS PHE PRO LYS PHE SER GLN ASP LEU ALA          
SEQRES   2 2  731  GLN ASP PRO THR THR ARG ARG ILE TRP TYR GLY ILE ALA          
SEQRES   3 2  731  THR ALA HIS ASP PHE GLU THR HIS ASP GLY MET THR GLU          
SEQRES   4 2  731  GLU ASN LEU TYR GLN LYS ILE PHE ALA SER HIS PHE GLY          
SEQRES   5 2  731  HIS ILE ALA ILE ILE PHE LEU TRP THR SER GLY THR LEU          
SEQRES   6 2  731  PHE HIS VAL ALA TRP GLN GLY ASN PHE GLU GLN TRP ILE          
SEQRES   7 2  731  LYS ASP PRO LEU ASN ILE ARG PRO ILE ALA HIS ALA ILE          
SEQRES   8 2  731  TRP ASP PRO HIS PHE GLY GLU GLY ALA VAL ASN ALA PHE          
SEQRES   9 2  731  THR GLN ALA GLY ALA SER ASN PRO VAL ASN ILE ALA TYR          
SEQRES  10 2  731  SER GLY VAL TYR HIS TRP PHE TYR THR ILE GLY MET THR          
SEQRES  11 2  731  THR ASN GLN GLU LEU TYR SER GLY ALA VAL PHE LEU LEU          
SEQRES  12 2  731  VAL LEU ALA SER LEU PHE LEU PHE ALA GLY TRP LEU HIS          
SEQRES  13 2  731  LEU GLN PRO LYS PHE ARG PRO SER LEU ALA TRP PHE LYS          
SEQRES  14 2  731  ASN ALA GLU SER ARG LEU ASN HIS HIS LEU ALA GLY LEU          
SEQRES  15 2  731  PHE GLY VAL SER SER LEU ALA TRP ALA GLY HIS LEU VAL          
SEQRES  16 2  731  HIS VAL ALA ILE PRO GLU ALA ARG GLY GLN HIS VAL GLY          
SEQRES  17 2  731  TRP ASP ASN PHE LEU SER THR PRO PRO HIS PRO ALA GLY          
SEQRES  18 2  731  LEU MET PRO PHE PHE THR GLY ASN TRP GLY VAL TYR ALA          
SEQRES  19 2  731  ALA ASP PRO ASP THR ALA GLY HIS ILE PHE GLY THR SER          
SEQRES  20 2  731  GLU GLY ALA GLY THR ALA ILE LEU THR PHE LEU GLY GLY          
SEQRES  21 2  731  PHE HIS PRO GLN THR GLU SER LEU TRP LEU THR ASP ILE          
SEQRES  22 2  731  ALA HIS HIS HIS LEU ALA ILE ALA VAL ILE PHE ILE ILE          
SEQRES  23 2  731  ALA GLY HIS MET TYR ARG THR ASN TRP GLY ILE GLY HIS          
SEQRES  24 2  731  SER ILE LYS GLU ILE LEU ASN ALA HIS LYS GLY PRO LEU          
SEQRES  25 2  731  THR GLY ALA GLY HIS THR ASN LEU TYR ASP THR ILE ASN          
SEQRES  26 2  731  ASN SER LEU HIS PHE GLN LEU GLY LEU ALA LEU ALA SER          
SEQRES  27 2  731  LEU GLY VAL ILE THR SER LEU VAL ALA GLN HIS MET TYR          
SEQRES  28 2  731  SER LEU PRO SER TYR ALA PHE ILE ALA GLN ASP HIS THR          
SEQRES  29 2  731  THR GLN ALA ALA LEU TYR THR HIS HIS GLN TYR ILE ALA          
SEQRES  30 2  731  GLY PHE LEU MET VAL GLY ALA PHE ALA HIS GLY ALA ILE          
SEQRES  31 2  731  PHE PHE VAL ARG ASP TYR ASP PRO VAL ALA ASN LYS ASP          
SEQRES  32 2  731  ASN VAL LEU ALA ARG MET LEU GLU HIS LYS GLU ALA LEU          
SEQRES  33 2  731  ILE SER HIS LEU SER TRP VAL SER LEU PHE LEU GLY PHE          
SEQRES  34 2  731  HIS THR LEU GLY LEU TYR VAL HIS ASN ASP VAL VAL VAL          
SEQRES  35 2  731  ALA PHE GLY THR PRO GLU LYS GLN ILE LEU ILE GLU PRO          
SEQRES  36 2  731  VAL PHE ALA GLN TRP ILE GLN ALA THR SER GLY LYS ALA          
SEQRES  37 2  731  LEU TYR GLY PHE ASP VAL LEU LEU SER ASN PRO ASP SER          
SEQRES  38 2  731  ILE ALA SER THR THR GLY ALA ALA TRP LEU PRO GLY TRP          
SEQRES  39 2  731  LEU ASP ALA ILE ASN SER GLY THR ASN SER LEU PHE LEU          
SEQRES  40 2  731  THR ILE GLY PRO GLY ASP PHE LEU VAL HIS HIS ALA ILE          
SEQRES  41 2  731  ALA LEU GLY LEU HIS THR THR ALA LEU ILE LEU ILE LYS          
SEQRES  42 2  731  GLY ALA LEU ASP ALA ARG GLY SER LYS LEU MET PRO ASP          
SEQRES  43 2  731  LYS LYS ASP PHE GLY TYR SER PHE PRO CYS ASP GLY PRO          
SEQRES  44 2  731  GLY ARG GLY GLY THR CYS ASP ILE SER ALA TRP ASP ALA          
SEQRES  45 2  731  PHE TYR LEU ALA MET PHE TRP MET LEU ASN THR LEU GLY          
SEQRES  46 2  731  TRP LEU THR PHE TYR TRP HIS TRP LYS HIS LEU GLY VAL          
SEQRES  47 2  731  TRP SER GLY ASN VAL ALA GLN PHE ASN GLU ASN SER THR          
SEQRES  48 2  731  TYR LEU MET GLY TRP PHE ARG ASP TYR LEU TRP ALA ASN          
SEQRES  49 2  731  SER ALA GLN LEU ILE ASN GLY TYR ASN PRO TYR GLY VAL          
SEQRES  50 2  731  ASN ASN LEU SER VAL TRP ALA TRP MET PHE LEU PHE GLY          
SEQRES  51 2  731  HIS LEU VAL TRP ALA THR GLY PHE MET PHE LEU ILE SER          
SEQRES  52 2  731  TRP ARG GLY TYR TRP GLN GLU LEU ILE GLU THR ILE VAL          
SEQRES  53 2  731  TRP ALA HIS GLU ARG THR PRO LEU ALA ASN LEU VAL ARG          
SEQRES  54 2  731  TRP LYS ASP LYS PRO VAL ALA LEU SER ILE VAL GLN ALA          
SEQRES  55 2  731  ARG LEU VAL GLY LEU ALA HIS PHE THR VAL GLY TYR VAL          
SEQRES  56 2  731  LEU THR TYR ALA ALA PHE LEU ILE ALA SER THR ALA GLY          
SEQRES  57 2  731  LYS PHE GLY                                                  
SEQRES   1 3   81  MET SER HIS SER VAL LYS ILE TYR ASP THR CYS ILE GLY          
SEQRES   2 3   81  CYS THR GLN CYS VAL ARG ALA CYS PRO LEU ASP VAL LEU          
SEQRES   3 3   81  GLU MET VAL PRO TRP ASP GLY CYS LYS ALA ALA GLN ILE          
SEQRES   4 3   81  ALA SER SER PRO ARG THR GLU ASP CYS VAL GLY CYS LYS          
SEQRES   5 3   81  ARG CYS GLU THR ALA CYS PRO THR ASP PHE LEU SER ILE          
SEQRES   6 3   81  ARG VAL TYR LEU GLY ALA GLU THR THR ARG SER MET GLY          
SEQRES   7 3   81  LEU ALA TYR                                                  
SEQRES   1 4  141  MET THR GLU LEU SER GLY GLN PRO PRO LYS PHE GLY GLY          
SEQRES   2 4  141  SER THR GLY GLY LEU LEU SER LYS ALA ASN ARG GLU GLU          
SEQRES   3 4  141  LYS TYR ALA ILE THR TRP THR SER ALA SER GLU GLN VAL          
SEQRES   4 4  141  PHE GLU MET PRO THR GLY GLY ALA ALA ILE MET ASN GLU          
SEQRES   5 4  141  GLY GLU ASN LEU LEU TYR LEU ALA ARG LYS GLU GLN CYS          
SEQRES   6 4  141  LEU ALA LEU GLY THR GLN LEU ARG THR LYS PHE LYS PRO          
SEQRES   7 4  141  LYS ILE GLN ASP TYR LYS ILE TYR ARG VAL TYR PRO SER          
SEQRES   8 4  141  GLY GLU VAL GLN TYR LEU HIS PRO ALA ASP GLY VAL PHE          
SEQRES   9 4  141  PRO GLU LYS VAL ASN GLU GLY ARG GLU ALA GLN GLY THR          
SEQRES  10 4  141  LYS THR ARG ARG ILE GLY GLN ASN PRO GLU PRO VAL THR          
SEQRES  11 4  141  ILE LYS PHE SER GLY LYS ALA PRO TYR GLU VAL                  
SEQRES   1 5   74  MET ALA LEU ASN ARG GLY ASP LYS VAL ARG ILE LYS ARG          
SEQRES   2 5   74  THR GLU SER TYR TRP TYR GLY ASP VAL GLY THR VAL ALA          
SEQRES   3 5   74  SER VAL GLU LYS SER GLY ILE LEU TYR PRO VAL ILE VAL          
SEQRES   4 5   74  ARG PHE ASP ARG VAL ASN TYR ASN GLY PHE SER GLY SER          
SEQRES   5 5   74  ALA SER GLY VAL ASN THR ASN ASN PHE ALA GLU ASN GLU          
SEQRES   6 5   74  LEU GLU LEU VAL GLN ALA ALA ALA LYS                          
SEQRES   1 6  125  MET ASP GLY LEU LYS SER PHE LEU SER THR ALA PRO VAL          
SEQRES   2 6  125  MET ILE MET ALA LEU LEU THR PHE THR ALA GLY ILE LEU          
SEQRES   3 6  125  ILE GLU PHE ASN ALA PHE TYR PRO ASP LEU LEU PHE HIS          
SEQRES   4 6  125  PRO CYS SER CYS ALA GLY ASP PHE LEU ILE PRO SER ILE          
SEQRES   5 6  125  ILE PHE LEU TYR ILE ALA GLY TRP ILE GLY TRP VAL GLY          
SEQRES   6 6  125  ARG SER TYR LEU ILE GLU ILE ARG GLU SER LYS ASN PRO          
SEQRES   7 6  125  GLU MET GLN GLU VAL VAL ILE ASN VAL PRO LEU ALA ILE          
SEQRES   8 6  125  LYS LYS MET LEU GLY GLY PHE LEU TRP PRO LEU ALA ALA          
SEQRES   9 6  125  VAL GLY GLU TYR THR SER GLY LYS LEU VAL MET LYS ASP          
SEQRES  10 6  125  SER GLU ILE PRO THR SER PRO ARG                              
SEQRES   1 9   40  MET ASP GLY SER TYR ALA ALA SER TYR LEU PRO TRP ILE          
SEQRES   2 9   40  LEU ILE PRO MET VAL GLY TRP LEU PHE PRO ALA VAL THR          
SEQRES   3 9   40  MET GLY LEU LEU PHE ILE HIS ILE GLU SER GLU GLY GLU          
SEQRES   4 9   40  GLY                                                          
SEQRES   1 8  157  MET ALA GLU SER ASN GLN VAL VAL GLN ALA TYR ASN GLY          
SEQRES   2 8  157  ASP PRO PHE VAL GLY HIS LEU SER THR PRO ILE SER ASP          
SEQRES   3 8  157  SER ALA PHE THR ARG THR PHE ILE GLY ASN LEU PRO ALA          
SEQRES   4 8  157  TYR ARG LYS GLY LEU SER PRO ILE LEU ARG GLY LEU GLU          
SEQRES   5 8  157  VAL GLY MET ALA HIS GLY TYR PHE LEU ILE GLY PRO TRP          
SEQRES   6 8  157  THR LEU LEU GLY PRO LEU ARG ASP SER GLU TYR GLN TYR          
SEQRES   7 8  157  ILE GLY GLY LEU ILE GLY ALA LEU ALA LEU ILE LEU VAL          
SEQRES   8 8  157  ALA THR ALA ALA LEU SER SER TYR GLY LEU VAL THR PHE          
SEQRES   9 8  157  GLN GLY GLU GLN GLY SER GLY ASP THR LEU GLN THR ALA          
SEQRES  10 8  157  ASP GLY TRP SER GLN PHE ALA ALA GLY PHE PHE VAL GLY          
SEQRES  11 8  157  GLY MET GLY GLY ALA PHE VAL ALA TYR PHE LEU LEU GLU          
SEQRES  12 8  157  ASN LEU SER VAL VAL ASP GLY ILE PHE ARG GLY LEU PHE          
SEQRES  13 8  157  ASN                                                          
SEQRES   1 7   31  MET ALA LEU SER ASP THR GLN ILE LEU ALA ALA LEU VAL          
SEQRES   2 7   31  VAL ALA LEU LEU PRO ALA PHE LEU ALA PHE ARG LEU SER          
SEQRES   3 7   31  THR GLU LEU TYR LYS                                          
SEQRES   1 K  128  MET THR ALA ILE ALA ARG GLU ARG GLY ARG SER LYS ARG          
SEQRES   2 K  128  GLY ILE ALA LEU HIS ARG LEU GLU TYR LEU LYS GLU ASN          
SEQRES   3 K  128  GLN VAL PHE GLU ILE ILE PHE GLY GLU PRO LEU SER MET          
SEQRES   4 K  128  PHE ASN THR ALA LEU LEU LEU ALA GLN ALA SER PRO THR          
SEQRES   5 K  128  THR ALA GLY TRP SER LEU SER VAL GLY ILE ILE MET CYS          
SEQRES   6 K  128  LEU CYS ASN VAL PHE ALA PHE VAL ILE GLY TYR PHE ALA          
SEQRES   7 K  128  ILE GLN LYS THR GLY LYS GLY LYS ASP LEU ALA LEU PRO          
SEQRES   8 K  128  GLN LEU ALA SER LYS LYS THR PHE GLY LEU PRO GLU LEU          
SEQRES   9 K  128  LEU ALA THR MET SER PHE GLY HIS ILE LEU GLY ALA GLY          
SEQRES  10 K  128  MET VAL LEU GLY LEU ALA SER SER GLY ILE LEU                  
SEQRES   1 I   40  MET ASP GLY SER TYR ALA ALA SER TYR LEU PRO TRP ILE          
SEQRES   2 I   40  LEU ILE PRO MET VAL GLY TRP LEU PHE PRO ALA VAL THR          
SEQRES   3 I   40  MET GLY LEU LEU PHE ILE HIS ILE GLU SER GLU GLY GLU          
SEQRES   4 I   40  GLY                                                          
SEQRES   1 k  128  MET THR ALA ILE ALA ARG GLU ARG GLY ARG SER LYS ARG          
SEQRES   2 k  128  GLY ILE ALA LEU HIS ARG LEU GLU TYR LEU LYS GLU ASN          
SEQRES   3 k  128  GLN VAL PHE GLU ILE ILE PHE GLY GLU PRO LEU SER MET          
SEQRES   4 k  128  PHE ASN THR ALA LEU LEU LEU ALA GLN ALA SER PRO THR          
SEQRES   5 k  128  THR ALA GLY TRP SER LEU SER VAL GLY ILE ILE MET CYS          
SEQRES   6 k  128  LEU CYS ASN VAL PHE ALA PHE VAL ILE GLY TYR PHE ALA          
SEQRES   7 k  128  ILE GLN LYS THR GLY LYS GLY LYS ASP LEU ALA LEU PRO          
SEQRES   8 k  128  GLN LEU ALA SER LYS LYS THR PHE GLY LEU PRO GLU LEU          
SEQRES   9 k  128  LEU ALA THR MET SER PHE GLY HIS ILE LEU GLY ALA GLY          
SEQRES  10 k  128  MET VAL LEU GLY LEU ALA SER SER GLY ILE LEU                  
SEQRES   1 0  128  MET THR ALA ILE ALA ARG GLU ARG GLY ARG SER LYS ARG          
SEQRES   2 0  128  GLY ILE ALA LEU HIS ARG LEU GLU TYR LEU LYS GLU ASN          
SEQRES   3 0  128  GLN VAL PHE GLU ILE ILE PHE GLY GLU PRO LEU SER MET          
SEQRES   4 0  128  PHE ASN THR ALA LEU LEU LEU ALA GLN ALA SER PRO THR          
SEQRES   5 0  128  THR ALA GLY TRP SER LEU SER VAL GLY ILE ILE MET CYS          
SEQRES   6 0  128  LEU CYS ASN VAL PHE ALA PHE VAL ILE GLY TYR PHE ALA          
SEQRES   7 0  128  ILE GLN LYS THR GLY LYS GLY LYS ASP LEU ALA LEU PRO          
SEQRES   8 0  128  GLN LEU ALA SER LYS LYS THR PHE GLY LEU PRO GLU LEU          
SEQRES   9 0  128  LEU ALA THR MET SER PHE GLY HIS ILE LEU GLY ALA GLY          
SEQRES  10 0  128  MET VAL LEU GLY LEU ALA SER SER GLY ILE LEU                  
HET    CLA  A1801      52                                                       
HET    PQN  A2001      33                                                       
HET    SF4  A3001       8                                                       
HET    BCR  A4001      40                                                       
HET    BCR  A4002      40                                                       
HET    BCR  A4003      40                                                       
HET    BCR  A4007      40                                                       
HET    BCR  A4008      40                                                       
HET    LHG  A5001      49                                                       
HET    LHG  A5003      49                                                       
HET    CLA  A1237      55                                                       
HET    CLA  A1022      65                                                       
HET    CLA  A1101      65                                                       
HET    CLA  A1102      65                                                       
HET    CLA  A1103      65                                                       
HET    CLA  A1104      65                                                       
HET    CLA  A1105      48                                                       
HET    CLA  A1106      65                                                       
HET    CLA  A1107      65                                                       
HET    CLA  A1108      45                                                       
HET    CLA  A1109      65                                                       
HET    CLA  A1110      54                                                       
HET    CLA  A1111      60                                                       
HET    CLA  A1112      45                                                       
HET    CLA  A1113      45                                                       
HET    CLA  A1115      46                                                       
HET    CLA  A1116      54                                                       
HET    CLA  A1117      65                                                       
HET    CLA  A1118      61                                                       
HET    CLA  A1119      65                                                       
HET    CLA  A1122      59                                                       
HET    CLA  A1123      65                                                       
HET    CLA  A1124      55                                                       
HET    CLA  A1125      52                                                       
HET    CLA  A1126      65                                                       
HET    CLA  A1127      65                                                       
HET    CLA  A1128      65                                                       
HET    CLA  A1130      46                                                       
HET    CLA  A1131      65                                                       
HET    CLA  A1137      65                                                       
HET    CLA  A1138      46                                                       
HET    CLA  A1139      50                                                       
HET    CLA  A1140      65                                                       
HET    CLA  A1011      65                                                       
HET    CLA  A1012      65                                                       
HET    CLA  A1114      46                                                       
HET    CLA  A1120      46                                                       
HET    CLA  A1121      46                                                       
HET    CLA  A1129      46                                                       
HET    CLA  A1132      65                                                       
HET    CLA  A1133      46                                                       
HET    CLA  A1134      46                                                       
HET    CLA  A1135      51                                                       
HET    CLA  A1136      46                                                       
HET    PQN  B2002      33                                                       
HET    BCR  B4004      40                                                       
HET    BCR  B4005      40                                                       
HET    BCR  B4006      40                                                       
HET    BCR  B4009      40                                                       
HET    BCR  B4010      40                                                       
HET    BCR  B4011      40                                                       
HET    BCR  B4014      40                                                       
HET    BCR  B4017      40                                                       
HET    LMG  B5002      55                                                       
HET    LHG  B5004      49                                                       
HET    CLA  B1013      65                                                       
HET    CLA  B1021      65                                                       
HET    CLA  B1023      65                                                       
HET    CLA  B1201      54                                                       
HET    CLA  B1202      65                                                       
HET    CLA  B1203      65                                                       
HET    CLA  B1204      65                                                       
HET    CLA  B1205      55                                                       
HET    CLA  B1207      65                                                       
HET    CLA  B1208      45                                                       
HET    CLA  B1209      45                                                       
HET    CLA  B1210      65                                                       
HET    CLA  B1212      45                                                       
HET    CLA  B1213      65                                                       
HET    CLA  B1214      59                                                       
HET    CLA  B1215      65                                                       
HET    CLA  B1216      65                                                       
HET    CLA  B1217      47                                                       
HET    CLA  B1218      45                                                       
HET    CLA  B1219      55                                                       
HET    CLA  B1220      46                                                       
HET    CLA  B1221      54                                                       
HET    CLA  B1222      56                                                       
HET    CLA  B1223      65                                                       
HET    CLA  B1224      55                                                       
HET    CLA  B1225      65                                                       
HET    CLA  B1226      65                                                       
HET    CLA  B1227      45                                                       
HET    CLA  B1228      50                                                       
HET    CLA  B1229      65                                                       
HET    CLA  B1230      58                                                       
HET    CLA  B1231      45                                                       
HET    CLA  B1232      45                                                       
HET    CLA  B1234      60                                                       
HET    CLA  B1235      60                                                       
HET    CLA  B1236      47                                                       
HET    CLA  B1240      45                                                       
HET    CLA  B1206      65                                                       
HET    CLA  B1211      46                                                       
HET    CLA  B1238      65                                                       
HET    CLA  B1239      46                                                       
HET    SF4  C3002       8                                                       
HET    SF4  C3003       8                                                       
HET    BCR  F4018      40                                                       
HET    BCR  F4020      40                                                       
HET    BCR  F4013      40                                                       
HET    CLA  L1501      65                                                       
HET    CLA  L1502      46                                                       
HET    CLA  L1503      65                                                       
HET    BCR  L4019      40                                                       
HET    BCR  L4022      40                                                       
HET    BCR  M4021      40                                                       
HET    CLA  a1801      52                                                       
HET    PQN  a2001      33                                                       
HET    SF4  a3001       8                                                       
HET    BCR  a4001      40                                                       
HET    BCR  a4002      40                                                       
HET    BCR  a4003      40                                                       
HET    BCR  a4007      40                                                       
HET    BCR  a4008      40                                                       
HET    LHG  a5001      49                                                       
HET    LHG  a5003      49                                                       
HET    CLA  a1237      55                                                       
HET    CLA  a1022      65                                                       
HET    CLA  a1101      65                                                       
HET    CLA  a1102      65                                                       
HET    CLA  a1103      65                                                       
HET    CLA  a1104      65                                                       
HET    CLA  a1105      48                                                       
HET    CLA  a1106      65                                                       
HET    CLA  a1107      65                                                       
HET    CLA  a1108      45                                                       
HET    CLA  a1109      65                                                       
HET    CLA  a1110      54                                                       
HET    CLA  a1111      60                                                       
HET    CLA  a1112      45                                                       
HET    CLA  a1113      45                                                       
HET    CLA  a1115      46                                                       
HET    CLA  a1116      54                                                       
HET    CLA  a1117      65                                                       
HET    CLA  a1118      61                                                       
HET    CLA  a1119      65                                                       
HET    CLA  a1122      59                                                       
HET    CLA  a1123      65                                                       
HET    CLA  a1124      55                                                       
HET    CLA  a1125      52                                                       
HET    CLA  a1126      65                                                       
HET    CLA  a1127      65                                                       
HET    CLA  a1128      65                                                       
HET    CLA  a1130      46                                                       
HET    CLA  a1131      65                                                       
HET    CLA  a1137      65                                                       
HET    CLA  a1138      46                                                       
HET    CLA  a1139      50                                                       
HET    CLA  a1140      65                                                       
HET    CLA  a1011      65                                                       
HET    CLA  a1012      65                                                       
HET    CLA  a1114      46                                                       
HET    CLA  a1120      46                                                       
HET    CLA  a1121      46                                                       
HET    CLA  a1129      46                                                       
HET    CLA  a1132      65                                                       
HET    CLA  a1133      46                                                       
HET    CLA  a1134      46                                                       
HET    CLA  a1135      51                                                       
HET    CLA  a1136      46                                                       
HET    PQN  b2002      33                                                       
HET    BCR  b4004      40                                                       
HET    BCR  b4005      40                                                       
HET    BCR  b4006      40                                                       
HET    BCR  b4009      40                                                       
HET    BCR  b4010      40                                                       
HET    BCR  b4011      40                                                       
HET    BCR  b4014      40                                                       
HET    BCR  b4017      40                                                       
HET    LMG  b5002      55                                                       
HET    LHG  b5004      49                                                       
HET    CLA  b1013      65                                                       
HET    CLA  b1021      65                                                       
HET    CLA  b1023      65                                                       
HET    CLA  b1201      54                                                       
HET    CLA  b1202      65                                                       
HET    CLA  b1203      65                                                       
HET    CLA  b1204      65                                                       
HET    CLA  b1205      55                                                       
HET    CLA  b1207      65                                                       
HET    CLA  b1208      45                                                       
HET    CLA  b1209      45                                                       
HET    CLA  b1210      65                                                       
HET    CLA  b1212      45                                                       
HET    CLA  b1213      65                                                       
HET    CLA  b1214      59                                                       
HET    CLA  b1215      65                                                       
HET    CLA  b1216      65                                                       
HET    CLA  b1217      47                                                       
HET    CLA  b1218      45                                                       
HET    CLA  b1219      55                                                       
HET    CLA  b1220      46                                                       
HET    CLA  b1221      54                                                       
HET    CLA  b1222      56                                                       
HET    CLA  b1223      65                                                       
HET    CLA  b1224      55                                                       
HET    CLA  b1225      65                                                       
HET    CLA  b1226      65                                                       
HET    CLA  b1227      45                                                       
HET    CLA  b1228      50                                                       
HET    CLA  b1229      65                                                       
HET    CLA  b1230      58                                                       
HET    CLA  b1231      45                                                       
HET    CLA  b1232      45                                                       
HET    CLA  b1234      60                                                       
HET    CLA  b1235      60                                                       
HET    CLA  b1236      47                                                       
HET    CLA  b1240      45                                                       
HET    CLA  b1206      65                                                       
HET    CLA  b1211      46                                                       
HET    CLA  b1238      65                                                       
HET    CLA  b1239      46                                                       
HET    SF4  c3002       8                                                       
HET    SF4  c3003       8                                                       
HET    BCR  f4018      40                                                       
HET    BCR  f4020      40                                                       
HET    BCR  f4013      40                                                       
HET    CLA  l1501      65                                                       
HET    CLA  l1502      46                                                       
HET    CLA  l1503      65                                                       
HET    BCR  l4019      40                                                       
HET    BCR  l4022      40                                                       
HET    BCR  m4021      40                                                       
HET    CLA  11801      52                                                       
HET    PQN  12001      33                                                       
HET    SF4  13001       8                                                       
HET    BCR  14001      40                                                       
HET    BCR  14002      40                                                       
HET    BCR  14003      40                                                       
HET    BCR  14007      40                                                       
HET    BCR  14008      40                                                       
HET    LHG  15001      49                                                       
HET    LHG  15003      49                                                       
HET    CLA  11237      55                                                       
HET    CLA  11022      65                                                       
HET    CLA  11101      65                                                       
HET    CLA  11102      65                                                       
HET    CLA  11103      65                                                       
HET    CLA  11104      65                                                       
HET    CLA  11105      48                                                       
HET    CLA  11106      65                                                       
HET    CLA  11107      65                                                       
HET    CLA  11108      45                                                       
HET    CLA  11109      65                                                       
HET    CLA  11110      54                                                       
HET    CLA  11111      60                                                       
HET    CLA  11112      45                                                       
HET    CLA  11113      45                                                       
HET    CLA  11115      46                                                       
HET    CLA  11116      54                                                       
HET    CLA  11117      65                                                       
HET    CLA  11118      61                                                       
HET    CLA  11119      65                                                       
HET    CLA  11122      59                                                       
HET    CLA  11123      65                                                       
HET    CLA  11124      55                                                       
HET    CLA  11125      52                                                       
HET    CLA  11126      65                                                       
HET    CLA  11127      65                                                       
HET    CLA  11128      65                                                       
HET    CLA  11130      46                                                       
HET    CLA  11131      65                                                       
HET    CLA  11137      65                                                       
HET    CLA  11138      46                                                       
HET    CLA  11139      50                                                       
HET    CLA  11140      65                                                       
HET    CLA  11011      65                                                       
HET    CLA  11012      65                                                       
HET    CLA  11114      46                                                       
HET    CLA  11120      46                                                       
HET    CLA  11121      46                                                       
HET    CLA  11129      46                                                       
HET    CLA  11132      65                                                       
HET    CLA  11133      46                                                       
HET    CLA  11134      46                                                       
HET    CLA  11135      51                                                       
HET    CLA  11136      46                                                       
HET    PQN  22002      33                                                       
HET    BCR  24004      40                                                       
HET    BCR  24005      40                                                       
HET    BCR  24006      40                                                       
HET    BCR  24009      40                                                       
HET    BCR  24010      40                                                       
HET    BCR  24011      40                                                       
HET    BCR  24014      40                                                       
HET    BCR  24017      40                                                       
HET    LMG  25002      55                                                       
HET    LHG  25004      49                                                       
HET    CLA  21013      65                                                       
HET    CLA  21021      65                                                       
HET    CLA  21023      65                                                       
HET    CLA  21201      54                                                       
HET    CLA  21202      65                                                       
HET    CLA  21203      65                                                       
HET    CLA  21204      65                                                       
HET    CLA  21205      55                                                       
HET    CLA  21206      65                                                       
HET    CLA  21207      65                                                       
HET    CLA  21208      45                                                       
HET    CLA  21209      45                                                       
HET    CLA  21210      65                                                       
HET    CLA  21212      45                                                       
HET    CLA  21213      65                                                       
HET    CLA  21214      59                                                       
HET    CLA  21215      65                                                       
HET    CLA  21216      65                                                       
HET    CLA  21217      47                                                       
HET    CLA  21218      45                                                       
HET    CLA  21219      55                                                       
HET    CLA  21220      46                                                       
HET    CLA  21221      54                                                       
HET    CLA  21222      56                                                       
HET    CLA  21223      65                                                       
HET    CLA  21224      55                                                       
HET    CLA  21225      65                                                       
HET    CLA  21226      65                                                       
HET    CLA  21227      45                                                       
HET    CLA  21228      50                                                       
HET    CLA  21229      65                                                       
HET    CLA  21230      58                                                       
HET    CLA  21231      45                                                       
HET    CLA  21232      45                                                       
HET    CLA  21234      60                                                       
HET    CLA  21235      60                                                       
HET    CLA  21236      47                                                       
HET    CLA  21240      45                                                       
HET    CLA  21211      46                                                       
HET    CLA  21238      65                                                       
HET    CLA  21239      46                                                       
HET    SF4  33002       8                                                       
HET    SF4  33003       8                                                       
HET    BCR  64018      40                                                       
HET    BCR  64020      40                                                       
HET    BCR  64013      40                                                       
HET    CLA  81501      65                                                       
HET    CLA  81502      46                                                       
HET    CLA  81503      65                                                       
HET    BCR  84019      40                                                       
HET    BCR  84022      40                                                       
HET    BCR  74021      40                                                       
HET    CLA  K1401      65                                                       
HET    CLA  K1402      50                                                       
HET    CLA  k1401      65                                                       
HET    CLA  k1402      50                                                       
HET    CLA  01401      65                                                       
HET    CLA  01402      50                                                       
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PQN PHYLLOQUINONE                                                    
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETSYN     PQN VITAMIN K1; 2-METHYL-3-PHYTYL-1,4-NAPHTHOQUINONE                 
FORMUL  31  CLA    273(C55 H72 MG N4 O5 2+)                                     
FORMUL  32  PQN    6(C31 H46 O2)                                                
FORMUL  33  SF4    9(FE4 S4)                                                    
FORMUL  34  BCR    57(C40 H56)                                                  
FORMUL  39  LHG    9(C38 H75 O10 P)                                             
FORMUL  94  LMG    3(C45 H86 O10)                                               
HELIX    1   1 GLU A   26  LYS A   30  5                                   5    
HELIX    2   2 THR A   45  ASN A   54  1                                  10    
HELIX    3   3 ASP A   57  THR A   62  1                                   6    
HELIX    4   4 ASP A   64  PHE A   97  1                                  34    
HELIX    5   5 ASN A   99  ASP A  106  1                                   8    
HELIX    6   6 GLY A  122  ASN A  127  5                                   6    
HELIX    7   7 GLY A  142  GLY A  151  1                                  10    
HELIX    8   8 ASP A  154  VAL A  182  1                                  29    
HELIX    9   9 LYS A  186  GLN A  191  1                                   6    
HELIX   10  10 ASN A  192  GLY A  203  1                                  12    
HELIX   11  11 LEU A  204  VAL A  219  1                                  16    
HELIX   12  12 VAL A  219  GLY A  230  1                                  12    
HELIX   13  13 HIS A  240  GLU A  245  1                                   6    
HELIX   14  14 GLU A  245  LEU A  252  1                                   8    
HELIX   15  15 TRP A  268  PHE A  274  5                                   7    
HELIX   16  16 TRP A  289  GLY A  308  1                                  20    
HELIX   17  17 SER A  320  ALA A  327  1                                   8    
HELIX   18  18 GLY A  330  GLY A  334  5                                   5    
HELIX   19  19 GLY A  339  LEU A  344  1                                   6    
HELIX   20  20 SER A  347  TYR A  371  1                                  25    
HELIX   21  21 ASP A  382  ASP A  415  1                                  34    
HELIX   22  22 ASP A  417  ASN A  421  5                                   5    
HELIX   23  23 ASN A  424  ARG A  431  1                                   8    
HELIX   24  24 HIS A  432  LEU A  464  1                                  33    
HELIX   25  25 PRO A  480  LEU A  492  1                                  13    
HELIX   26  26 GLY A  528  TYR A  555  1                                  28    
HELIX   27  27 ASP A  564  GLY A  569  1                                   6    
HELIX   28  28 GLY A  587  VAL A  617  1                                  31    
HELIX   29  29 ASN A  634  ALA A  639  1                                   6    
HELIX   30  30 THR A  641  PHE A  649  1                                   9    
HELIX   31  31 PHE A  649  ALA A  654  1                                   6    
HELIX   32  32 ALA A  654  ASN A  659  1                                   6    
HELIX   33  33 LEU A  665  SER A  688  1                                  24    
HELIX   34  34 GLY A  689  ASN A  708  1                                  20    
HELIX   35  35 SER A  719  GLY A  751  1                                  33    
HELIX   36  36 SER B    9  GLN B   14  1                                   6    
HELIX   37  37 THR B   18  THR B   27  1                                  10    
HELIX   38  38 ASP B   30  HIS B   34  5                                   5    
HELIX   39  39 GLU B   39  GLY B   72  1                                  34    
HELIX   40  40 ASN B   73  ILE B   78  1                                   6    
HELIX   41  41 GLY B   97  THR B  105  1                                   9    
HELIX   42  42 GLY B  119  GLY B  128  1                                  10    
HELIX   43  43 THR B  131  HIS B  156  1                                  26    
HELIX   44  44 SER B  164  ASN B  170  1                                   7    
HELIX   45  45 ASN B  170  GLY B  181  1                                  12    
HELIX   46  46 PHE B  183  VAL B  197  1                                  15    
HELIX   47  47 VAL B  197  ALA B  202  1                                   6    
HELIX   48  48 LEU B  222  GLY B  228  1                                   7    
HELIX   49  49 TRP B  230  ALA B  235  5                                   6    
HELIX   50  50 TRP B  269  GLY B  288  1                                  20    
HELIX   51  51 SER B  300  HIS B  308  1                                   9    
HELIX   52  52 ASN B  319  SER B  327  1                                   9    
HELIX   53  53 SER B  327  TYR B  351  1                                  25    
HELIX   54  54 ASP B  362  ASP B  395  1                                  34    
HELIX   55  55 ASN B  404  HIS B  412  1                                   9    
HELIX   56  56 HIS B  412  PHE B  444  1                                  33    
HELIX   57  57 THR B  446  GLN B  450  5                                   5    
HELIX   58  58 PRO B  455  SER B  465  1                                  11    
HELIX   59  59 VAL B  474  ASN B  478  5                                   5    
HELIX   60  60 TRP B  490  ASN B  499  1                                  10    
HELIX   61  61 GLY B  510  ASP B  537  1                                  28    
HELIX   62  62 ASP B  546  GLY B  551  1                                   6    
HELIX   63  63 SER B  568  TRP B  599  1                                  32    
HELIX   64  64 VAL B  603  SER B  610  1                                   8    
HELIX   65  65 TYR B  612  TYR B  620  1                                   9    
HELIX   66  66 LEU B  640  SER B  663  1                                  24    
HELIX   67  67 TRP B  664  THR B  682  1                                  19    
HELIX   68  68 SER B  698  PHE B  730  1                                  33    
HELIX   69  69 ARG C   44  CYS C   48  5                                   5    
HELIX   70  70 LYS C   52  CYS C   58  1                                   7    
HELIX   71 279 LEU D   19  GLU D   25  1                                   7    
HELIX   72 280 ARG D   61  ARG D   73  1                                  13    
HELIX   73 281 ARG D  121  ASN D  125  5                                   5    
HELIX   74  71 ALA E   62  ASN E   64  5                                   3    
HELIX   75  72 ASP F    2  SER F    9  1                                   8    
HELIX   76  73 PRO F   12  THR F   20  1                                   9    
HELIX   77  74 PHE F   21  PHE F   29  1                                   9    
HELIX   78  75 ILE F   52  LYS F   76  1                                  25    
HELIX   79  76 ASN F   77  VAL F   84  1                                   8    
HELIX   80  77 ASN F   86  GLY F   96  1                                  11    
HELIX   81  78 LEU F   99  SER F  110  1                                  12    
HELIX   82  79 SER L   27  LEU L   37  1                                  11    
HELIX   83  80 SER L   45  ILE L   62  1                                  18    
HELIX   84  81 ILE L   62  GLY L   69  1                                   8    
HELIX   85  82 PRO L   70  SER L   74  5                                   5    
HELIX   86  83 TYR L   76  PHE L  104  1                                  29    
HELIX   87  84 ASP L  112  GLN L  115  5                                   4    
HELIX   88  85 THR L  116  ASN L  144  1                                  29    
HELIX   89  86 ASN L  144  ARG L  153  1                                  10    
HELIX   90  87 SER M    4  LYS M   31  1                                  28    
HELIX   91  88 PHE a   25  LYS a   30  5                                   6    
HELIX   92  89 THR a   45  ASN a   54  1                                  10    
HELIX   93  90 ASP a   57  THR a   62  1                                   6    
HELIX   94  91 ASP a   64  PHE a   97  1                                  34    
HELIX   95  92 ASN a   99  ASP a  106  1                                   8    
HELIX   96  93 GLY a  122  ASN a  127  5                                   6    
HELIX   97  94 GLY a  142  GLY a  151  1                                  10    
HELIX   98  95 ASP a  154  VAL a  182  1                                  29    
HELIX   99  96 LYS a  186  GLN a  191  1                                   6    
HELIX  100  97 ASN a  192  GLY a  203  1                                  12    
HELIX  101  98 LEU a  204  VAL a  219  1                                  16    
HELIX  102  99 VAL a  219  GLY a  230  1                                  12    
HELIX  103 100 HIS a  240  GLU a  245  1                                   6    
HELIX  104 101 GLU a  245  LEU a  252  1                                   8    
HELIX  105 102 TRP a  268  PHE a  274  5                                   7    
HELIX  106 103 TRP a  289  GLY a  308  1                                  20    
HELIX  107 104 SER a  320  ALA a  327  1                                   8    
HELIX  108 105 GLY a  330  GLY a  334  5                                   5    
HELIX  109 106 GLY a  339  LEU a  344  1                                   6    
HELIX  110 107 SER a  347  TYR a  371  1                                  25    
HELIX  111 108 ASP a  382  ASP a  415  1                                  34    
HELIX  112 109 ASP a  417  ASN a  421  5                                   5    
HELIX  113 110 ASN a  424  ARG a  431  1                                   8    
HELIX  114 111 HIS a  432  LEU a  464  1                                  33    
HELIX  115 112 PRO a  480  LEU a  492  1                                  13    
HELIX  116 113 GLY a  528  TYR a  555  1                                  28    
HELIX  117 114 ASP a  564  GLY a  569  1                                   6    
HELIX  118 115 PRO a  577  GLY a  581  5                                   5    
HELIX  119 116 GLY a  587  VAL a  617  1                                  31    
HELIX  120 117 ASN a  634  ALA a  639  1                                   6    
HELIX  121 118 THR a  641  PHE a  649  1                                   9    
HELIX  122 119 PHE a  649  ALA a  654  1                                   6    
HELIX  123 120 ALA a  654  ASN a  659  1                                   6    
HELIX  124 121 LEU a  665  SER a  688  1                                  24    
HELIX  125 122 GLY a  689  LEU a  707  1                                  19    
HELIX  126 123 SER a  719  GLY a  751  1                                  33    
HELIX  127 124 SER b    9  GLN b   14  1                                   6    
HELIX  128 125 THR b   18  THR b   27  1                                  10    
HELIX  129 126 ASP b   30  HIS b   34  5                                   5    
HELIX  130 127 GLU b   39  GLY b   72  1                                  34    
HELIX  131 128 ASN b   73  ILE b   78  1                                   6    
HELIX  132 129 GLY b   97  THR b  105  1                                   9    
HELIX  133 130 GLY b  119  GLY b  128  1                                  10    
HELIX  134 131 THR b  131  HIS b  156  1                                  26    
HELIX  135 132 SER b  164  ASN b  170  1                                   7    
HELIX  136 133 ASN b  170  GLY b  181  1                                  12    
HELIX  137 134 PHE b  183  VAL b  197  1                                  15    
HELIX  138 135 VAL b  197  ALA b  202  1                                   6    
HELIX  139 136 LEU b  222  GLY b  228  1                                   7    
HELIX  140 137 TRP b  230  ALA b  235  5                                   6    
HELIX  141 138 TRP b  269  GLY b  288  1                                  20    
HELIX  142 139 SER b  300  ALA b  307  1                                   8    
HELIX  143 140 ASN b  319  SER b  327  1                                   9    
HELIX  144 141 SER b  327  TYR b  351  1                                  25    
HELIX  145 142 ASP b  362  ASP b  395  1                                  34    
HELIX  146 143 ASN b  404  HIS b  412  1                                   9    
HELIX  147 144 HIS b  412  PHE b  444  1                                  33    
HELIX  148 145 THR b  446  GLN b  450  5                                   5    
HELIX  149 146 PRO b  455  GLY b  466  1                                  12    
HELIX  150 147 VAL b  474  ASN b  478  5                                   5    
HELIX  151 148 TRP b  490  ASN b  499  1                                  10    
HELIX  152 149 GLY b  510  ASP b  537  1                                  28    
HELIX  153 150 ASP b  546  GLY b  551  5                                   6    
HELIX  154 151 SER b  568  TRP b  599  1                                  32    
HELIX  155 152 VAL b  603  SER b  610  1                                   8    
HELIX  156 153 TYR b  612  TYR b  620  1                                   9    
HELIX  157 154 LEU b  640  SER b  663  1                                  24    
HELIX  158 155 TRP b  664  THR b  682  1                                  19    
HELIX  159 156 SER b  698  PHE b  730  1                                  33    
HELIX  160 157 ARG c   44  CYS c   48  5                                   5    
HELIX  161 158 LYS c   52  CYS c   58  1                                   7    
HELIX  162 282 LEU d   19  GLU d   25  1                                   7    
HELIX  163 283 ARG d   61  ARG d   73  1                                  13    
HELIX  164 284 ARG d  121  ASN d  125  5                                   5    
HELIX  165 159 ALA e   62  ASN e   64  5                                   3    
HELIX  166 160 ASP f    2  THR f   10  1                                   9    
HELIX  167 161 THR f   10  THR f   20  1                                  11    
HELIX  168 162 THR f   20  PHE f   29  1                                  10    
HELIX  169 163 LEU f   48  LYS f   76  1                                  29    
HELIX  170 164 ASN f   77  VAL f   84  1                                   8    
HELIX  171 165 ASN f   86  GLY f   96  1                                  11    
HELIX  172 166 LEU f   99  SER f  110  1                                  12    
HELIX  173 167 TYR i    9  TRP i   20  1                                  12    
HELIX  174 168 TRP i   20  GLU i   35  1                                  16    
HELIX  175 169 SER l   27  LEU l   37  1                                  11    
HELIX  176 170 SER l   45  ILE l   62  1                                  18    
HELIX  177 171 ILE l   62  GLY l   69  1                                   8    
HELIX  178 172 PRO l   70  SER l   74  5                                   5    
HELIX  179 173 TYR l   76  PHE l  104  1                                  29    
HELIX  180 174 ASP l  112  GLN l  115  5                                   4    
HELIX  181 175 THR l  116  ASN l  144  1                                  29    
HELIX  182 176 ASN l  144  ARG l  153  1                                  10    
HELIX  183 177 SER m    4  ALA m   15  1                                  12    
HELIX  184 178 ALA m   15  LYS m   31  1                                  17    
HELIX  185 179 PHE 1   25  LYS 1   30  5                                   6    
HELIX  186 180 THR 1   45  ASN 1   54  1                                  10    
HELIX  187 181 ASP 1   57  THR 1   62  1                                   6    
HELIX  188 182 ASP 1   64  PHE 1   97  1                                  34    
HELIX  189 183 ASN 1   99  ASP 1  106  1                                   8    
HELIX  190 184 GLY 1  122  ASN 1  127  5                                   6    
HELIX  191 185 GLY 1  142  GLY 1  151  1                                  10    
HELIX  192 186 ASP 1  154  VAL 1  182  1                                  29    
HELIX  193 187 LYS 1  186  GLN 1  191  1                                   6    
HELIX  194 188 ASN 1  192  GLY 1  203  1                                  12    
HELIX  195 189 LEU 1  204  VAL 1  219  1                                  16    
HELIX  196 190 VAL 1  219  GLY 1  230  1                                  12    
HELIX  197 191 HIS 1  240  GLU 1  245  1                                   6    
HELIX  198 192 GLU 1  245  LEU 1  252  1                                   8    
HELIX  199 193 TRP 1  268  PHE 1  274  5                                   7    
HELIX  200 194 TRP 1  289  GLY 1  308  1                                  20    
HELIX  201 195 SER 1  320  ALA 1  327  1                                   8    
HELIX  202 196 GLY 1  330  GLY 1  334  5                                   5    
HELIX  203 197 GLY 1  339  LEU 1  344  1                                   6    
HELIX  204 198 SER 1  347  TYR 1  371  1                                  25    
HELIX  205 199 ASP 1  382  ASP 1  415  1                                  34    
HELIX  206 200 ASP 1  417  ASN 1  421  5                                   5    
HELIX  207 201 ASN 1  424  ARG 1  431  1                                   8    
HELIX  208 202 HIS 1  432  LEU 1  464  1                                  33    
HELIX  209 203 PRO 1  480  LEU 1  492  1                                  13    
HELIX  210 204 GLY 1  528  TYR 1  555  1                                  28    
HELIX  211 205 ASP 1  564  GLY 1  569  1                                   6    
HELIX  212 206 GLY 1  587  VAL 1  617  1                                  31    
HELIX  213 207 ASN 1  634  ALA 1  639  1                                   6    
HELIX  214 208 THR 1  641  PHE 1  649  1                                   9    
HELIX  215 209 PHE 1  649  ALA 1  654  1                                   6    
HELIX  216 210 ALA 1  654  ASN 1  659  1                                   6    
HELIX  217 211 LEU 1  665  PHE 1  687  1                                  23    
HELIX  218 212 GLY 1  689  LEU 1  707  1                                  19    
HELIX  219 213 SER 1  719  GLY 1  751  1                                  33    
HELIX  220 214 SER 2    9  GLN 2   14  1                                   6    
HELIX  221 215 THR 2   18  THR 2   27  1                                  10    
HELIX  222 216 ASP 2   30  HIS 2   34  5                                   5    
HELIX  223 217 THR 2   38  GLY 2   72  1                                  35    
HELIX  224 218 ASN 2   73  ILE 2   78  1                                   6    
HELIX  225 219 GLY 2   97  THR 2  105  1                                   9    
HELIX  226 220 GLY 2  119  GLY 2  128  1                                  10    
HELIX  227 221 THR 2  131  HIS 2  156  1                                  26    
HELIX  228 222 SER 2  164  ASN 2  170  1                                   7    
HELIX  229 223 ASN 2  170  GLY 2  181  1                                  12    
HELIX  230 224 PHE 2  183  VAL 2  197  1                                  15    
HELIX  231 225 VAL 2  197  ALA 2  202  1                                   6    
HELIX  232 226 LEU 2  222  GLY 2  228  1                                   7    
HELIX  233 227 TRP 2  230  ALA 2  235  5                                   6    
HELIX  234 228 TRP 2  269  GLY 2  288  1                                  20    
HELIX  235 229 SER 2  300  ALA 2  307  1                                   8    
HELIX  236 230 ASN 2  319  SER 2  327  1                                   9    
HELIX  237 231 SER 2  327  TYR 2  351  1                                  25    
HELIX  238 232 ASP 2  362  ASP 2  395  1                                  34    
HELIX  239 233 ASN 2  404  HIS 2  412  1                                   9    
HELIX  240 234 HIS 2  412  PHE 2  444  1                                  33    
HELIX  241 235 THR 2  446  GLN 2  450  5                                   5    
HELIX  242 236 PRO 2  455  GLY 2  466  1                                  12    
HELIX  243 237 VAL 2  474  ASN 2  478  5                                   5    
HELIX  244 238 TRP 2  490  ASN 2  499  1                                  10    
HELIX  245 239 GLY 2  510  ASP 2  537  1                                  28    
HELIX  246 240 ASP 2  546  GLY 2  551  1                                   6    
HELIX  247 241 SER 2  568  TRP 2  599  1                                  32    
HELIX  248 242 VAL 2  603  SER 2  610  1                                   8    
HELIX  249 243 TYR 2  612  TYR 2  620  1                                   9    
HELIX  250 244 LEU 2  640  SER 2  663  1                                  24    
HELIX  251 245 TRP 2  664  THR 2  682  1                                  19    
HELIX  252 246 SER 2  698  PHE 2  730  1                                  33    
HELIX  253 247 ARG 3   44  CYS 3   48  5                                   5    
HELIX  254 248 LYS 3   52  CYS 3   58  1                                   7    
HELIX  255 285 LEU 4   19  GLU 4   25  1                                   7    
HELIX  256 286 ARG 4   61  ARG 4   73  1                                  13    
HELIX  257 287 ARG 4  121  ASN 4  125  5                                   5    
HELIX  258 249 ALA 5   62  ASN 5   64  5                                   3    
HELIX  259 250 ASP 6    2  SER 6    9  1                                   8    
HELIX  260 251 THR 6   10  THR 6   20  1                                  11    
HELIX  261 252 THR 6   20  PHE 6   29  1                                  10    
HELIX  262 253 LEU 6   48  LYS 6   76  1                                  29    
HELIX  263 254 ASN 6   77  VAL 6   84  1                                   8    
HELIX  264 255 ASN 6   86  GLY 6   96  1                                  11    
HELIX  265 256 LEU 6   99  SER 6  110  1                                  12    
HELIX  266 257 TYR 9    9  TRP 9   20  1                                  12    
HELIX  267 258 TRP 9   20  GLU 9   35  1                                  16    
HELIX  268 259 SER 8   27  LEU 8   37  1                                  11    
HELIX  269 260 SER 8   45  LEU 8   61  1                                  17    
HELIX  270 261 ILE 8   62  GLY 8   69  1                                   8    
HELIX  271 262 PRO 8   70  SER 8   74  5                                   5    
HELIX  272 263 TYR 8   76  PHE 8  104  1                                  29    
HELIX  273 264 ASP 8  112  GLN 8  115  5                                   4    
HELIX  274 265 THR 8  116  ASN 8  144  1                                  29    
HELIX  275 266 ASN 8  144  ARG 8  153  1                                  10    
HELIX  276 267 SER 7    4  ALA 7   15  1                                  12    
HELIX  277 268 ALA 7   15  LYS 7   31  1                                  17    
HELIX  278 269 SER K   57  TYR K   76  1                                  20    
HELIX  279 270 LEU K   93  THR K   98  1                                   6    
HELIX  280 271 GLY K  100  SER K  125  1                                  26    
HELIX  281 272 TYR I    9  GLU I   35  1                                  27    
HELIX  282 273 SER k   57  TYR k   76  1                                  20    
HELIX  283 274 LEU k   93  THR k   98  1                                   6    
HELIX  284 275 GLY k  100  SER k  124  1                                  25    
HELIX  285 276 SER 0   57  TYR 0   76  1                                  20    
HELIX  286 277 LEU 0   93  THR 0   98  1                                   6    
HELIX  287 278 GLY 0  100  SER 0  124  1                                  25    
SHEET    1   A 2 VAL A  16  ASN A  18  0                                        
SHEET    2   A 2 LYS A 183  PRO A 185 -1  O  ALA A 184   N  ASP A  17           
SHEET    1   B 3 SER A 113  ALA A 114  0                                        
SHEET    2   B 3 HIS A 135  GLN A 138 -1  O  ILE A 137   N  ALA A 114           
SHEET    3   B 3 GLY A 128  ASP A 129 -1  N  GLY A 128   O  GLY A 136           
SHEET    1   C 2 ILE A 514  VAL A 516  0                                        
SHEET    2   C 2 LYS A 519  MET A 522 -1  O  LYS A 519   N  VAL A 516           
SHEET    1   D 2 THR A 620  VAL A 621  0                                        
SHEET    2   D 2 VAL A 627  THR A 628 -1  O  THR A 628   N  THR A 620           
SHEET    1   E 2 TYR B 632  ASN B 633  0                                        
SHEET    2   E 2 GLY B 636  VAL B 637 -1  O  GLY B 636   N  ASN B 633           
SHEET    1   F 2 SER C   4  ILE C   7  0                                        
SHEET    2   F 2 ILE C  65  TYR C  68 -1  O  TYR C  68   N  SER C   4           
SHEET    1   G 2 GLU C  27  PRO C  30  0                                        
SHEET    2   G 2 GLN C  38  SER C  41 -1  O  ILE C  39   N  VAL C  29           
SHEET    1   H 5 THR E  58  PHE E  61  0                                        
SHEET    2   H 5 VAL E  37  ARG E  40 -1  N  VAL E  37   O  PHE E  61           
SHEET    3   H 5 VAL E  22  VAL E  28 -1  N  THR E  24   O  ARG E  40           
SHEET    4   H 5 LYS E   8  ILE E  11 -1  N  VAL E   9   O  GLY E  23           
SHEET    5   H 5 LEU E  66  LEU E  68 -1  O  GLU E  67   N  ARG E  10           
SHEET    1   I 2 GLN L   9  ALA L  10  0                                        
SHEET    2   I 2 LEU L  20  SER L  21 -1  O  SER L  21   N  GLN L   9           
SHEET    1   J 2 VAL a  16  ASN a  18  0                                        
SHEET    2   J 2 LYS a 183  PRO a 185 -1  O  ALA a 184   N  ASP a  17           
SHEET    1   K 3 SER a 113  ALA a 114  0                                        
SHEET    2   K 3 HIS a 135  GLN a 138 -1  O  ILE a 137   N  ALA a 114           
SHEET    3   K 3 GLY a 128  ASP a 129 -1  N  GLY a 128   O  GLY a 136           
SHEET    1   L 2 ILE a 514  VAL a 516  0                                        
SHEET    2   L 2 LYS a 519  MET a 522 -1  O  LYS a 519   N  VAL a 516           
SHEET    1   M 2 THR a 620  VAL a 621  0                                        
SHEET    2   M 2 VAL a 627  THR a 628 -1  O  THR a 628   N  THR a 620           
SHEET    1   N 2 ILE b  87  ALA b  90  0                                        
SHEET    2   N 2 VAL b 113  ILE b 115 -1  O  ASN b 114   N  ALA b  88           
SHEET    1   O 2 TYR b 632  ASN b 633  0                                        
SHEET    2   O 2 GLY b 636  VAL b 637 -1  O  GLY b 636   N  ASN b 633           
SHEET    1   P 2 SER c   4  ILE c   7  0                                        
SHEET    2   P 2 ILE c  65  TYR c  68 -1  O  TYR c  68   N  SER c   4           
SHEET    1   Q 2 GLU c  27  PRO c  30  0                                        
SHEET    2   Q 2 GLN c  38  SER c  41 -1  O  ILE c  39   N  VAL c  29           
SHEET    1   R 5 THR e  58  PHE e  61  0                                        
SHEET    2   R 5 VAL e  37  ARG e  40 -1  N  VAL e  37   O  PHE e  61           
SHEET    3   R 5 VAL e  22  VAL e  28 -1  N  ALA e  26   O  ILE e  38           
SHEET    4   R 5 LYS e   8  ILE e  11 -1  N  VAL e   9   O  GLY e  23           
SHEET    5   R 5 LEU e  66  LEU e  68 -1  O  GLU e  67   N  ARG e  10           
SHEET    1   S 2 GLN l   9  ALA l  10  0                                        
SHEET    2   S 2 LEU l  20  SER l  21 -1  O  SER l  21   N  GLN l   9           
SHEET    1   T 2 VAL 1  16  ASN 1  18  0                                        
SHEET    2   T 2 LYS 1 183  PRO 1 185 -1  O  ALA 1 184   N  ASP 1  17           
SHEET    1   U 3 SER 1 113  ALA 1 114  0                                        
SHEET    2   U 3 HIS 1 135  GLN 1 138 -1  O  ILE 1 137   N  ALA 1 114           
SHEET    3   U 3 GLY 1 128  ASP 1 129 -1  N  GLY 1 128   O  GLY 1 136           
SHEET    1   V 2 ILE 1 514  VAL 1 516  0                                        
SHEET    2   V 2 LYS 1 519  MET 1 522 -1  O  LYS 1 519   N  VAL 1 516           
SHEET    1   W 2 THR 1 620  VAL 1 621  0                                        
SHEET    2   W 2 VAL 1 627  THR 1 628 -1  O  THR 1 628   N  THR 1 620           
SHEET    1   X 2 ILE 2  87  ALA 2  90  0                                        
SHEET    2   X 2 VAL 2 113  ILE 2 115 -1  O  ASN 2 114   N  ALA 2  88           
SHEET    1   Y 2 TYR 2 632  ASN 2 633  0                                        
SHEET    2   Y 2 GLY 2 636  VAL 2 637 -1  O  GLY 2 636   N  ASN 2 633           
SHEET    1   Z 3 ILE 3  65  TYR 3  68  0                                        
SHEET    2   Z 3 SER 3   4  TYR 3   8 -1  N  SER 3   4   O  TYR 3  68           
SHEET    3   Z 3 THR 4 117  LYS 4 118  1  O  LYS 4 118   N  ILE 3   7           
SHEET    1  AA 2 GLU 3  27  PRO 3  30  0                                        
SHEET    2  AA 2 GLN 3  38  SER 3  41 -1  O  ILE 3  39   N  VAL 3  29           
SHEET    1  AB 5 THR 5  58  PHE 5  61  0                                        
SHEET    2  AB 5 VAL 5  37  PHE 5  41 -1  N  VAL 5  37   O  PHE 5  61           
SHEET    3  AB 5 VAL 5  22  VAL 5  28 -1  N  ALA 5  26   O  ILE 5  38           
SHEET    4  AB 5 LYS 5   8  ILE 5  11 -1  N  VAL 5   9   O  GLY 5  23           
SHEET    5  AB 5 LEU 5  66  LEU 5  68 -1  O  GLU 5  67   N  ARG 5  10           
SHEET    1  AC 2 GLN 8   9  ALA 8  10  0                                        
SHEET    2  AC 2 LEU 8  20  SER 8  21 -1  O  SER 8  21   N  GLN 8   9           
SHEET    1  AD 4 GLY D  53  LEU D  59  0                                        
SHEET    2  AD 4 LYS D  27  SER D  34 -1  N  TYR D  28   O  LEU D  59           
SHEET    3  AD 4 LYS D  84  VAL D  88 -1  O  TYR D  86   N  ALA D  29           
SHEET    4  AD 4 VAL D  94  TYR D  96 -1  O  GLN D  95   N  ARG D  87           
SHEET    1  AE 2 VAL D  39  GLU D  41  0                                        
SHEET    2  AE 2 ALA D  47  ILE D  49 -1  O  ALA D  48   N  PHE D  40           
SHEET    1  AF 4 GLY d  53  LEU d  59  0                                        
SHEET    2  AF 4 LYS d  27  SER d  34 -1  N  TYR d  28   O  LEU d  59           
SHEET    3  AF 4 LYS d  84  VAL d  88 -1  O  TYR d  86   N  ALA d  29           
SHEET    4  AF 4 VAL d  94  TYR d  96 -1  O  GLN d  95   N  ARG d  87           
SHEET    1  AG 2 VAL d  39  GLU d  41  0                                        
SHEET    2  AG 2 ALA d  47  ILE d  49 -1  O  ALA d  48   N  PHE d  40           
SHEET    1  AH 4 GLY 4  53  LEU 4  59  0                                        
SHEET    2  AH 4 LYS 4  27  SER 4  34 -1  N  TYR 4  28   O  LEU 4  59           
SHEET    3  AH 4 LYS 4  84  VAL 4  88 -1  O  TYR 4  86   N  ALA 4  29           
SHEET    4  AH 4 VAL 4  94  TYR 4  96 -1  O  GLN 4  95   N  ARG 4  87           
SHEET    1  AI 2 VAL 4  39  GLU 4  41  0                                        
SHEET    2  AI 2 ALA 4  47  ILE 4  49 -1  O  ALA 4  48   N  PHE 4  40           
LINK         SG  CYS 1 574                FE4  SF4 13001     1555   1555  1.92  
LINK         SG  CYS C  17                FE4  SF4 C3003     1555   1555  1.93  
LINK         SG  CYS b 565                FE3  SF4 a3001     1555   1555  1.94  
LINK         SG  CYS B 556                FE1  SF4 A3001     1555   1555  1.96  
LINK         SG  CYS 2 556                FE1  SF4 13001     1555   1555  1.96  
LINK         SG  CYS C  51                FE1  SF4 C3002     1555   1555  2.02  
LINK         SG  CYS 3  54                FE3  SF4 33002     1555   1555  2.04  
LINK         SG  CYS A 574                FE4  SF4 A3001     1555   1555  2.05  
LINK         SG  CYS c  17                FE4  SF4 c3003     1555   1555  2.09  
LINK         SG  CYS a 583                FE2  SF4 a3001     1555   1555  2.13  
LINK         SG  CYS 1 583                FE2  SF4 13001     1555   1555  2.18  
LINK         SG  CYS b 556                FE1  SF4 a3001     1555   1555  2.33  
LINK         SG  CYS c  54                FE3  SF4 c3002     1555   1555  2.37  
LINK         OE1 GLN a 115                MG   CLA a1106     1555   1555  2.82  
LINK         OE1 GLN A 115                MG   CLA A1106     1555   1555  2.83  
LINK         OE1 GLN 1 115                MG   CLA 11106     1555   1555  2.86  
LINK         OE2 GLU l  52                MG   CLA l1501     1555   1555  2.87  
LINK         O5  LHG B5004                MG   CLA B1240     1555   1555  2.88  
LINK         OD2 ASP B  93                MG   CLA B1206     1555   1555  2.90  
LINK         OD2 ASP 2  93                MG   CLA 21206     1555   1555  2.91  
LINK         O1A CLA a1102                MG   CLA a1109     1555   1555  2.91  
LINK         OE1 GLN A 123                MG   CLA A1107     1555   1555  2.91  
LINK        MG   CLA A1801                 O5  LHG A5003     1555   1555  2.93  
LINK        MG   CLA a1801                 O5  LHG a5003     1555   1555  2.94  
LINK        MG   CLA 11801                 O5  LHG 15003     1555   1555  2.95  
LINK         OE2 GLU L  52                MG   CLA L1501     1555   1555  2.96  
LINK         OD2 ASP b  93                MG   CLA b1206     1555   1555  2.97  
LINK         OE1 GLN a 123                MG   CLA a1107     1555   1555  2.97  
LINK         O1A CLA A1102                MG   CLA A1109     1555   1555  2.98  
LINK         O   THR A 497                MG   CLA A1134     1555   1555  2.98  
LINK         O5  LHG 25004                MG   CLA 21240     1555   1555  2.99  
CISPEP   1 PRO 6   40    CYS 6   41          0        -4.07                     
SITE     1 AC1  9 ALA A 327  HIS A 328  LYS A 329  PRO A 331                    
SITE     2 AC1  9 PHE A 332  CLA A1121  CLA A1122  BCR A4007                    
SITE     3 AC1  9 LHG A5003                                                     
SITE     1 AC2 11 MET A 684  PHE A 685  SER A 688  ARG A 690                    
SITE     2 AC2 11 TRP A 693  ALA A 717  LEU A 718  CLA A1101                    
SITE     3 AC2 11 CLA A1138  CLA A1140  CLA B1013                               
SITE     1 AC3  5 CYS A 574  PRO A 577  CYS A 583  CYS B 556                    
SITE     2 AC3  5 CYS B 565                                                     
SITE     1 AC4 13 PHE A 263  ILE A 305  HIS A 309  CLA A1113                    
SITE     2 AC4 13 CLA A1118  CLA A1120  BCR A4002  PHE K  72                    
SITE     3 AC4 13 PHE K  77  ALA K 106  SER K 109  PHE K 110                    
SITE     4 AC4 13 CLA K1401                                                     
SITE     1 AC5 13 PHE A  84  THR A 161  GLY A 164  GLY A 165                    
SITE     2 AC5 13 MET A 168  LEU A 207  GLY A 211  CLA A1103                    
SITE     3 AC5 13 CLA A1112  CLA A1113  CLA A1114  BCR A4001                    
SITE     4 AC5 13 BCR A4003                                                     
SITE     1 AC6  9 GLY A 203  LEU A 207  GLY A 208  CLA A1103                    
SITE     2 AC6  9 CLA A1111  CLA A1117  CLA A1118  CLA A1127                    
SITE     3 AC6  9 BCR A4002                                                     
SITE     1 AC7 10 ALA A 350  ILE A 354  PHE A 411  CLA A1119                    
SITE     2 AC7 10 CLA A1122  CLA A1123  CLA A1137  CLA A1801                    
SITE     3 AC7 10 BCR A4008  LHG A5003                                          
SITE     1 AC8 10 LEU A 358  ILE A 401  ALA A 404  LEU A 550                    
SITE     2 AC8 10 CLA A1119  CLA A1124  CLA A1125  CLA A1133                    
SITE     3 AC8 10 CLA A1137  BCR A4007                                          
SITE     1 AC9 14 ASN A  50  ALA A  53  ASN A  54  ARG A 571                    
SITE     2 AC9 14 TRP A 588  SER A 719  ILE A 721  GLN A 722                    
SITE     3 AC9 14 ALA A 725  CLA A1101  CLA A1104  CLA A1106                    
SITE     4 AC9 14 CLA A1128  CLA A1140                                          
SITE     1 BC1 12 HIS A 328  GLY A 330  PRO A 331  PHE A 332                    
SITE     2 BC1 12 THR A 333  HIS A 337  CLA A1122  CLA A1129                    
SITE     3 BC1 12 CLA A1136  CLA A1137  CLA A1801  BCR A4007                    
SITE     1 BC2 13 SER A 438  ASN A 441  ILE A 445  CLA A1131                    
SITE     2 BC2 13 ILE B 675  ALA B 678  HIS B 679  THR B 682                    
SITE     3 BC2 13 CLA B1238  BCR B4017  BCR F4020  CLA L1502                    
SITE     4 BC2 13 BCR L4019                                                     
SITE     1 BC3 19 PHE A 452  ILE A 456  PHE A 540  TRP A 597                    
SITE     2 BC3 19 ASN A 600  ILE A 642  TYR A 731  CLA A1011                    
SITE     3 BC3 19 TRP B 645  LEU B 648  HIS B 651  LEU B 652                    
SITE     4 BC3 19 TRP B 654  ALA B 655  CLA B1021  CLA B1023                    
SITE     5 BC3 19 CLA B1206  CLA B1207  BCR B4017                               
SITE     1 BC4 15 TRP A  49  HIS A  52  CLA A1012  CLA A1102                    
SITE     2 BC4 15 CLA A1126  CLA A1138  CLA A1139  CLA A1140                    
SITE     3 BC4 15 PQN A2001  LHG A5001  CLA B1013  BCR B4014                    
SITE     4 BC4 15 ALA F  11  VAL F  83  BCR F4013                               
SITE     1 BC5 13 TRP A  28  PHE A  34  LEU A  51  ALA A  55                    
SITE     2 BC5 13 HIS A  56  GLY A  78  HIS A  79  CLA A1101                    
SITE     3 BC5 13 CLA A1103  CLA A1104  CLA A1106  CLA A1107                    
SITE     4 BC5 13 CLA A1109                                                     
SITE     1 BC6 20 HIS A  56  PHE A  58  ILE A  72  ALA A  75                    
SITE     2 BC6 20 HIS A  76  HIS A  79  LEU A  80  PHE A  84                    
SITE     3 BC6 20 TRP A 348  HIS A 349  LEU A 352  ASN A 355                    
SITE     4 BC6 20 LEU A 356  CLA A1102  CLA A1104  CLA A1111                    
SITE     5 BC6 20 CLA A1123  CLA A1128  BCR A4002  BCR A4003                    
SITE     1 BC7 10 HIS A  56  HIS A  79  TRP A  86  LEU A 400                    
SITE     2 BC7 10 CLA A1102  CLA A1103  CLA A1106  CLA A1127                    
SITE     3 BC7 10 CLA A1128  LHG A5001                                          
SITE     1 BC8 10 VAL A  85  SER A  88  GLY A  89  PHE A  92                    
SITE     2 BC8 10 HIS A  93  PHE A  97  TRP A 118  CLA A1106                    
SITE     3 BC8 10 CLA A1107  BCR F4013                                          
SITE     1 BC9 18 GLN A 115  GLN A 138  ILE A 139  THR A 140                    
SITE     2 BC9 18 SER A 141  LEU A 143  ALA A 667  TYR A 668                    
SITE     3 BC9 18 CLA A1102  CLA A1104  CLA A1105  CLA A1107                    
SITE     4 BC9 18 CLA A1109  CLA A1126  CLA A1140  LHG A5001                    
SITE     5 BC9 18 BCR B4011  BCR F4013                                          
SITE     1 CC1 14 GLN A 115  VAL A 116  VAL A 117  TRP A 118                    
SITE     2 CC1 14 GLN A 123  LEU A 126  ILE A 670  CLA A1102                    
SITE     3 CC1 14 CLA A1105  CLA A1106  CLA A1126  VAL B 440                    
SITE     4 CC1 14 PHE B 444  BCR F4013                                          
SITE     1 CC2 11 VAL A  14  PHE A  77  MET A 172  PHE A 174                    
SITE     2 CC2 11 ALA A 175  PHE A 178  HIS A 179  LYS A 183                    
SITE     3 CC2 11 TRP A 189  CLA A1110  CLA A1111                               
SITE     1 CC3 15 THR A  23  SER A  24  PHE A  25  LYS A  27                    
SITE     2 CC3 15 TRP A  28  HIS A  33  LYS A  71  VAL A  85                    
SITE     3 CC3 15 LEU A 173  GLY A 176  TRP A 177  TYR A 180                    
SITE     4 CC3 15 HIS A 181  CLA A1102  CLA A1106                               
SITE     1 CC4 10 LYS A  13  TRP A 189  ASN A 192  SER A 195                    
SITE     2 CC4 10 HIS A 199  ASN A 314  CLA A1108  CLA A1111                    
SITE     3 CC4 10 CLA A1118  GLY K  83                                          
SITE     1 CC5 16 PHE A  73  HIS A  76  PHE A  77  LEU A  80                    
SITE     2 CC5 16 MET A 172  TRP A 189  ASN A 192  MET A 196                    
SITE     3 CC5 16 HIS A 199  HIS A 200  LEU A 204  CLA A1103                    
SITE     4 CC5 16 CLA A1108  CLA A1110  CLA A1123  BCR A4003                    
SITE     1 CC6 13 GLY A 151  PHE A 152  GLN A 157  CYS A 160                    
SITE     2 CC6 13 THR A 161  GLY A 211  TRP A 212  HIS A 215                    
SITE     3 CC6 13 VAL A 219  HIS A 240  CLA A1113  CLA A1114                    
SITE     4 CC6 13 BCR A4002                                                     
SITE     1 CC7 11 LEU A 210  GLY A 214  ILE A 217  HIS A 218                    
SITE     2 CC7 11 PRO A 246  PHE A 256  GLY A 259  LEU A 260                    
SITE     3 CC7 11 CLA A1112  BCR A4001  BCR A4002                               
SITE     1 CC8 13 TRP A 268  SER A 272  LEU A 275  PHE A 277                    
SITE     2 CC8 13 HIS A 295  LEU A 298  ALA A 299  VAL A 302                    
SITE     3 CC8 13 ASN A 500  CLA A1116  CLA A1134  ALA K  49                    
SITE     4 CC8 13 CLA K1401                                                     
SITE     1 CC9 16 THR A 276  PHE A 277  ASP A 292  THR A 293                    
SITE     2 CC9 16 HIS A 295  HIS A 296  ALA A 299  ILE A 300                    
SITE     3 CC9 16 HIS A 369  MET A 373  ALA A 505  CLA A1115                    
SITE     4 CC9 16 CLA A1117  CLA A1125  CLA A1133  CLA A1134                    
SITE     1 DC1 17 ALA A 149  LEU A 205  GLY A 208  SER A 209                    
SITE     2 DC1 17 TRP A 212  GLN A 216  HIS A 296  HIS A 297                    
SITE     3 DC1 17 PHE A 304  LEU A 362  ILE A 365  VAL A 366                    
SITE     4 DC1 17 PRO A 375  TYR A 376  CLA A1116  CLA A1127                    
SITE     5 DC1 17 BCR A4003                                                     
SITE     1 DC2 15 ASN A 198  HIS A 199  ALA A 202  GLY A 203                    
SITE     2 DC2 15 HIS A 309  TYR A 311  THR A 313  TRP A 315                    
SITE     3 DC2 15 ILE A 317  CLA A1110  BCR A4001  BCR A4003                    
SITE     4 DC2 15 LEU K 105  ALA K 106  SER K 109                               
SITE     1 DC3 15 MET A 197  LEU A 201  LEU A 205  PHE A 304                    
SITE     2 DC3 15 ALA A 307  MET A 310  TYR A 311  MET A 321                    
SITE     3 DC3 15 CLA A1120  CLA A1121  CLA A1122  CLA A1123                    
SITE     4 DC3 15 CLA A1124  BCR A4007  BCR A4008                               
SITE     1 DC4 15 ILE A 324  LEU A 325  HIS A 328  THR A 333                    
SITE     2 DC4 15 HIS A 337  LEU A 340  MET A 429  CLA A1119                    
SITE     3 DC4 15 CLA A1121  CLA A1123  CLA A1129  CLA A1137                    
SITE     4 DC4 15 CLA A1801  BCR A4007  LHG A5003                               
SITE     1 DC5 19 PHE A 190  VAL A 193  MET A 196  MET A 197                    
SITE     2 DC5 19 HIS A 200  MET A 321  LEU A 344  THR A 345                    
SITE     3 DC5 19 THR A 346  TRP A 348  ILE A 354  ASN A 355                    
SITE     4 DC5 19 LEU A 358  CLA A1103  CLA A1111  CLA A1119                    
SITE     5 DC5 19 CLA A1122  CLA A1127  BCR A4007                               
SITE     1 DC6 11 ILE A 364  ILE A 365  GLN A 368  ILE A 401                    
SITE     2 DC6 11 ILE A 542  SER A 601  CLA A1119  CLA A1125                    
SITE     3 DC6 11 CLA A1135  CLA A1137  BCR A4008                               
SITE     1 DC7 13 LEU A 358  ILE A 365  HIS A 369  TYR A 371                    
SITE     2 DC7 13 ALA A 372  MET A 373  SER A 506  PHE A 509                    
SITE     3 DC7 13 CLA A1116  CLA A1124  CLA A1133  CLA A1135                    
SITE     4 DC7 13 BCR A4008                                                     
SITE     1 DC8 14 TRP A  86  MET A  90  SER A 141  SER A 388                    
SITE     2 DC8 14 THR A 391  HIS A 392  TRP A 395  ILE A 736                    
SITE     3 DC8 14 CLA A1012  CLA A1101  CLA A1106  CLA A1107                    
SITE     4 DC8 14 CLA A1127  BCR B4011                                          
SITE     1 DC9 16 LEU A  87  SER A 141  GLY A 142  LEU A 146                    
SITE     2 DC9 16 THR A 363  MET A 370  TYR A 376  LEU A 389                    
SITE     3 DC9 16 HIS A 392  HIS A 393  ILE A 396  CLA A1104                    
SITE     4 DC9 16 CLA A1117  CLA A1123  CLA A1126  BCR A4003                    
SITE     1 EC1 16 HIS A  52  ALA A  53  ASP A  57  LEU A 356                    
SITE     2 EC1 16 PHE A 399  LEU A 400  GLY A 403  HIS A 407                    
SITE     3 EC1 16 ILE A 410  PHE A 570  ARG A 571  TRP A 588                    
SITE     4 EC1 16 CLA A1103  CLA A1104  CLA A1140  LHG A5001                    
SITE     1 EC2 10 HIS A 439  TRP A 442  CLA A1129  ALA B 678                    
SITE     2 EC2 10 THR B 682  PRO B 683  HIS L  19  LEU L  20                    
SITE     3 EC2 10 THR L  22  ILE L  24                                          
SITE     1 EC3 13 TRP A 442  ILE A 445  PHE A 446  PHE A 449                    
SITE     2 EC3 13 HIS A 450  CLA A1132  CLA A1136  CLA A1237                    
SITE     3 EC3 13 CLA B1023  CLA B1238  PQN B2002  BCR F4018                    
SITE     4 EC3 13 BCR F4020                                                     
SITE     1 EC4 13 ILE A 436  LEU A 440  VAL A 443  ALA A 539                    
SITE     2 EC4 13 HIS A 543  CLA A1122  CLA A1124  CLA A1129                    
SITE     3 EC4 13 CLA A1135  CLA A1136  BCR A4007  BCR A4008                    
SITE     4 EC4 13 LHG A5003                                                     
SITE     1 EC5 12 ILE A 700  HIS A 704  LEU A 707  CLA A1101                    
SITE     2 EC5 12 CLA A1139  PQN A2001  SER B 418  SER B 421                    
SITE     3 EC5 12 TRP B 422  CLA B1229  BCR B4014  GLY F  62                    
SITE     1 EC6 11 THR A  45  ILE A  48  TRP A  49  HIS A 704                    
SITE     2 EC6 11 VAL A 709  PRO A 711  PRO A 715  ARG A 716                    
SITE     3 EC6 11 CLA A1101  CLA A1138  ILE F  85                               
SITE     1 EC7 18 TRP A  49  VAL A 678  PHE A 681  GLN A 722                    
SITE     2 EC7 18 ALA A 725  VAL A 726  ALA A 729  HIS A 730                    
SITE     3 EC7 18 LEU A 733  CLA A1101  CLA A1106  CLA A1128                    
SITE     4 EC7 18 PQN A2001  LHG A5001  CLA B1013  BCR B4011                    
SITE     5 EC7 18 ILE F  15  BCR F4013                                          
SITE     1 EC8 23 TYR A 455  THR A 541  TYR A 599  ASN A 600                    
SITE     2 EC8 23 SER A 603  PHE A 607  ILE A 642  LEU A 650                    
SITE     3 EC8 23 ALA A 654  ILE A 658  PHE A 672  HIS A 676                    
SITE     4 EC8 23 PHE A 679  TYR A 731  GLY A 735  THR A 738                    
SITE     5 EC8 23 THR A 739  PHE A 742  CLA A1012  CLA A1022                    
SITE     6 EC8 23 PHE B 617  TRP B 622  CLA B1021                               
SITE     1 EC9 18 ILE A 670  MET A 671  LEU A 673  HIS A 676                    
SITE     2 EC9 18 PHE A 677  ALA A 680  CLA A1011  CLA A1101                    
SITE     3 EC9 18 CLA A1126  PHE B 578  TRP B 579  ASN B 582                    
SITE     4 EC9 18 LEU B 613  PHE B 617  PHE B 710  CLA B1013                    
SITE     5 EC9 18 CLA B1021  BCR B4011                                          
SITE     1 FC1  4 HIS A 240  LEU A 244  CLA A1112  BCR A4002                    
SITE     1 FC2 11 ILE A 306  HIS A 309  MET A 310  GLY A 318                    
SITE     2 FC2 11 HIS A 319  CLA A1119  CLA A1121  BCR A4001                    
SITE     3 FC2 11 PHE K  72  PHE K  77  ALA K  78                               
SITE     1 FC3  8 HIS A 319  ILE A 324  ALA A 327  HIS A 328                    
SITE     2 FC3  8 CLA A1119  CLA A1120  CLA A1122  CLA A1801                    
SITE     1 FC4 12 PHE A 332  THR A 333  LEU A 425  ARG A 428                    
SITE     2 FC4 12 HIS A 432  HIS A 439  CLA A1122  CLA A1130                    
SITE     3 FC4 12 CLA A1137  LHG A5003  VAL L   8  PRO L  23                    
SITE     1 FC5 20 PHE A 449  GLY A 453  LEU A 454  ILE A 456                    
SITE     2 FC5 20 HIS A 457  THR A 460  MET A 461  ARG A 466                    
SITE     3 FC5 20 ASP A 469  CLA A1131  HIS B  95  CLA B1206                    
SITE     4 FC5 20 CLA B1207  BCR F4020  PRO L  64  TRP L  65                    
SITE     5 FC5 20 LEU L  68  PRO L  70  CLA L1503  BCR L4022                    
SITE     1 FC6  8 HIS A 490  ALA A 493  THR A 497  CLA A1116                    
SITE     2 FC6  8 CLA A1125  CLA A1134  CLA A1135  BCR A4008                    
SITE     1 FC7  8 PHE A 277  THR A 497  PRO A 499  ASN A 500                    
SITE     2 FC7  8 CLA A1115  CLA A1116  CLA A1133  CLA K1401                    
SITE     1 FC8 16 GLN A 368  TYR A 371  VAL A 486  GLN A 487                    
SITE     2 FC8 16 PHE A 509  ILE A 525  HIS A 535  HIS A 538                    
SITE     3 FC8 16 VAL A 605  HIS A 608  PHE A 609  CLA A1124                    
SITE     4 FC8 16 CLA A1125  CLA A1133  CLA A1136  CLA A1137                    
SITE     1 FC9 13 PHE A 446  LEU A 447  GLN A 479  PRO A 480                    
SITE     2 FC9 13 ILE A 481  PHE A 482  ALA A 483  HIS A 535                    
SITE     3 FC9 13 HIS A 536  CLA A1131  CLA A1135  CLA A1137                    
SITE     4 FC9 13 LHG A5003                                                     
SITE     1 GC1 13 CLA A1131  MET B 659  PHE B 660  SER B 663                    
SITE     2 GC1 13 TRP B 664  ARG B 665  TRP B 668  ALA B 696                    
SITE     3 GC1 13 LEU B 697  ALA B 702  CLA B1239  LMG B5002                    
SITE     4 GC1 13 BCR L4019                                                     
SITE     1 GC2  8 LEU B 188  PHE B 225  ILE B 285  HIS B 289                    
SITE     2 GC2  8 ILE B 297  CLA B1212  CLA B1217  CLA B1218                    
SITE     1 GC3  7 PHE B  58  PHE B 149  SER B 186  CLA B1202                    
SITE     2 GC3  7 CLA B1209  CLA B1210  CLA B1225                               
SITE     1 GC4  6 TRP B 123  MET B 129  PHE B 141  CLA B1211                    
SITE     2 GC4  6 CLA B1212  CLA B1225                                          
SITE     1 GC5  7 MET B 409  LEU B 416  CLA B1220  CLA B1223                    
SITE     2 GC5  7 CLA B1227  BCR B4010  LHG B5004                               
SITE     1 GC6 12 ALA B 337  MET B 381  ALA B 384  PHE B 385                    
SITE     2 GC6 12 GLY B 388  PHE B 392  CLA B1222  CLA B1223                    
SITE     3 GC6 12 CLA B1232  CLA B1234  CLA B1236  BCR B4009                    
SITE     1 GC7 11 ALA A 674  PHE A 677  VAL A 737  TRP A 740                    
SITE     2 GC7 11 CLA A1012  CLA A1106  CLA A1126  CLA A1140                    
SITE     3 GC7 11 CLA B1013  CLA B1229  CLA B1230                               
SITE     1 GC8  7 CLA A1101  CLA A1138  CLA B1013  CLA B1229                    
SITE     2 GC8  7 CLA B1230  ILE F  53  PHE F  54                               
SITE     1 GC9 11 CLA A1022  CLA A1237  TRP B 645  MET B 646                    
SITE     2 GC9 11 PHE B 649  ILE B 672  ILE B 675  CLA B1023                    
SITE     3 GC9 11 CLA B1205  CLA B1206  CLA B1239                               
SITE     1 HC1 15 TYR B  23  ALA B  26  SER B 553  TRP B 570                    
SITE     2 HC1 15 GLN B 701  LEU B 704  ALA B 708  THR B 711                    
SITE     3 HC1 15 CLA B1201  CLA B1203  CLA B1204  CLA B1224                    
SITE     4 HC1 15 CLA B1226  CLA B1239  PQN B2002                               
SITE     1 HC2 15 HIS B 308  LYS B 309  GLY B 310  PRO B 311                    
SITE     2 HC2 15 LEU B 312  THR B 313  HIS B 317  VAL B 405                    
SITE     3 HC2 15 CLA B1220  CLA B1222  CLA B1223  CLA B1227                    
SITE     4 HC2 15 CLA B1236  CLA B1240  BCR B4009                               
SITE     1 HC3 25 PHE A 677  ALA A 680  PHE A 681  LEU A 683                    
SITE     2 HC3 25 MET A 684  PHE A 687  TYR A 692  TRP A 693                    
SITE     3 HC3 25 LEU A 696  CLA A1012  CLA A1101  CLA A1140                    
SITE     4 HC3 25 PQN A2001  SER B 421  SER B 424  LEU B 425                    
SITE     5 HC3 25 GLY B 428  PHE B 429  LEU B 522  LEU B 529                    
SITE     6 HC3 25 ILE B 530  LEU B 575  TRP B 579  BCR B4011                    
SITE     7 HC3 25 BCR B4014                                                     
SITE     1 HC4 21 TRP A 651  CLA A1011  CLA A1012  CLA A1022                    
SITE     2 HC4 21 TYR B 435  ALA B 519  ASN B 582  TRP B 586                    
SITE     3 HC4 21 PHE B 589  LEU B 613  TRP B 616  LEU B 621                    
SITE     4 HC4 21 SER B 625  ILE B 629  PHE B 647  HIS B 651                    
SITE     5 HC4 21 TRP B 654  TYR B 714  THR B 717  TYR B 718                    
SITE     6 HC4 21 PHE B 721                                                     
SITE     1 HC5 22 ASN A 441  ILE A 445  GLY A 448  PHE A 449                    
SITE     2 HC5 22 PHE A 540  LEU A 547  ILE A 548  PHE A 596                    
SITE     3 HC5 22 TRP A 597  CLA A1022  CLA A1131  ALA B 655                    
SITE     4 HC5 22 THR B 656  PHE B 658  MET B 659  TYR B 667                    
SITE     5 HC5 22 TRP B 668  LEU B 671  CLA B1207  CLA B1239                    
SITE     6 HC5 22 BCR B4017  BCR F4018                                          
SITE     1 HC6 15 PHE B   5  PHE B   8  ALA B  28  HIS B  29                    
SITE     2 HC6 15 HIS B  34  LYS B  45  CLA B1203  CLA B1226                    
SITE     3 HC6 15 LMG B5002  BCR L4019  PHE M  23  SER M  26                    
SITE     4 HC6 15 LEU M  29  TYR M  30  BCR M4021                               
SITE     1 HC7 18 HIS B  29  PHE B  31  ILE B  46  SER B  49                    
SITE     2 HC7 18 HIS B  50  HIS B  53  ILE B  54  ARG B 174                    
SITE     3 HC7 18 LEU B 328  GLN B 331  LEU B 332  ALA B 335                    
SITE     4 HC7 18 LEU B 336  CLA B1203  CLA B1210  CLA B1221                    
SITE     5 HC7 18 CLA B1226  BCR B4005                                          
SITE     1 HC8 11 HIS B  29  HIS B  53  TRP B  60  LEU B 339                    
SITE     2 HC8 11 PHE B 379  CLA B1201  CLA B1202  CLA B1224                    
SITE     3 HC8 11 CLA B1225  CLA B1226  LMG B5002                               
SITE     1 HC9 22 LEU B  59  SER B  62  GLY B  63  PHE B  66                    
SITE     2 HC9 22 HIS B  67  TRP B  70  GLN B  71  HIS B  89                    
SITE     3 HC9 22 LEU B 143  CLA B1205  CLA B1206  LMG B5002                    
SITE     4 HC9 22 BCR F4018  LEU I  10  PRO I  11  LEU I  14                    
SITE     5 HC9 22 ILE I  15  VAL I  18  ALA M  11  LEU M  12                    
SITE     6 HC9 22 ALA M  15  BCR M4021                                          
SITE     1 IC1 15 TRP B  60  THR B  64  VAL B  68  ALA B  88                    
SITE     2 IC1 15 HIS B  89  ILE B 115  ALA B 116  TYR B 117                    
SITE     3 IC1 15 SER B 118  VAL B 642  TRP B 643  CLA B1204                    
SITE     4 IC1 15 CLA B1206  CLA B1224  BCR B4017                               
SITE     1 IC2 14 CLA A1022  CLA A1132  HIS B  95  CLA B1023                    
SITE     2 IC2 14 CLA B1206  BCR F4018  BCR F4020  GLY I  19                    
SITE     3 IC2 14 TRP I  20  TRP L  65  PRO L  70  ILE L  83                    
SITE     4 IC2 14 GLY L  84  ALA L  87                                          
SITE     1 IC3 10 PHE B  51  LEU B 148  PHE B 151  ALA B 152                    
SITE     2 IC3 10 LEU B 155  HIS B 156  PHE B 161  TRP B 167                    
SITE     3 IC3 10 CLA B1209  CLA B1210                                          
SITE     1 IC4  9 TRP B 167  ASN B 170  SER B 173  HIS B 177                    
SITE     2 IC4  9 TRP B 295  CLA B1208  CLA B1210  CLA B1217                    
SITE     3 IC4  9 BCR B4005                                                     
SITE     1 IC5 16 PHE B  47  HIS B  50  PHE B  51  ILE B  54                    
SITE     2 IC5 16 TRP B 167  ARG B 174  HIS B 177  HIS B 178                    
SITE     3 IC5 16 LEU B 182  PHE B 183  CLA B1202  CLA B1208                    
SITE     4 IC5 16 CLA B1209  CLA B1215  CLA B1225  BCR B4005                    
SITE     1 IC6 17 LEU B 188  ALA B 189  ALA B 191  GLY B 192                    
SITE     2 IC6 17 HIS B 196  PHE B 212  LEU B 213  THR B 215                    
SITE     3 IC6 17 PRO B 216  PRO B 217  GLY B 221  LEU B 222                    
SITE     4 IC6 17 LEU B 255  LEU B 278  CLA B1211  BCR B4004                    
SITE     5 IC6 17 BCR B4006                                                     
SITE     1 IC7 11 TRP B 230  PRO B 237  ASP B 238  LEU B 255                    
SITE     2 IC7 11 PHE B 257  LEU B 258  HIS B 275  GLY B 487                    
SITE     3 IC7 11 ALA B 489  TRP B 490  CLA B1214                               
SITE     1 IC8 15 PHE B 257  LEU B 268  ASP B 272  HIS B 275                    
SITE     2 IC8 15 HIS B 276  ILE B 280  ILE B 283  HIS B 349                    
SITE     3 IC8 15 LEU B 353  TRP B 494  CLA B1213  CLA B1215                    
SITE     4 IC8 15 CLA B1223  CLA B1231  CLA B1232                               
SITE     1 IC9 19 TRP B 123  THR B 126  ILE B 127  PHE B 183                    
SITE     2 IC9 19 SER B 186  SER B 187  TRP B 190  ILE B 273                    
SITE     3 IC9 19 HIS B 276  HIS B 277  ILE B 280  VAL B 346                    
SITE     4 IC9 19 MET B 350  SER B 355  CLA B1210  CLA B1214                    
SITE     5 IC9 19 CLA B1223  CLA B1225  CLA B1231                               
SITE     1 JC1 11 LEU B 179  ILE B 283  PHE B 284  ALA B 287                    
SITE     2 JC1 11 MET B 290  TYR B 291  CLA B1218  CLA B1219                    
SITE     3 JC1 11 CLA B1220  CLA B1221  CLA B1223                               
SITE     1 JC2  9 ASN B 176  HIS B 177  VAL B 185  HIS B 289                    
SITE     2 JC2  9 TYR B 291  THR B 293  ILE B 297  CLA B1209                    
SITE     3 JC2  9 BCR B4004                                                     
SITE     1 JC3  7 ILE B 286  MET B 290  GLY B 298  HIS B 299                    
SITE     2 JC3  7 CLA B1216  CLA B1219  BCR B4004                               
SITE     1 JC4  9 MET B 290  HIS B 299  ILE B 304  ALA B 307                    
SITE     2 JC4  9 HIS B 308  CLA B1216  CLA B1218  CLA B1220                    
SITE     3 JC4  9 CLA B1240                                                     
SITE     1 JC5 10 LEU B 305  HIS B 317  PHE B 330  VAL B 405                    
SITE     2 JC5 10 CLA B1216  CLA B1219  CLA B1221  CLA B1227                    
SITE     3 JC5 10 BCR B4009  LHG B5004                                          
SITE     1 JC6 13 ALA B 171  ARG B 174  HIS B 178  PHE B 183                    
SITE     2 JC6 13 ILE B 301  ILE B 324  LEU B 334  SER B 338                    
SITE     3 JC6 13 ILE B 342  CLA B1202  CLA B1216  CLA B1220                    
SITE     4 JC6 13 CLA B1223                                                     
SITE     1 JC7 16 VAL B 341  SER B 344  LEU B 345  GLN B 348                    
SITE     2 JC7 16 GLN B 374  MET B 381  PHE B 385  LEU B 524                    
SITE     3 JC7 16 THR B 527  LEU B 531  MET B 580  CLA B1223                    
SITE     4 JC7 16 CLA B1234  CLA B1236  BCR B4010  LHG B5004                    
SITE     1 JC8 16 SER B 338  VAL B 341  LEU B 345  HIS B 349                    
SITE     2 JC8 16 SER B 352  CLA B1214  CLA B1215  CLA B1216                    
SITE     3 JC8 16 CLA B1221  CLA B1222  CLA B1231  CLA B1234                    
SITE     4 JC8 16 CLA B1236  BCR B4009  BCR B4010  LHG B5004                    
SITE     1 JC9 12 TRP B  60  SER B 118  ALA B 368  THR B 371                    
SITE     2 JC9 12 HIS B 372  TYR B 375  LEU B 716  ALA B 719                    
SITE     3 JC9 12 CLA B1203  CLA B1205  CLA B1225  LMG B5002                    
SITE     1 KC1 20 TRP B  60  THR B  61  SER B 118  GLY B 119                    
SITE     2 KC1 20 TRP B 123  ILE B 342  THR B 343  VAL B 346                    
SITE     3 KC1 20 MET B 350  TYR B 356  LEU B 369  HIS B 372                    
SITE     4 KC1 20 HIS B 373  CLA B1203  CLA B1210  CLA B1211                    
SITE     5 KC1 20 CLA B1215  CLA B1224  BCR B4005  BCR B4006                    
SITE     1 KC2 18 ALA B  26  HIS B  29  ASP B  30  HIS B 329                    
SITE     2 KC2 18 LEU B 336  PHE B 379  GLY B 383  HIS B 387                    
SITE     3 KC2 18 ILE B 390  ARG B 394  TYR B 552  TRP B 570                    
SITE     4 KC2 18 PHE B 573  CLA B1201  CLA B1202  CLA B1203                    
SITE     5 KC2 18 CLA B1239  LMG B5002                                          
SITE     1 KC3 13 LEU B 312  THR B 313  VAL B 405  ARG B 408                    
SITE     2 KC3 13 MET B 409  GLU B 411  HIS B 412  HIS B 419                    
SITE     3 KC3 13 CLA B1220  CLA B1228  CLA B1236  BCR B4009                    
SITE     4 KC3 13 LHG B5004                                                     
SITE     1 KC4  8 TRP A 702  LYS A 706  ALA B 415  HIS B 419                    
SITE     2 KC4  8 TRP B 422  CLA B1227  CLA B1229  CLA B1236                    
SITE     1 KC5 12 CLA A1138  TRP B 422  LEU B 425  PHE B 426                    
SITE     2 KC5 12 HIS B 430  CLA B1228  CLA B1230  CLA B1235                    
SITE     3 KC5 12 BCR B4011  BCR B4014  SER F  51  ALA F  58                    
SITE     1 KC6 10 VAL A 121  HIS B 430  GLY B 433  LEU B 434                    
SITE     2 KC6 10 VAL B 436  HIS B 437  LYS B 449  CLA B1229                    
SITE     3 KC6 10 BCR B4011  BCR B4014                                          
SITE     1 KC7 12 TRP B 460  ILE B 461  THR B 464  SER B 465                    
SITE     2 KC7 12 LEU B 475  LEU B 476  TRP B 494  CLA B1214                    
SITE     3 KC7 12 CLA B1215  CLA B1223  CLA B1232  CLA B1234                    
SITE     1 KC8  6 ILE B 482  THR B 486  TRP B 490  CLA B1214                    
SITE     2 KC8  6 CLA B1231  BCR B4010                                          
SITE     1 KC9 19 GLN B 348  TYR B 351  TYR B 370  PHE B 457                    
SITE     2 KC9 19 ALA B 458  ILE B 461  GLN B 462  PHE B 506                    
SITE     3 KC9 19 LEU B 507  HIS B 517  ILE B 520  LEU B 587                    
SITE     4 KC9 19 TYR B 590  TRP B 591  CLA B1222  CLA B1223                    
SITE     5 KC9 19 CLA B1231  CLA B1235  BCR B4010                               
SITE     1 LC1 14 TRP B 422  PHE B 426  LEU B 427  GLU B 454                    
SITE     2 LC1 14 PRO B 455  VAL B 456  PHE B 457  ALA B 458                    
SITE     3 LC1 14 PHE B 514  HIS B 517  HIS B 518  CLA B1229                    
SITE     4 LC1 14 CLA B1234  CLA B1236                                          
SITE     1 LC2 13 LEU B 420  TRP B 422  VAL B 423  ALA B 521                    
SITE     2 LC2 13 HIS B 525  ILE B 532  CLA B1222  CLA B1223                    
SITE     3 LC2 13 CLA B1227  CLA B1228  CLA B1235  BCR B4010                    
SITE     4 LC2 13 LHG B5004                                                     
SITE     1 LC3  5 LYS B 309  PRO B 311  LEU B 312  CLA B1219                    
SITE     2 LC3  5 LHG B5004                                                     
SITE     1 LC4 21 THR A 460  ALA A 463  CLA A1022  CLA A1132                    
SITE     2 LC4 21 ILE B  91  TRP B  92  ASP B  93  HIS B  95                    
SITE     3 LC4 21 ASN B 114  SER B 641  VAL B 642  TRP B 645                    
SITE     4 LC4 21 CLA B1204  CLA B1205  CLA B1207  CLA B1239                    
SITE     5 LC4 21 BCR B4017  BCR F4018  ILE I  15  PRO I  23                    
SITE     6 LC4 21 THR I  26                                                     
SITE     1 LC5 16 ILE B 127  GLY B 128  GLU B 134  GLY B 138                    
SITE     2 LC5 16 PHE B 141  SER B 186  ALA B 189  TRP B 190                    
SITE     3 LC5 16 HIS B 193  VAL B 197  GLY B 208  TRP B 209                    
SITE     4 LC5 16 PHE B 212  CLA B1212  CLA B1225  BCR B4006                    
SITE     1 LC6 21 CLA A1131  CLA A1237  THR B  18  ILE B  21                    
SITE     2 LC6 21 TRP B  22  ILE B 675  VAL B 676  HIS B 679                    
SITE     3 LC6 21 VAL B 688  TRP B 690  LYS B 691  PRO B 694                    
SITE     4 LC6 21 VAL B 695  BCR F4018  BCR F4020  TRP I  20                    
SITE     5 LC6 21 PHE I  31  LEU L  88  VAL L  91  TYR L  99                    
SITE     6 LC6 21 BCR L4019                                                     
SITE     1 LC7 13 PHE B 649  LEU B 652  VAL B 653  MET B 659                    
SITE     2 LC7 13 PHE B 660  VAL B 705  HIS B 709  CLA B1023                    
SITE     3 LC7 13 CLA B1206  CLA B1226  PQN B2002  BCR B4017                    
SITE     4 LC7 13 LMG B5002                                                     
SITE     1 LC8  5 CYS C  21  CYS C  48  CYS C  51  LYS C  52                    
SITE     2 LC8  5 CYS C  54                                                     
SITE     1 LC9  6 CYS C  11  ILE C  12  CYS C  14  THR C  15                    
SITE     2 LC9  6 CYS C  17  CYS C  58                                          
SITE     1 MC1  9 CLA A1131  CLA B1023  CLA B1204  CLA B1206                    
SITE     2 MC1  9 CLA B1207  CLA B1238  BCR F4020  PHE I  22                    
SITE     3 MC1  9 PRO I  23                                                     
SITE     1 MC2 10 CLA A1131  CLA A1132  CLA A1237  CLA B1207                    
SITE     2 MC2 10 CLA B1238  BCR F4018  TRP L  65  GLY L  84                    
SITE     3 MC2 10 ALA L  87  CLA L1502                                          
SITE     1 MC3  7 TRP A 118  CLA A1101  CLA A1105  CLA A1106                    
SITE     2 MC3  7 CLA A1107  CLA A1140  PRO F  12                               
SITE     1 MC4 10 ASN L  36  LEU L  37  ARG L  41  LEU L  48                    
SITE     2 MC4 10 GLU L  52  MET L  55  ALA L  56  CLA L1502                    
SITE     3 MC4 10 CLA L1503  BCR L4022                                          
SITE     1 MC5 11 CLA A1237  LEU B 684  BCR F4020  PHE L  33                    
SITE     2 MC5 11 PRO L  38  GLU L  52  VAL L  53  ALA L  56                    
SITE     3 MC5 11 HIS L  57  CLA L1501  BCR L4019                               
SITE     1 MC6 10 CLA A1132  TYR L  59  PHE L  60  GLY L  63                    
SITE     2 MC6 10 PRO L  64  THR L  66  LEU L 142  LEU L 145                    
SITE     3 MC6 10 CLA L1501  BCR L4022                                          
SITE     1 MC7 11 CLA A1237  CLA B1201  CLA B1238  PQN B2002                    
SITE     2 MC7 11 MET I  27  LEU I  30  ALA L  92  ALA L  95                    
SITE     3 MC7 11 LEU L  96  PHE L 127  CLA L1502                               
SITE     1 MC8  7 CLA A1132  MET L  55  ALA L  56  GLY L 133                    
SITE     2 MC8  7 VAL L 137  CLA L1501  CLA L1503                               
SITE     1 MC9 10 LEU B 150  CLA B1201  CLA B1204  LEU M   9                    
SITE     2 MC9 10 LEU M  12  ALA M  15  LEU M  16  ALA M  19                    
SITE     3 MC9 10 ALA M  22  SER M  26                                          
SITE     1 NC1  8 ALA a 327  HIS a 328  LYS a 329  PRO a 331                    
SITE     2 NC1  8 PHE a 332  CLA a1121  CLA a1122  LHG a5003                    
SITE     1 NC2 12 MET a 684  PHE a 685  SER a 688  TRP a 693                    
SITE     2 NC2 12 ALA a 717  LEU a 718  CLA a1101  CLA a1139                    
SITE     3 NC2 12 CLA a1140  CLA b1013  BCR b4014  ALA f  11                    
SITE     1 NC3  4 CYS a 574  CYS a 583  CYS b 556  CYS b 565                    
SITE     1 NC4 12 PHE a 263  ILE a 305  HIS a 309  CLA a1113                    
SITE     2 NC4 12 CLA a1118  CLA a1120  BCR a4002  PHE k  77                    
SITE     3 NC4 12 ALA k 106  SER k 109  PHE k 110  CLA k1401                    
SITE     1 NC5  9 THR a 161  LEU a 207  GLY a 211  CLA a1103                    
SITE     2 NC5  9 CLA a1112  CLA a1113  CLA a1118  BCR a4001                    
SITE     3 NC5  9 BCR a4003                                                     
SITE     1 NC6  8 GLY a 208  CLA a1103  CLA a1104  CLA a1111                    
SITE     2 NC6  8 CLA a1117  CLA a1118  CLA a1127  BCR a4002                    
SITE     1 NC7  8 ALA a 350  ILE a 354  PHE a 411  CLA a1119                    
SITE     2 NC7  8 CLA a1122  CLA a1123  BCR a4008  LHG a5003                    
SITE     1 NC8  9 ALA a 357  LEU a 358  SER a 361  ILE a 401                    
SITE     2 NC8  9 CLA a1119  CLA a1124  CLA a1125  CLA a1137                    
SITE     3 NC8  9 BCR a4007                                                     
SITE     1 NC9 16 TRP a  49  ASN a  50  ALA a  53  ASN a  54                    
SITE     2 NC9 16 ARG a 571  SER a 719  ILE a 721  ALA a 725                    
SITE     3 NC9 16 VAL a 728  CLA a1101  CLA a1102  CLA a1104                    
SITE     4 NC9 16 CLA a1106  CLA a1128  CLA a1140  GLY e  51                    
SITE     1 OC1 12 HIS a 328  LYS a 329  GLY a 330  PHE a 332                    
SITE     2 OC1 12 THR a 333  HIS a 337  CLA a1122  CLA a1129                    
SITE     3 OC1 12 CLA a1136  CLA a1137  CLA a1801  BCR a4007                    
SITE     1 OC2 12 SER a 438  ASN a 441  TRP a 442  ILE a 445                    
SITE     2 OC2 12 ILE b 675  ALA b 678  HIS b 679  ALA b 685                    
SITE     3 OC2 12 CLA b1238  BCR b4017  BCR f4020  CLA l1502                    
SITE     1 OC3 18 PHE a 452  ILE a 456  PHE a 540  PHE a 596                    
SITE     2 OC3 18 TRP a 597  ASN a 600  ILE a 642  CLA a1011                    
SITE     3 OC3 18 TRP b 645  LEU b 648  HIS b 651  LEU b 652                    
SITE     4 OC3 18 TRP b 654  ALA b 655  CLA b1021  CLA b1023                    
SITE     5 OC3 18 CLA b1206  BCR b4017                                          
SITE     1 OC4 13 ILE a  48  TRP a  49  HIS a  52  CLA a1102                    
SITE     2 OC4 13 CLA a1109  CLA a1126  CLA a1138  CLA a1139                    
SITE     3 OC4 13 CLA a1140  PQN a2001  LHG a5001  VAL f  83                    
SITE     4 OC4 13 BCR f4013                                                     
SITE     1 OC5  9 HIS a  33  HIS a  56  GLY a  78  HIS a  79                    
SITE     2 OC5  9 CLA a1101  CLA a1104  CLA a1106  CLA a1109                    
SITE     3 OC5  9 LHG a5001                                                     
SITE     1 OC6 21 HIS a  56  PHE a  58  ILE a  72  HIS a  76                    
SITE     2 OC6 21 HIS a  79  LEU a  80  VAL a  83  PHE a  84                    
SITE     3 OC6 21 LEU a  87  MET a 168  TRP a 348  HIS a 349                    
SITE     4 OC6 21 LEU a 352  ASN a 355  LEU a 356  LEU a 359                    
SITE     5 OC6 21 CLA a1104  CLA a1111  CLA a1128  BCR a4002                    
SITE     6 OC6 21 BCR a4003                                                     
SITE     1 OC7 11 HIS a  56  HIS a  79  TRP a  86  CLA a1102                    
SITE     2 OC7 11 CLA a1103  CLA a1106  CLA a1126  CLA a1127                    
SITE     3 OC7 11 CLA a1128  BCR a4003  LHG a5001                               
SITE     1 OC8  6 VAL a  85  PHE a  92  HIS a  93  TRP a 118                    
SITE     2 OC8  6 CLA a1106  CLA a1107                                          
SITE     1 OC9 20 TRP a  86  MET a  90  GLN a 115  GLN a 138                    
SITE     2 OC9 20 ILE a 139  THR a 140  SER a 141  LEU a 143                    
SITE     3 OC9 20 ALA a 667  TYR a 668  CLA a1012  CLA a1102                    
SITE     4 OC9 20 CLA a1104  CLA a1105  CLA a1107  CLA a1109                    
SITE     5 OC9 20 CLA a1126  LHG a5001  BCR b4011  BCR f4013                    
SITE     1 PC1 14 VAL a  85  GLN a 115  VAL a 116  TRP a 118                    
SITE     2 PC1 14 GLN a 123  LEU a 126  ILE a 137  ILE a 670                    
SITE     3 PC1 14 CLA a1105  CLA a1106  CLA a1126  VAL b 440                    
SITE     4 PC1 14 PHE b 444  CLA b1230                                          
SITE     1 PC2 10 PHE a  77  LEU a 171  MET a 172  PHE a 174                    
SITE     2 PC2 10 PHE a 178  HIS a 179  LYS a 183  TRP a 189                    
SITE     3 PC2 10 CLA a1110  CLA a1111                                          
SITE     1 PC3 17 THR a  23  SER a  24  LYS a  27  TRP a  28                    
SITE     2 PC3 17 HIS a  33  LYS a  71  SER a  74  GLY a  78                    
SITE     3 PC3 17 VAL a  82  LEU a 173  GLY a 176  TRP a 177                    
SITE     4 PC3 17 TYR a 180  HIS a 181  CLA a1101  CLA a1102                    
SITE     5 PC3 17 CLA a1106                                                     
SITE     1 PC4  9 LYS a  13  TRP a 189  SER a 195  HIS a 199                    
SITE     2 PC4  9 ASN a 314  TRP a 315  CLA a1108  CLA a1111                    
SITE     3 PC4  9 CLA a1118                                                     
SITE     1 PC5 15 PHE a  73  HIS a  76  PHE a  77  LEU a  80                    
SITE     2 PC5 15 MET a 172  TRP a 189  MET a 196  HIS a 199                    
SITE     3 PC5 15 HIS a 200  LEU a 204  CLA a1103  CLA a1108                    
SITE     4 PC5 15 CLA a1110  CLA a1123  BCR a4003                               
SITE     1 PC6 13 GLY a 151  PHE a 152  GLN a 157  CYS a 160                    
SITE     2 PC6 13 THR a 161  GLY a 211  TRP a 212  HIS a 215                    
SITE     3 PC6 13 VAL a 219  PRO a 239  CLA a1113  CLA a1114                    
SITE     4 PC6 13 BCR a4002                                                     
SITE     1 PC7  9 LEU a 210  ILE a 217  HIS a 218  PHE a 256                    
SITE     2 PC7  9 GLY a 259  LEU a 260  CLA a1112  BCR a4001                    
SITE     3 PC7  9 BCR a4002                                                     
SITE     1 PC8 13 TRP a 268  SER a 272  LEU a 275  PHE a 277                    
SITE     2 PC8 13 HIS a 295  LEU a 298  ALA a 299  VAL a 302                    
SITE     3 PC8 13 ASN a 500  CLA a1116  CLA a1134  ALA k  49                    
SITE     4 PC8 13 CLA k1401                                                     
SITE     1 PC9 16 PHE a 277  GLY a 279  ASP a 292  HIS a 295                    
SITE     2 PC9 16 HIS a 296  ALA a 299  ILE a 300  LEU a 303                    
SITE     3 PC9 16 HIS a 369  MET a 373  ALA a 505  CLA a1115                    
SITE     4 PC9 16 CLA a1117  CLA a1125  CLA a1133  CLA a1134                    
SITE     1 QC1 17 ALA a 149  LEU a 205  GLY a 208  SER a 209                    
SITE     2 QC1 17 TRP a 212  GLN a 216  HIS a 296  HIS a 297                    
SITE     3 QC1 17 ILE a 300  PHE a 304  LEU a 362  PRO a 375                    
SITE     4 QC1 17 TYR a 376  CLA a1116  CLA a1125  CLA a1127                    
SITE     5 QC1 17 BCR a4003                                                     
SITE     1 QC2 15 HIS a 199  ALA a 202  GLY a 203  LEU a 207                    
SITE     2 QC2 15 ILE a 305  HIS a 309  THR a 313  TRP a 315                    
SITE     3 QC2 15 ILE a 317  CLA a1110  BCR a4001  BCR a4002                    
SITE     4 QC2 15 BCR a4003  LEU k 105  SER k 109                               
SITE     1 QC3 17 MET a 197  LEU a 201  LEU a 205  PHE a 304                    
SITE     2 QC3 17 ALA a 307  MET a 310  TYR a 311  MET a 429                    
SITE     3 QC3 17 LEU a 550  LEU a 554  CLA a1120  CLA a1121                    
SITE     4 QC3 17 CLA a1122  CLA a1123  CLA a1125  BCR a4007                    
SITE     5 QC3 17 BCR a4008                                                     
SITE     1 QC4 15 ILE a 324  LEU a 325  HIS a 328  THR a 333                    
SITE     2 QC4 15 HIS a 337  LEU a 340  LEU a 426  MET a 429                    
SITE     3 QC4 15 CLA a1119  CLA a1121  CLA a1123  CLA a1129                    
SITE     4 QC4 15 CLA a1801  BCR a4007  LHG a5003                               
SITE     1 QC5 18 PHE a 190  VAL a 193  MET a 196  MET a 197                    
SITE     2 QC5 18 HIS a 200  MET a 321  LEU a 344  THR a 345                    
SITE     3 QC5 18 THR a 346  TRP a 348  ILE a 354  ASN a 355                    
SITE     4 QC5 18 LEU a 358  CLA a1111  CLA a1119  CLA a1122                    
SITE     5 QC5 18 CLA a1127  BCR a4007                                          
SITE     1 QC6  9 ILE a 364  GLN a 368  ILE a 401  THR a 545                    
SITE     2 QC6  9 SER a 601  CLA a1125  CLA a1135  CLA a1137                    
SITE     3 QC6  9 BCR a4008                                                     
SITE     1 QC7 14 LEU a 358  GLN a 368  HIS a 369  TYR a 371                    
SITE     2 QC7 14 ALA a 372  MET a 373  SER a 506  PHE a 509                    
SITE     3 QC7 14 CLA a1116  CLA a1117  CLA a1119  CLA a1124                    
SITE     4 QC7 14 CLA a1133  BCR a4008                                          
SITE     1 QC8 15 TRP a  86  SER a 141  SER a 388  THR a 391                    
SITE     2 QC8 15 HIS a 392  TRP a 395  PHE a 399  ILE a 736                    
SITE     3 QC8 15 TRP a 740  CLA a1101  CLA a1104  CLA a1106                    
SITE     4 QC8 15 CLA a1107  CLA a1127  BCR b4011                               
SITE     1 QC9 16 SER a 141  GLY a 142  LEU a 146  LEU a 359                    
SITE     2 QC9 16 THR a 363  VAL a 366  MET a 370  TYR a 376                    
SITE     3 QC9 16 LEU a 389  HIS a 392  HIS a 393  CLA a1104                    
SITE     4 QC9 16 CLA a1117  CLA a1123  CLA a1126  BCR a4003                    
SITE     1 RC1 18 HIS a  52  ALA a  53  HIS a  56  LEU a 352                    
SITE     2 RC1 18 LEU a 356  PHE a 399  GLY a 403  HIS a 407                    
SITE     3 RC1 18 ILE a 410  ARG a 414  PHE a 570  ARG a 571                    
SITE     4 RC1 18 TRP a 588  CLA a1103  CLA a1104  CLA a1140                    
SITE     5 RC1 18 LHG a5001  BCR b4011                                          
SITE     1 RC2 11 HIS a 439  CLA a1129  CLA a1137  ALA b 678                    
SITE     2 RC2 11 THR b 682  PRO b 683  HIS l  19  LEU l  20                    
SITE     3 RC2 11 THR l  22  ILE l  24  SER l  25                               
SITE     1 RC3 12 TRP a 442  PHE a 446  PHE a 449  HIS a 450                    
SITE     2 RC3 12 CLA a1132  CLA b1023  CLA b1238  CLA b1239                    
SITE     3 RC3 12 PQN b2002  BCR b4017  BCR f4018  BCR f4020                    
SITE     1 RC4 12 LEU a 440  TRP a 442  VAL a 443  ALA a 539                    
SITE     2 RC4 12 HIS a 543  CLA a1124  CLA a1129  CLA a1130                    
SITE     3 RC4 12 CLA a1135  CLA a1136  BCR a4008  LHG a5003                    
SITE     1 RC5 14 ILE a 700  ALA a 703  HIS a 704  LEU a 707                    
SITE     2 RC5 14 CLA a1101  CLA a1139  SER b 418  SER b 421                    
SITE     3 RC5 14 TRP b 422  LEU b 425  CLA b1228  CLA b1229                    
SITE     4 RC5 14 BCR b4014  GLY f  62                                          
SITE     1 RC6 12 THR a  45  VAL a 701  HIS a 704  VAL a 709                    
SITE     2 RC6 12 PRO a 711  PRO a 715  ARG a 716  CLA a1101                    
SITE     3 RC6 12 CLA a1138  PQN a2001  SER f   9  ALA f  90                    
SITE     1 RC7 14 TRP a  49  PHE a 681  GLN a 722  VAL a 726                    
SITE     2 RC7 14 ALA a 729  HIS a 730  CLA a1101  CLA a1128                    
SITE     3 RC7 14 PQN a2001  LHG a5001  CLA b1013  BCR b4011                    
SITE     4 RC7 14 ILE f  15  BCR f4013                                          
SITE     1 RC8 18 TYR a 599  ILE a 604  PHE a 607  TRP a 645                    
SITE     2 RC8 18 LEU a 650  ALA a 654  HIS a 676  PHE a 679                    
SITE     3 RC8 18 TYR a 731  GLY a 735  THR a 738  THR a 739                    
SITE     4 RC8 18 PHE a 742  CLA a1012  CLA a1022  PHE b 617                    
SITE     5 RC8 18 TRP b 622  CLA b1021                                          
SITE     1 RC9 18 ILE a 670  MET a 671  LEU a 673  ALA a 674                    
SITE     2 RC9 18 HIS a 676  PHE a 677  ALA a 680  CLA a1011                    
SITE     3 RC9 18 CLA a1106  PHE b 578  TRP b 579  ASN b 582                    
SITE     4 RC9 18 TRP b 586  LEU b 613  PHE b 710  CLA b1013                    
SITE     5 RC9 18 CLA b1021  BCR b4011                                          
SITE     1 SC1  4 LEU a 238  HIS a 240  LEU a 244  CLA a1112                    
SITE     1 SC2 10 ILE a 306  HIS a 309  MET a 310  GLY a 318                    
SITE     2 SC2 10 HIS a 319  CLA a1119  CLA a1121  BCR a4001                    
SITE     3 SC2 10 PHE k  72  PHE k  77                                          
SITE     1 SC3  7 HIS a 319  ILE a 324  HIS a 328  CLA a1119                    
SITE     2 SC3  7 CLA a1120  CLA a1122  CLA a1801                               
SITE     1 SC4 14 PHE a 332  THR a 333  LEU a 425  ARG a 428                    
SITE     2 SC4 14 HIS a 432  ILE a 436  HIS a 439  CLA a1122                    
SITE     3 SC4 14 CLA a1130  CLA a1137  LHG a5003  VAL l   8                    
SITE     4 SC4 14 LEU l  20  PRO l  23                                          
SITE     1 SC5 19 PHE a 449  GLY a 453  LEU a 454  ILE a 456                    
SITE     2 SC5 19 HIS a 457  THR a 460  MET a 461  ARG a 466                    
SITE     3 SC5 19 CLA a1131  HIS b  95  CLA b1207  BCR f4020                    
SITE     4 SC5 19 PRO l  64  TRP l  65  LEU l  68  GLY l  69                    
SITE     5 SC5 19 PRO l  70  CLA l1503  BCR l4022                               
SITE     1 SC6  9 LEU a 489  HIS a 490  ALA a 493  THR a 497                    
SITE     2 SC6  9 ALA a 498  CLA a1116  CLA a1125  CLA a1134                    
SITE     3 SC6  9 CLA a1135                                                     
SITE     1 SC7  8 PHE a 277  THR a 497  ALA a 498  PRO a 499                    
SITE     2 SC7  8 ASN a 500  CLA a1115  CLA a1116  CLA a1133                    
SITE     1 SC8 16 GLN a 368  TYR a 371  PHE a 482  ALA a 483                    
SITE     2 SC8 16 VAL a 486  GLN a 487  PHE a 509  ILE a 525                    
SITE     3 SC8 16 HIS a 535  HIS a 538  VAL a 605  HIS a 608                    
SITE     4 SC8 16 CLA a1124  CLA a1133  CLA a1136  CLA a1137                    
SITE     1 SC9 13 PHE a 446  LEU a 447  GLN a 479  PRO a 480                    
SITE     2 SC9 13 ILE a 481  PHE a 482  ALA a 483  PHE a 532                    
SITE     3 SC9 13 HIS a 535  HIS a 536  CLA a1135  CLA a1137                    
SITE     4 SC9 13 LHG a5003                                                     
SITE     1 TC1 13 CLA a1131  MET b 659  SER b 663  TRP b 664                    
SITE     2 TC1 13 ARG b 665  TRP b 668  ALA b 696  LEU b 697                    
SITE     3 TC1 13 ALA b 702  CLA b1238  CLA b1239  BCR b4017                    
SITE     4 TC1 13 BCR l4019                                                     
SITE     1 TC2  8 LEU b 188  PHE b 225  ILE b 285  HIS b 289                    
SITE     2 TC2  8 ILE b 297  CLA b1212  CLA b1217  CLA b1218                    
SITE     1 TC3  8 PHE b  58  PHE b 149  GLY b 181  SER b 186                    
SITE     2 TC3  8 CLA b1203  CLA b1209  CLA b1210  CLA b1225                    
SITE     1 TC4  4 MET b 129  TRP b 209  CLA b1211  CLA b1212                    
SITE     1 TC5  5 CLA b1220  CLA b1223  CLA b1227  CLA b1240                    
SITE     2 TC5  5 BCR b4010                                                     
SITE     1 TC6 14 PHE b 330  GLY b 333  LEU b 334  ALA b 337                    
SITE     2 TC6 14 MET b 381  ALA b 384  PHE b 385  PHE b 392                    
SITE     3 TC6 14 CLA b1216  CLA b1222  CLA b1223  CLA b1232                    
SITE     4 TC6 14 BCR b4009  LHG b5004                                          
SITE     1 TC7 10 PHE a 677  LEU a 733  VAL a 737  CLA a1012                    
SITE     2 TC7 10 CLA a1106  CLA a1126  CLA a1128  CLA a1140                    
SITE     3 TC7 10 CLA b1013  CLA b1230                                          
SITE     1 TC8  8 CLA a1138  PQN a2001  PHE b 429  CLA b1013                    
SITE     2 TC8  8 CLA b1229  CLA b1230  ILE f  53  PHE f  54                    
SITE     1 TC9 13 ILE a 445  PHE a 449  CLA a1022  CLA a1131                    
SITE     2 TC9 13 CLA a1237  TRP b 645  MET b 646  PHE b 649                    
SITE     3 TC9 13 CLA b1023  CLA b1205  CLA b1206  CLA b1239                    
SITE     4 TC9 13 PQN b2002                                                     
SITE     1 UC1 12 LEU b  12  TYR b  23  ALA b  26  SER b 553                    
SITE     2 UC1 12 TRP b 570  SER b 698  GLN b 701  CLA b1201                    
SITE     3 UC1 12 CLA b1203  CLA b1224  CLA b1226  CLA b1239                    
SITE     1 UC2 14 HIS b 308  LYS b 309  GLY b 310  PRO b 311                    
SITE     2 UC2 14 LEU b 312  THR b 313  HIS b 317  VAL b 405                    
SITE     3 UC2 14 CLA b1220  CLA b1223  CLA b1227  CLA b1236                    
SITE     4 UC2 14 CLA b1240  BCR b4010                                          
SITE     1 UC3 23 PHE a 677  ALA a 680  PHE a 681  LEU a 683                    
SITE     2 UC3 23 MET a 684  PHE a 687  TYR a 692  TRP a 693                    
SITE     3 UC3 23 CLA a1012  CLA a1140  PQN a2001  SER b 421                    
SITE     4 UC3 23 SER b 424  LEU b 425  GLY b 428  PHE b 429                    
SITE     5 UC3 23 LEU b 522  LEU b 529  ILE b 530  LEU b 575                    
SITE     6 UC3 23 TRP b 579  BCR b4011  BCR b4014                               
SITE     1 UC4 21 LEU a 650  TRP a 651  CLA a1011  CLA a1012                    
SITE     2 UC4 21 CLA a1022  TYR b 435  ALA b 519  ASN b 582                    
SITE     3 UC4 21 TRP b 586  PHE b 589  LEU b 613  TRP b 616                    
SITE     4 UC4 21 LEU b 621  SER b 625  PHE b 647  HIS b 651                    
SITE     5 UC4 21 TRP b 654  TYR b 714  THR b 717  TYR b 718                    
SITE     6 UC4 21 PHE b 721                                                     
SITE     1 UC5 20 ASN a 441  CYS a 444  ILE a 445  GLY a 448                    
SITE     2 UC5 20 PHE a 449  PHE a 452  PHE a 540  LEU a 547                    
SITE     3 UC5 20 ILE a 548  PHE a 596  TRP a 597  CLA a1022                    
SITE     4 UC5 20 CLA a1131  ALA b 655  THR b 656  PHE b 658                    
SITE     5 UC5 20 MET b 659  TYR b 667  TRP b 668  BCR b4017                    
SITE     1 UC6 17 PHE b   5  PHE b   8  ILE b  25  ALA b  28                    
SITE     2 UC6 17 HIS b  29  PHE b  31  HIS b  34  ILE b  56                    
SITE     3 UC6 17 CLA b1202  CLA b1203  CLA b1226  LMG b5002                    
SITE     4 UC6 17 PHE m  23  SER m  26  LEU m  29  TYR m  30                    
SITE     5 UC6 17 BCR m4021                                                     
SITE     1 UC7 16 HIS b  29  PHE b  31  ILE b  46  SER b  49                    
SITE     2 UC7 16 HIS b  50  HIS b  53  ILE b  54  LEU b 328                    
SITE     3 UC7 16 LEU b 332  ALA b 335  LEU b 339  CLA b1201                    
SITE     4 UC7 16 CLA b1203  CLA b1210  CLA b1221  CLA b1226                    
SITE     1 UC8 11 HIS b  29  HIS b  53  TRP b  60  PHE b 379                    
SITE     2 UC8 11 CLA b1201  CLA b1202  CLA b1224  CLA b1225                    
SITE     3 UC8 11 CLA b1226  BCR b4005  LMG b5002                               
SITE     1 UC9 20 LEU b  59  TRP b  60  SER b  62  GLY b  63                    
SITE     2 UC9 20 PHE b  66  HIS b  67  TRP b  70  GLN b  71                    
SITE     3 UC9 20 HIS b  89  LEU b 143  CLA b1205  CLA b1206                    
SITE     4 UC9 20 LEU i  10  PRO i  11  LEU i  14  ILE i  15                    
SITE     5 UC9 20 VAL i  18  ALA m  11  ALA m  15  BCR m4021                    
SITE     1 VC1 13 THR b  64  ALA b  88  HIS b  89  ILE b 115                    
SITE     2 VC1 13 ALA b 116  TYR b 117  SER b 118  VAL b 642                    
SITE     3 VC1 13 TRP b 643  CLA b1204  CLA b1206  CLA b1224                    
SITE     4 VC1 13 BCR b4017                                                     
SITE     1 VC2 16 TYR 8  59  VAL 8 137  ILE 8 151  CLA 81501                    
SITE     2 VC2 16 CLA 81503  BCR 84022  CLA a1132  HIS b  95                    
SITE     3 VC2 16 CLA b1206  BCR f4018  BCR f4020  TRP i  20                    
SITE     4 VC2 16 TRP l  65  PRO l  70  LEU l  71  ILE l  83                    
SITE     1 VC3  8 LEU b 148  PHE b 151  HIS b 156  LYS b 160                    
SITE     2 VC3  8 PHE b 161  TRP b 167  CLA b1209  CLA b1210                    
SITE     1 VC4 10 TRP b 167  ASN b 170  SER b 173  HIS b 177                    
SITE     2 VC4 10 ASN b 294  TRP b 295  CLA b1208  CLA b1210                    
SITE     3 VC4 10 CLA b1217  BCR b4005                                          
SITE     1 VC5 17 PHE b  47  HIS b  50  PHE b  51  TRP b 167                    
SITE     2 VC5 17 PHE b 168  ARG b 174  HIS b 177  HIS b 178                    
SITE     3 VC5 17 LEU b 182  PHE b 183  TYR b 356  CLA b1202                    
SITE     4 VC5 17 CLA b1208  CLA b1209  CLA b1215  CLA b1225                    
SITE     5 VC5 17 BCR b4005                                                     
SITE     1 VC6 14 LEU b 188  ALA b 189  ALA b 191  GLY b 192                    
SITE     2 VC6 14 HIS b 196  PHE b 212  LEU b 213  THR b 215                    
SITE     3 VC6 14 PRO b 216  PRO b 217  LEU b 222  CLA b1211                    
SITE     4 VC6 14 BCR b4004  BCR b4006                                          
SITE     1 VC7  6 TRP b 230  LEU b 255  PHE b 257  HIS b 275                    
SITE     2 VC7  6 ALA b 489  CLA b1214                                          
SITE     1 VC8 19 PHE b 257  GLY b 259  GLY b 260  LEU b 268                    
SITE     2 VC8 19 ASP b 272  HIS b 275  HIS b 276  ALA b 279                    
SITE     3 VC8 19 ILE b 280  ILE b 283  HIS b 349  LEU b 353                    
SITE     4 VC8 19 TRP b 490  TRP b 494  CLA b1213  CLA b1215                    
SITE     5 VC8 19 CLA b1223  CLA b1231  CLA b1232                               
SITE     1 VC9 21 TRP b 123  LEU b 182  PHE b 183  SER b 186                    
SITE     2 VC9 21 SER b 187  TRP b 190  HIS b 276  HIS b 277                    
SITE     3 VC9 21 ILE b 280  ILE b 342  VAL b 346  HIS b 349                    
SITE     4 VC9 21 MET b 350  SER b 355  TYR b 356  CLA b1210                    
SITE     5 VC9 21 CLA b1214  CLA b1216  CLA b1223  CLA b1225                    
SITE     6 VC9 21 CLA b1231                                                     
SITE     1 WC1 14 LEU b 179  ILE b 283  PHE b 284  ALA b 287                    
SITE     2 WC1 14 MET b 290  TYR b 291  CLA b1215  CLA b1218                    
SITE     3 WC1 14 CLA b1219  CLA b1220  CLA b1221  CLA b1223                    
SITE     4 WC1 14 CLA b1234  BCR b4010                                          
SITE     1 WC2  6 HIS b 177  HIS b 289  THR b 293  ILE b 297                    
SITE     2 WC2  6 CLA b1209  BCR b4004                                          
SITE     1 WC3  6 ILE b 286  GLY b 298  HIS b 299  CLA b1216                    
SITE     2 WC3  6 CLA b1219  BCR b4004                                          
SITE     1 WC4  9 MET b 290  HIS b 299  ILE b 304  ALA b 307                    
SITE     2 WC4  9 HIS b 308  CLA b1216  CLA b1218  CLA b1220                    
SITE     3 WC4  9 CLA b1240                                                     
SITE     1 WC5 13 ILE b 304  LEU b 305  HIS b 308  HIS b 317                    
SITE     2 WC5 13 PHE b 330  VAL b 405  CLA b1216  CLA b1219                    
SITE     3 WC5 13 CLA b1221  CLA b1227  CLA b1240  BCR b4009                    
SITE     4 WC5 13 LHG b5004                                                     
SITE     1 WC6 13 ARG b 174  HIS b 178  LEU b 179  LEU b 305                    
SITE     2 WC6 13 ILE b 324  LEU b 334  ALA b 335  SER b 338                    
SITE     3 WC6 13 ILE b 342  CLA b1202  CLA b1216  CLA b1220                    
SITE     4 WC6 13 CLA b1223                                                     
SITE     1 WC7 13 VAL b 341  SER b 344  GLN b 348  GLN b 374                    
SITE     2 WC7 13 MET b 381  PHE b 385  LEU b 524  LEU b 531                    
SITE     3 WC7 13 MET b 580  CLA b1223  CLA b1234  CLA b1236                    
SITE     4 WC7 13 BCR b4010                                                     
SITE     1 WC8 17 ALA b 337  SER b 338  VAL b 341  LEU b 345                    
SITE     2 WC8 17 HIS b 349  SER b 352  CLA b1214  CLA b1215                    
SITE     3 WC8 17 CLA b1216  CLA b1221  CLA b1222  CLA b1231                    
SITE     4 WC8 17 CLA b1234  CLA b1236  BCR b4009  BCR b4010                    
SITE     5 WC8 17 LHG b5004                                                     
SITE     1 WC9 10 TRP b  60  SER b 118  ALA b 368  THR b 371                    
SITE     2 WC9 10 HIS b 372  ALA b 719  CLA b1203  CLA b1205                    
SITE     3 WC9 10 CLA b1225  LMG b5002                                          
SITE     1 XC1 17 THR b  61  SER b 118  GLY b 119  TRP b 123                    
SITE     2 XC1 17 THR b 343  MET b 350  TYR b 356  LEU b 369                    
SITE     3 XC1 17 HIS b 372  HIS b 373  ILE b 376  CLA b1203                    
SITE     4 XC1 17 CLA b1210  CLA b1211  CLA b1215  CLA b1224                    
SITE     5 XC1 17 BCR b4005                                                     
SITE     1 XC2 19 ALA b  26  HIS b  29  ASP b  30  HIS b 329                    
SITE     2 XC2 19 LEU b 332  LEU b 336  PHE b 379  GLY b 383                    
SITE     3 XC2 19 HIS b 387  ILE b 390  ARG b 394  TYR b 552                    
SITE     4 XC2 19 TRP b 570  PHE b 573  CLA b1201  CLA b1202                    
SITE     5 XC2 19 CLA b1203  CLA b1239  LMG b5002                               
SITE     1 XC3 14 LEU b 312  THR b 313  VAL b 405  ARG b 408                    
SITE     2 XC3 14 MET b 409  GLU b 411  HIS b 412  LEU b 416                    
SITE     3 XC3 14 HIS b 419  CLA b1220  CLA b1228  CLA b1236                    
SITE     4 XC3 14 BCR b4009  LHG b5004                                          
SITE     1 XC4  7 LYS a 706  CLA a1138  HIS b 419  TRP b 422                    
SITE     2 XC4  7 CLA b1227  CLA b1235  CLA b1236                               
SITE     1 XC5 10 CLA a1138  TRP b 422  LEU b 425  PHE b 426                    
SITE     2 XC5 10 HIS b 430  CLA b1230  CLA b1235  BCR b4014                    
SITE     3 XC5 10 SER f  51  ALA f  58                                          
SITE     1 XC6 10 VAL a 121  CLA a1107  GLY b 433  VAL b 436                    
SITE     2 XC6 10 HIS b 437  LYS b 449  CLA b1229  BCR b4011                    
SITE     3 XC6 10 BCR b4014  TYR f  33                                          
SITE     1 XC7  9 TRP b 460  ILE b 461  SER b 465  LEU b 475                    
SITE     2 XC7  9 TRP b 494  CLA b1214  CLA b1215  CLA b1223                    
SITE     3 XC7  9 CLA b1232                                                     
SITE     1 XC8  6 ILE b 482  THR b 486  TRP b 490  CLA b1214                    
SITE     2 XC8  6 CLA b1231  BCR b4010                                          
SITE     1 XC9 19 GLN b 348  TYR b 351  TYR b 370  PHE b 457                    
SITE     2 XC9 19 ALA b 458  ILE b 461  GLN b 462  PHE b 506                    
SITE     3 XC9 19 LEU b 507  HIS b 517  ILE b 520  LEU b 524                    
SITE     4 XC9 19 LEU b 587  TYR b 590  TRP b 591  CLA b1216                    
SITE     5 XC9 19 CLA b1222  CLA b1223  CLA b1235                               
SITE     1 YC1 15 VAL b 423  PHE b 426  LEU b 427  GLU b 454                    
SITE     2 YC1 15 PRO b 455  VAL b 456  PHE b 457  ALA b 458                    
SITE     3 YC1 15 PHE b 514  HIS b 517  HIS b 518  CLA b1228                    
SITE     4 YC1 15 CLA b1229  CLA b1234  CLA b1236                               
SITE     1 YC2 12 LEU b 420  TRP b 422  VAL b 423  ALA b 521                    
SITE     2 YC2 12 HIS b 525  ILE b 532  CLA b1222  CLA b1223                    
SITE     3 YC2 12 CLA b1227  CLA b1228  CLA b1235  LHG b5004                    
SITE     1 YC3  8 HIS b 308  LYS b 309  PRO b 311  LEU b 312                    
SITE     2 YC3  8 CLA b1219  CLA b1220  BCR b4009  LHG b5004                    
SITE     1 YC4 22 THR a 460  ALA a 463  LEU a 464  CLA a1022                    
SITE     2 YC4 22 ILE b  91  TRP b  92  ASP b  93  HIS b  95                    
SITE     3 YC4 22 ASN b 114  SER b 641  VAL b 642  CLA b1204                    
SITE     4 YC4 22 CLA b1205  CLA b1207  CLA b1239  BCR b4017                    
SITE     5 YC4 22 BCR f4018  PHE i  22  PRO i  23  THR i  26                    
SITE     6 YC4 22 MET i  27  BCR l4019                                          
SITE     1 YC5 14 ILE b 127  GLY b 128  GLY b 138  SER b 186                    
SITE     2 YC5 14 ALA b 189  TRP b 190  HIS b 193  VAL b 197                    
SITE     3 YC5 14 GLY b 208  TRP b 209  PHE b 212  CLA b1212                    
SITE     4 YC5 14 CLA b1225  BCR b4006                                          
SITE     1 YC6 19 CLA a1131  CLA a1237  THR b  18  ILE b  21                    
SITE     2 YC6 19 TRP b  22  ILE b 675  HIS b 679  VAL b 688                    
SITE     3 YC6 19 TRP b 690  LYS b 691  ASP b 692  PRO b 694                    
SITE     4 YC6 19 VAL b 695  PQN b2002  BCR f4018  PHE i  31                    
SITE     5 YC6 19 TYR l  99  THR l 103  BCR l4019                               
SITE     1 YC7 12 CLA a1131  TRP b  22  PHE b 649  MET b 659                    
SITE     2 YC7 12 PHE b 660  ALA b 708  HIS b 709  CLA b1206                    
SITE     3 YC7 12 CLA b1226  PQN b2002  BCR b4017  LMG b5002                    
SITE     1 YC8  5 CYS c  21  CYS c  48  CYS c  51  LYS c  52                    
SITE     2 YC8  5 CYS c  54                                                     
SITE     1 YC9  7 CYS c  11  ILE c  12  GLY c  13  CYS c  14                    
SITE     2 YC9  7 THR c  15  CYS c  17  CYS c  58                               
SITE     1 ZC1  7 CLA a1131  CLA b1206  CLA b1207  CLA b1238                    
SITE     2 ZC1  7 BCR f4020  PHE i  22  PRO i  23                               
SITE     1 ZC2 10 CLA a1131  CLA a1132  CLA a1237  CLA b1207                    
SITE     2 ZC2 10 BCR f4018  TRP i  20  TRP l  65  ALA l  87                    
SITE     3 ZC2 10 LEU l  88  CLA l1502                                          
SITE     1 ZC3  6 TRP a 118  CLA a1101  CLA a1106  CLA a1140                    
SITE     2 ZC3  6 THR f  10  PRO f  12                                          
SITE     1 ZC4  9 PHE l  33  LEU l  37  ARG l  41  GLU l  52                    
SITE     2 ZC4  9 MET l  55  ALA l  56  CLA l1502  CLA l1503                    
SITE     3 ZC4  9 BCR l4022                                                     
SITE     1 ZC5 14 CLA a1237  LEU b 684  BCR f4020  PHE l  33                    
SITE     2 ZC5 14 LEU l  37  PRO l  38  GLU l  52  ALA l  56                    
SITE     3 ZC5 14 HIS l  57  PHE l  60  CLA l1501  CLA l1503                    
SITE     4 ZC5 14 BCR l4019  BCR l4022                                          
SITE     1 ZC6 11 CLA a1132  TYR l  59  PHE l  60  GLY l  63                    
SITE     2 ZC6 11 PRO l  64  THR l  66  ALA l 138  LEU l 142                    
SITE     3 ZC6 11 LEU l 145  CLA l1501  CLA l1502                               
SITE     1 ZC7 11 ILE b  25  CLA b1206  CLA b1238  PQN b2002                    
SITE     2 ZC7 11 MET i  27  LEU i  30  ALA l  92  ALA l  95                    
SITE     3 ZC7 11 LEU l  96  TYR l  99  CLA l1502                               
SITE     1 ZC8  9 BCR 84022  CLA a1132  MET l  55  ALA l  56                    
SITE     2 ZC8  9 TYR l  59  GLY l 133  VAL l 137  CLA l1501                    
SITE     3 ZC8  9 CLA l1502                                                     
SITE     1 ZC9  8 CLA b1201  CLA b1204  LEU m   9  LEU m  12                    
SITE     2 ZC9  8 VAL m  13  LEU m  16  ALA m  19  ALA m  22                    
SITE     1 AD1 10 ALA 1 327  HIS 1 328  LYS 1 329  PHE 1 332                    
SITE     2 AD1 10 CLA 11121  CLA 11122  BCR 14007  LHG 15003                    
SITE     3 AD1 10 PHE b 151  ARG m  24                                          
SITE     1 AD2 14 MET 1 684  PHE 1 685  SER 1 688  GLY 1 689                    
SITE     2 AD2 14 ARG 1 690  TRP 1 693  ALA 1 717  LEU 1 718                    
SITE     3 AD2 14 CLA 11101  CLA 11138  CLA 11139  CLA 11140                    
SITE     4 AD2 14 BCR 24014  ALA 6  11                                          
SITE     1 AD3  4 CYS 1 574  CYS 1 583  CYS 2 556  CYS 2 565                    
SITE     1 AD4 14 PHE 0  77  ALA 0 106  SER 0 109  PHE 0 110                    
SITE     2 AD4 14 PHE 1 263  PHE 1 264  LEU 1 298  VAL 1 302                    
SITE     3 AD4 14 ILE 1 305  HIS 1 309  CLA 11113  CLA 11118                    
SITE     4 AD4 14 CLA 11120  BCR 14002                                          
SITE     1 AD5 14 CLA 01402  PHE 1  84  THR 1 161  GLY 1 164                    
SITE     2 AD5 14 GLY 1 165  MET 1 168  LEU 1 207  GLY 1 211                    
SITE     3 AD5 14 CLA 11103  CLA 11112  CLA 11113  CLA 11118                    
SITE     4 AD5 14 BCR 14001  BCR 14003                                          
SITE     1 AD6  6 GLY 1 208  CLA 11103  CLA 11111  CLA 11118                    
SITE     2 AD6  6 CLA 11127  BCR 14002                                          
SITE     1 AD7  9 ALA 1 350  ILE 1 354  PHE 1 411  CLA 11119                    
SITE     2 AD7  9 CLA 11122  CLA 11123  CLA 11801  BCR 14008                    
SITE     3 AD7  9 LHG 15003                                                     
SITE     1 AD8 10 ALA 1 357  LEU 1 358  SER 1 361  ALA 1 404                    
SITE     2 AD8 10 GLY 1 405  CLA 11119  CLA 11124  CLA 11134                    
SITE     3 AD8 10 CLA 11137  BCR 14007                                          
SITE     1 AD9 16 TRP 1  49  ASN 1  50  HIS 1  52  ALA 1  53                    
SITE     2 AD9 16 ASN 1  54  ARG 1 571  SER 1 719  ILE 1 721                    
SITE     3 AD9 16 GLN 1 722  ALA 1 725  VAL 1 728  ALA 1 729                    
SITE     4 AD9 16 CLA 11102  CLA 11104  CLA 11128  CLA 11140                    
SITE     1 BD1 10 GLY 1 330  PRO 1 331  PHE 1 332  THR 1 333                    
SITE     2 BD1 10 HIS 1 337  CLA 11122  CLA 11129  CLA 11137                    
SITE     3 BD1 10 CLA 11801  BCR 14007                                          
SITE     1 BD2 16 SER 1 438  ASN 1 441  TRP 1 442  ILE 1 445                    
SITE     2 BD2 16 CLA 11130  CLA 11131  ILE 2 675  ALA 2 678                    
SITE     3 BD2 16 THR 2 682  ALA 2 685  CLA 21238  PQN 22002                    
SITE     4 BD2 16 BCR 24017  BCR 64020  CLA 81502  BCR 84019                    
SITE     1 BD3 20 PHE 1 452  ILE 1 456  PHE 1 540  PHE 1 596                    
SITE     2 BD3 20 TRP 1 597  ASN 1 600  ILE 1 642  TYR 1 731                    
SITE     3 BD3 20 CLA 11011  TRP 2 645  LEU 2 648  HIS 2 651                    
SITE     4 BD3 20 LEU 2 652  TRP 2 654  ALA 2 655  CLA 21021                    
SITE     5 BD3 20 CLA 21023  CLA 21206  CLA 21239  BCR 24017                    
SITE     1 BD4 13 TRP 1  47  ILE 1  48  TRP 1  49  LEU 1  51                    
SITE     2 BD4 13 HIS 1  52  CLA 11102  CLA 11109  CLA 11126                    
SITE     3 BD4 13 CLA 11139  CLA 11140  PQN 12001  CLA 21013                    
SITE     4 BD4 13 BCR 24014                                                     
SITE     1 BD5 13 HIS 1  33  PHE 1  34  LEU 1  51  ALA 1  55                    
SITE     2 BD5 13 HIS 1  56  PHE 1  58  GLY 1  78  CLA 11101                    
SITE     3 BD5 13 CLA 11104  CLA 11106  CLA 11107  CLA 11109                    
SITE     4 BD5 13 LHG 15001                                                     
SITE     1 BD6 18 HIS 1  56  PHE 1  58  ILE 1  72  ALA 1  75                    
SITE     2 BD6 18 HIS 1  76  HIS 1  79  LEU 1  80  PHE 1  84                    
SITE     3 BD6 18 TRP 1 348  HIS 1 349  LEU 1 352  ASN 1 355                    
SITE     4 BD6 18 LEU 1 356  CLA 11104  CLA 11123  CLA 11128                    
SITE     5 BD6 18 BCR 14002  BCR 14003                                          
SITE     1 BD7 12 HIS 1  56  HIS 1  79  TRP 1  86  PHE 1 399                    
SITE     2 BD7 12 LEU 1 400  CLA 11102  CLA 11103  CLA 11106                    
SITE     3 BD7 12 CLA 11126  CLA 11127  CLA 11128  LHG 15001                    
SITE     1 BD8 11 VAL 1  85  GLY 1  89  PHE 1  92  HIS 1  93                    
SITE     2 BD8 11 PHE 1  97  VAL 1 116  TRP 1 118  LEU 1 166                    
SITE     3 BD8 11 CLA 11106  CLA 11107  BCR 64013                               
SITE     1 BD9 19 TRP 1  86  MET 1  90  ALA 1 114  GLN 1 115                    
SITE     2 BD9 19 GLN 1 138  ILE 1 139  THR 1 140  SER 1 141                    
SITE     3 BD9 19 LEU 1 143  ALA 1 667  CLA 11102  CLA 11104                    
SITE     4 BD9 19 CLA 11105  CLA 11107  CLA 11109  CLA 11126                    
SITE     5 BD9 19 CLA 11128  BCR 24011  BCR 64013                               
SITE     1 CD1 16 GLN 1 115  VAL 1 116  VAL 1 117  TRP 1 118                    
SITE     2 CD1 16 GLN 1 123  LEU 1 126  ILE 1 137  ILE 1 670                    
SITE     3 CD1 16 CLA 11102  CLA 11105  CLA 11106  CLA 11126                    
SITE     4 CD1 16 VAL 2 440  PHE 2 444  CLA 21230  BCR 64013                    
SITE     1 CD2  9 PHE 1  77  MET 1 172  PHE 1 174  ALA 1 175                    
SITE     2 CD2  9 HIS 1 179  LYS 1 183  TRP 1 189  CLA 11110                    
SITE     3 CD2  9 CLA 11111                                                     
SITE     1 CD3 18 THR 1  23  SER 1  24  PHE 1  25  LYS 1  27                    
SITE     2 CD3 18 TRP 1  28  HIS 1  33  LYS 1  71  SER 1  74                    
SITE     3 CD3 18 GLY 1  78  VAL 1  82  LEU 1 173  GLY 1 176                    
SITE     4 CD3 18 TRP 1 177  TYR 1 180  HIS 1 181  CLA 11101                    
SITE     5 CD3 18 CLA 11102  CLA 11106                                          
SITE     1 CD4  6 TRP 1 189  SER 1 195  HIS 1 199  CLA 11108                    
SITE     2 CD4  6 CLA 11111  CLA 11118                                          
SITE     1 CD5 15 PHE 1  73  HIS 1  76  PHE 1  77  LEU 1  80                    
SITE     2 CD5 15 TRP 1 189  PHE 1 190  ASN 1 192  MET 1 196                    
SITE     3 CD5 15 HIS 1 199  HIS 1 200  LEU 1 204  CLA 11108                    
SITE     4 CD5 15 CLA 11110  CLA 11123  BCR 14003                               
SITE     1 CD6  9 GLY 1 151  PHE 1 152  THR 1 161  GLY 1 211                    
SITE     2 CD6  9 TRP 1 212  HIS 1 215  CLA 11113  CLA 11114                    
SITE     3 CD6  9 BCR 14002                                                     
SITE     1 CD7  9 LEU 1 210  ILE 1 217  HIS 1 218  PHE 1 256                    
SITE     2 CD7  9 GLY 1 259  LEU 1 260  CLA 11112  BCR 14001                    
SITE     3 CD7  9 BCR 14002                                                     
SITE     1 CD8 11 ALA 0  49  CLA 01401  TRP 1 268  LEU 1 275                    
SITE     2 CD8 11 PHE 1 277  HIS 1 295  LEU 1 298  VAL 1 302                    
SITE     3 CD8 11 ASN 1 500  CLA 11116  CLA 11134                               
SITE     1 CD9 15 PHE 1 277  GLY 1 279  ASP 1 292  HIS 1 295                    
SITE     2 CD9 15 HIS 1 296  ALA 1 299  ILE 1 300  LEU 1 303                    
SITE     3 CD9 15 HIS 1 369  MET 1 373  ALA 1 505  CLA 11115                    
SITE     4 CD9 15 CLA 11117  CLA 11125  CLA 11133                               
SITE     1 DD1 16 ALA 1 149  LEU 1 205  GLY 1 208  SER 1 209                    
SITE     2 DD1 16 TRP 1 212  GLN 1 216  HIS 1 296  HIS 1 297                    
SITE     3 DD1 16 ILE 1 300  PHE 1 304  LEU 1 362  PRO 1 375                    
SITE     4 DD1 16 TYR 1 376  CLA 11116  CLA 11119  CLA 11127                    
SITE     1 DD2 14 LEU 0 105  SER 0 109  HIS 1 199  ALA 1 202                    
SITE     2 DD2 14 GLY 1 203  LEU 1 207  ILE 1 305  HIS 1 309                    
SITE     3 DD2 14 THR 1 313  ILE 1 317  CLA 11110  BCR 14001                    
SITE     4 DD2 14 BCR 14002  BCR 14003                                          
SITE     1 DD3 18 MET 1 197  LEU 1 201  LEU 1 205  PHE 1 304                    
SITE     2 DD3 18 MET 1 310  TYR 1 311  MET 1 321  ILE 1 324                    
SITE     3 DD3 18 MET 1 429  VAL 1 553  CLA 11117  CLA 11121                    
SITE     4 DD3 18 CLA 11122  CLA 11123  CLA 11125  CLA 11129                    
SITE     5 DD3 18 BCR 14007  BCR 14008                                          
SITE     1 DD4 14 ILE 1 324  LEU 1 325  HIS 1 328  THR 1 333                    
SITE     2 DD4 14 HIS 1 337  LEU 1 340  MET 1 429  CLA 11119                    
SITE     3 DD4 14 CLA 11123  CLA 11129  CLA 11137  CLA 11801                    
SITE     4 DD4 14 BCR 14007  LHG 15003                                          
SITE     1 DD5 20 HIS 1  76  VAL 1 193  MET 1 196  MET 1 197                    
SITE     2 DD5 20 HIS 1 200  MET 1 321  LEU 1 344  THR 1 346                    
SITE     3 DD5 20 SER 1 347  TRP 1 348  GLN 1 351  ILE 1 354                    
SITE     4 DD5 20 ASN 1 355  LEU 1 358  CLA 11103  CLA 11111                    
SITE     5 DD5 20 CLA 11119  CLA 11122  CLA 11127  BCR 14007                    
SITE     1 DD6 11 ILE 1 364  ILE 1 365  GLN 1 368  ILE 1 401                    
SITE     2 DD6 11 ILE 1 542  THR 1 545  SER 1 601  CLA 11125                    
SITE     3 DD6 11 CLA 11135  CLA 11137  BCR 14008                               
SITE     1 DD7 13 LEU 1 358  GLN 1 368  HIS 1 369  TYR 1 371                    
SITE     2 DD7 13 ALA 1 372  MET 1 373  SER 1 506  PHE 1 509                    
SITE     3 DD7 13 CLA 11116  CLA 11119  CLA 11124  CLA 11133                    
SITE     4 DD7 13 CLA 11135                                                     
SITE     1 DD8 17 TRP 1  86  SER 1 141  THR 1 391  HIS 1 392                    
SITE     2 DD8 17 TRP 1 395  PHE 1 399  MET 1 671  ILE 1 736                    
SITE     3 DD8 17 TRP 1 740  CLA 11012  CLA 11101  CLA 11104                    
SITE     4 DD8 17 CLA 11106  CLA 11107  CLA 11127  CLA 11128                    
SITE     5 DD8 17 BCR 24011                                                     
SITE     1 DD9 15 LEU 1  87  GLY 1 142  LEU 1 146  LEU 1 205                    
SITE     2 DD9 15 THR 1 363  MET 1 370  TYR 1 376  LEU 1 389                    
SITE     3 DD9 15 HIS 1 392  HIS 1 393  CLA 11104  CLA 11117                    
SITE     4 DD9 15 CLA 11123  CLA 11126  BCR 14003                               
SITE     1 ED1 19 HIS 1  52  ALA 1  53  HIS 1  56  ASP 1  57                    
SITE     2 ED1 19 LEU 1 356  PHE 1 399  GLY 1 403  HIS 1 407                    
SITE     3 ED1 19 ILE 1 410  PHE 1 570  ARG 1 571  TRP 1 588                    
SITE     4 ED1 19 CLA 11103  CLA 11104  CLA 11106  CLA 11126                    
SITE     5 ED1 19 CLA 11140  LHG 15001  BCR 24011                               
SITE     1 ED2 11 HIS 1 439  TRP 1 442  CLA 11129  CLA 11137                    
SITE     2 ED2 11 CLA 11237  ALA 2 678  THR 2 682  PRO 2 683                    
SITE     3 ED2 11 THR 8  22  ILE 8  24  SER 8  25                               
SITE     1 ED3 12 TRP 1 442  ILE 1 445  PHE 1 446  PHE 1 449                    
SITE     2 ED3 12 HIS 1 450  CLA 11132  CLA 11136  CLA 11237                    
SITE     3 ED3 12 CLA 21239  PQN 22002  BCR 24017  BCR 64020                    
SITE     1 ED4 12 LEU 1 440  TRP 1 442  VAL 1 443  ILE 1 542                    
SITE     2 ED4 12 HIS 1 543  CLA 11122  CLA 11124  CLA 11129                    
SITE     3 ED4 12 CLA 11130  CLA 11136  BCR 14008  LHG 15003                    
SITE     1 ED5 13 ILE 1 700  ALA 1 703  HIS 1 704  LEU 1 707                    
SITE     2 ED5 13 CLA 11139  PQN 12001  SER 2 418  SER 2 421                    
SITE     3 ED5 13 TRP 2 422  CLA 21228  CLA 21229  BCR 24014                    
SITE     4 ED5 13 GLY 6  62                                                     
SITE     1 ED6 14 THR 1  45  ILE 1  48  TRP 1  49  VAL 1 701                    
SITE     2 ED6 14 HIS 1 704  VAL 1 709  PRO 1 711  PRO 1 715                    
SITE     3 ED6 14 ARG 1 716  CLA 11101  CLA 11138  PQN 12001                    
SITE     4 ED6 14 SER 6   9  GLU 6  82                                          
SITE     1 ED7 17 TRP 1  49  VAL 1 678  PHE 1 681  GLN 1 722                    
SITE     2 ED7 17 VAL 1 726  ALA 1 729  HIS 1 730  LEU 1 733                    
SITE     3 ED7 17 CLA 11012  CLA 11101  CLA 11128  PQN 12001                    
SITE     4 ED7 17 LHG 15001  CLA 21013  BCR 24011  ILE 6  15                    
SITE     5 ED7 17 BCR 64013                                                     
SITE     1 ED8 20 TYR 1 455  THR 1 541  TYR 1 599  ASN 1 600                    
SITE     2 ED8 20 PHE 1 607  ILE 1 642  ALA 1 654  ILE 1 658                    
SITE     3 ED8 20 HIS 1 676  PHE 1 679  TYR 1 731  GLY 1 735                    
SITE     4 ED8 20 THR 1 738  THR 1 739  PHE 1 742  CLA 11012                    
SITE     5 ED8 20 CLA 11022  PHE 2 617  TRP 2 622  CLA 21021                    
SITE     1 ED9 17 LEU 1 673  HIS 1 676  PHE 1 677  ALA 1 680                    
SITE     2 ED9 17 CLA 11011  CLA 11126  CLA 11140  VAL 2 436                    
SITE     3 ED9 17 VAL 2 440  PHE 2 578  TRP 2 579  ASN 2 582                    
SITE     4 ED9 17 LEU 2 613  PHE 2 617  CLA 21013  CLA 21021                    
SITE     5 ED9 17 BCR 24011                                                     
SITE     1 FD1  4 HIS 1 240  ILE 1 243  LEU 1 244  CLA 11112                    
SITE     1 FD2  6 ILE 1 306  HIS 1 309  GLY 1 318  HIS 1 319                    
SITE     2 FD2  6 CLA 11121  BCR 14001                                          
SITE     1 FD3  7 HIS 1 319  ILE 1 324  ALA 1 327  HIS 1 328                    
SITE     2 FD3  7 CLA 11119  CLA 11120  CLA 11801                               
SITE     1 FD4 15 PHE 1 332  THR 1 333  LEU 1 425  ARG 1 428                    
SITE     2 FD4 15 HIS 1 432  HIS 1 439  CLA 11119  CLA 11122                    
SITE     3 FD4 15 CLA 11130  CLA 11137  LHG 15003  VAL 8   8                    
SITE     4 FD4 15 LEU 8  20  PRO 8  23  ILE 8  24                               
SITE     1 FD5 18 PHE 1 449  GLY 1 453  LEU 1 454  ILE 1 456                    
SITE     2 FD5 18 HIS 1 457  THR 1 460  MET 1 461  ARG 1 466                    
SITE     3 FD5 18 ASP 1 469  CLA 11131  HIS 2  95  CLA 21207                    
SITE     4 FD5 18 BCR 64020  PRO 8  64  LEU 8  68  GLY 8  69                    
SITE     5 FD5 18 ARG 8  72  BCR 84022                                          
SITE     1 FD6 10 TRP 1 485  LEU 1 489  HIS 1 490  ALA 1 493                    
SITE     2 FD6 10 THR 1 497  ALA 1 498  CLA 11116  CLA 11125                    
SITE     3 FD6 10 CLA 11134  CLA 11135                                          
SITE     1 FD7  8 CLA 01401  THR 1 497  ALA 1 498  PRO 1 499                    
SITE     2 FD7  8 ASN 1 500  CLA 11115  CLA 11133  BCR 14008                    
SITE     1 FD8 18 GLN 1 368  TYR 1 371  PHE 1 482  ALA 1 483                    
SITE     2 FD8 18 VAL 1 486  GLN 1 487  PHE 1 509  ILE 1 525                    
SITE     3 FD8 18 LEU 1 527  HIS 1 535  HIS 1 538  VAL 1 605                    
SITE     4 FD8 18 HIS 1 608  PHE 1 609  CLA 11124  CLA 11125                    
SITE     5 FD8 18 CLA 11133  CLA 11136                                          
SITE     1 FD9 14 PHE 1 446  LEU 1 447  GLN 1 479  PRO 1 480                    
SITE     2 FD9 14 ILE 1 481  PHE 1 482  ALA 1 483  PHE 1 532                    
SITE     3 FD9 14 HIS 1 535  HIS 1 536  HIS 1 543  CLA 11131                    
SITE     4 FD9 14 CLA 11135  CLA 11137                                          
SITE     1 GD1 15 CLA 11131  CLA 11237  MET 2 659  PHE 2 660                    
SITE     2 GD1 15 SER 2 663  TRP 2 664  ARG 2 665  TRP 2 668                    
SITE     3 GD1 15 ALA 2 696  LEU 2 697  ALA 2 702  CLA 21238                    
SITE     4 GD1 15 CLA 21239  BCR 24017  BCR 84019                               
SITE     1 GD2  6 PHE 2 225  ILE 2 285  HIS 2 289  CLA 21212                    
SITE     2 GD2  6 CLA 21217  CLA 21218                                          
SITE     1 GD3  6 PHE 2 149  SER 2 186  CLA 21203  CLA 21209                    
SITE     2 GD3  6 CLA 21210  CLA 21225                                          
SITE     1 GD4  7 LEU 2  65  MET 2 129  PHE 2 141  LEU 2 142                    
SITE     2 GD4  7 LEU 2 145  CLA 21211  CLA 21212                               
SITE     1 GD5  8 MET 2 409  ILE 2 532  CLA 21219  CLA 21220                    
SITE     2 GD5  8 CLA 21223  CLA 21227  BCR 24010  LHG 25004                    
SITE     1 GD6 13 PHE 2 330  LEU 2 334  ALA 2 337  MET 2 381                    
SITE     2 GD6 13 ALA 2 384  PHE 2 385  GLY 2 388  CLA 21215                    
SITE     3 GD6 13 CLA 21222  CLA 21223  CLA 21234  CLA 21236                    
SITE     4 GD6 13 BCR 24009                                                     
SITE     1 GD7 13 ALA 1 674  PHE 1 677  VAL 1 737  CLA 11012                    
SITE     2 GD7 13 CLA 11106  CLA 11126  CLA 11128  CLA 11140                    
SITE     3 GD7 13 LEU 2 432  CLA 21013  CLA 21229  CLA 21230                    
SITE     4 GD7 13 BCR 24014                                                     
SITE     1 GD8  8 CLA 11101  CLA 11138  PQN 12001  CLA 21013                    
SITE     2 GD8  8 CLA 21229  BCR 24011  ILE 6  53  PHE 6  54                    
SITE     1 GD9 11 CLA 11022  CLA 11131  CLA 11237  TRP 2 645                    
SITE     2 GD9 11 PHE 2 649  TRP 2 668  CLA 21023  CLA 21205                    
SITE     3 GD9 11 CLA 21206  CLA 21239  PQN 22002                               
SITE     1 HD1 16 TYR 2  23  ALA 2  26  SER 2 553  TRP 2 570                    
SITE     2 HD1 16 SER 2 698  VAL 2 700  GLN 2 701  LEU 2 704                    
SITE     3 HD1 16 LEU 2 707  THR 2 711  VAL 2 715  CLA 21201                    
SITE     4 HD1 16 CLA 21203  CLA 21204  CLA 21206  CLA 21226                    
SITE     1 HD2 15 HIS 2 308  LYS 2 309  GLY 2 310  LEU 2 312                    
SITE     2 HD2 15 THR 2 313  HIS 2 317  VAL 2 405  CLA 21220                    
SITE     3 HD2 15 CLA 21222  CLA 21223  CLA 21227  CLA 21228                    
SITE     4 HD2 15 CLA 21236  CLA 21240  BCR 24009                               
SITE     1 HD3 25 PHE 1 677  ALA 1 680  PHE 1 681  LEU 1 683                    
SITE     2 HD3 25 MET 1 684  PHE 1 687  TYR 1 692  TRP 1 693                    
SITE     3 HD3 25 LEU 1 696  CLA 11012  CLA 11101  CLA 11140                    
SITE     4 HD3 25 SER 2 421  SER 2 424  LEU 2 425  GLY 2 428                    
SITE     5 HD3 25 PHE 2 429  LEU 2 522  LEU 2 529  ILE 2 530                    
SITE     6 HD3 25 LEU 2 575  PHE 2 578  TRP 2 579  BCR 24011                    
SITE     7 HD3 25 BCR 24014                                                     
SITE     1 HD4 21 LEU 1 646  LEU 1 650  TRP 1 651  CLA 11011                    
SITE     2 HD4 21 CLA 11012  CLA 11022  TYR 2 435  ALA 2 519                    
SITE     3 HD4 21 ASN 2 582  TRP 2 586  PHE 2 589  LEU 2 613                    
SITE     4 HD4 21 SER 2 625  ILE 2 629  PHE 2 647  HIS 2 651                    
SITE     5 HD4 21 TRP 2 654  TYR 2 714  THR 2 717  TYR 2 718                    
SITE     6 HD4 21 PHE 2 721                                                     
SITE     1 HD5 20 ASN 1 441  CYS 1 444  ILE 1 445  GLY 1 448                    
SITE     2 HD5 20 PHE 1 449  PHE 1 452  PHE 1 540  LEU 1 547                    
SITE     3 HD5 20 ILE 1 548  PHE 1 596  TRP 1 597  CLA 11022                    
SITE     4 HD5 20 ALA 2 655  THR 2 656  PHE 2 658  MET 2 659                    
SITE     5 HD5 20 TYR 2 667  TRP 2 668  LEU 2 671  BCR 24017                    
SITE     1 HD6 15 PHE 2   5  PHE 2   8  ALA 2  28  HIS 2  29                    
SITE     2 HD6 15 HIS 2  34  HIS 2  53  CLA 21202  CLA 21203                    
SITE     3 HD6 15 CLA 21226  LMG 25002  PHE 7  23  SER 7  26                    
SITE     4 HD6 15 LEU 7  29  TYR 7  30  BCR 74021                               
SITE     1 HD7 16 HIS 2  29  PHE 2  31  ILE 2  46  SER 2  49                    
SITE     2 HD7 16 HIS 2  50  HIS 2  53  ILE 2  54  LEU 2 328                    
SITE     3 HD7 16 LEU 2 332  ALA 2 335  LEU 2 336  CLA 21201                    
SITE     4 HD7 16 CLA 21203  CLA 21210  CLA 21221  CLA 21226                    
SITE     1 HD8 11 HIS 2  29  HIS 2  53  ILE 2  57  TRP 2  60                    
SITE     2 HD8 11 CLA 21201  CLA 21202  CLA 21204  CLA 21225                    
SITE     3 HD8 11 CLA 21226  BCR 24005  LMG 25002                               
SITE     1 HD9 22 LEU 2  59  SER 2  62  GLY 2  63  PHE 2  66                    
SITE     2 HD9 22 HIS 2  67  TRP 2  70  GLN 2  71  HIS 2  89                    
SITE     3 HD9 22 LEU 2 143  CLA 21203  CLA 21205  CLA 21206                    
SITE     4 HD9 22 LMG 25002  BCR 64018  ALA 7  11  LEU 7  12                    
SITE     5 HD9 22 ALA 7  15  BCR 74021  LEU 9  10  PRO 9  11                    
SITE     6 HD9 22 ILE 9  15  VAL 9  18                                          
SITE     1 ID1 15 THR 2  64  VAL 2  68  ALA 2  88  HIS 2  89                    
SITE     2 ID1 15 ILE 2 115  ALA 2 116  TYR 2 117  SER 2 118                    
SITE     3 ID1 15 VAL 2 642  TRP 2 643  MET 2 646  CLA 21204                    
SITE     4 ID1 15 CLA 21206  CLA 21224  BCR 24017                               
SITE     1 ID2 24 THR 1 460  ALA 1 463  CLA 11022  HIS 2  89                    
SITE     2 ID2 24 ILE 2  91  TRP 2  92  ASP 2  93  HIS 2  95                    
SITE     3 ID2 24 ASN 2 114  SER 2 641  VAL 2 642  TRP 2 645                    
SITE     4 ID2 24 CLA 21204  CLA 21205  CLA 21207  CLA 21239                    
SITE     5 ID2 24 BCR 24017  LMG 25002  BCR 64018  VAL 9  18                    
SITE     6 ID2 24 PHE 9  22  PRO 9  23  THR 9  26  MET 9  27                    
SITE     1 ID3 10 CLA 11132  HIS 2  95  CLA 21206  BCR 64020                    
SITE     2 ID3 10 TRP 8  65  PRO 8  70  ILE 8  83  ALA 8  87                    
SITE     3 ID3 10 GLY 9  19  TRP 9  20                                          
SITE     1 ID4 10 PHE 2  47  PHE 2  51  LEU 2 148  PHE 2 151                    
SITE     2 ID4 10 ALA 2 152  HIS 2 156  PHE 2 161  TRP 2 167                    
SITE     3 ID4 10 CLA 21209  CLA 21210                                          
SITE     1 ID5  8 TRP 2 167  SER 2 173  HIS 2 177  TRP 2 295                    
SITE     2 ID5  8 CLA 21208  CLA 21210  CLA 21217  BCR 24005                    
SITE     1 ID6 17 PHE 2  47  HIS 2  50  PHE 2  51  ILE 2  54                    
SITE     2 ID6 17 TRP 2 167  PHE 2 168  ARG 2 174  HIS 2 177                    
SITE     3 ID6 17 HIS 2 178  PHE 2 183  TYR 2 356  CLA 21202                    
SITE     4 ID6 17 CLA 21208  CLA 21209  CLA 21215  CLA 21225                    
SITE     5 ID6 17 BCR 24005                                                     
SITE     1 ID7 13 LEU 2 188  GLY 2 192  HIS 2 196  PHE 2 212                    
SITE     2 ID7 13 LEU 2 213  THR 2 215  PRO 2 216  PRO 2 217                    
SITE     3 ID7 13 GLY 2 221  LEU 2 222  CLA 21211  BCR 24004                    
SITE     4 ID7 13 BCR 24006                                                     
SITE     1 ID8 11 TRP 2 230  ALA 2 234  ALA 2 240  LEU 2 255                    
SITE     2 ID8 11 PHE 2 257  LEU 2 258  HIS 2 275  ALA 2 279                    
SITE     3 ID8 11 GLY 2 487  ALA 2 489  CLA 21214                               
SITE     1 ID9 16 PHE 2 257  LEU 2 268  ASP 2 272  HIS 2 275                    
SITE     2 ID9 16 HIS 2 276  ALA 2 279  ILE 2 280  ILE 2 283                    
SITE     3 ID9 16 HIS 2 349  LEU 2 353  TRP 2 490  TRP 2 494                    
SITE     4 ID9 16 CLA 21213  CLA 21215  CLA 21223  CLA 21231                    
SITE     1 JD1 18 TRP 2 123  SER 2 186  SER 2 187  TRP 2 190                    
SITE     2 JD1 18 ILE 2 273  HIS 2 276  HIS 2 277  ILE 2 280                    
SITE     3 JD1 18 ILE 2 342  MET 2 350  SER 2 355  TYR 2 356                    
SITE     4 JD1 18 CLA 21210  CLA 21214  CLA 21216  CLA 21223                    
SITE     5 JD1 18 CLA 21225  BCR 24010                                          
SITE     1 JD2 12 LEU 2 179  PHE 2 183  ILE 2 283  PHE 2 284                    
SITE     2 JD2 12 ALA 2 287  MET 2 290  TYR 2 291  CLA 21215                    
SITE     3 JD2 12 CLA 21218  CLA 21219  CLA 21220  CLA 21221                    
SITE     1 JD3 11 ASN 2 176  HIS 2 177  ALA 2 180  VAL 2 185                    
SITE     2 JD3 11 HIS 2 289  TYR 2 291  THR 2 293  TRP 2 295                    
SITE     3 JD3 11 ILE 2 297  CLA 21209  BCR 24004                               
SITE     1 JD4  7 ILE 2 286  MET 2 290  GLY 2 298  HIS 2 299                    
SITE     2 JD4  7 CLA 21216  CLA 21219  BCR 24004                               
SITE     1 JD5  9 MET 2 290  HIS 2 299  ILE 2 304  ALA 2 307                    
SITE     2 JD5  9 HIS 2 308  CLA 21216  CLA 21218  CLA 21240                    
SITE     3 JD5  9 BCR 24009                                                     
SITE     1 JD6 12 ILE 2 304  LEU 2 305  HIS 2 308  HIS 2 317                    
SITE     2 JD6 12 PHE 2 330  VAL 2 405  CLA 21216  CLA 21221                    
SITE     3 JD6 12 CLA 21227  CLA 21240  BCR 24009  LHG 25004                    
SITE     1 JD7 13 ARG 2 174  HIS 2 178  LEU 2 179  ILE 2 301                    
SITE     2 JD7 13 ILE 2 324  LEU 2 334  ALA 2 335  SER 2 338                    
SITE     3 JD7 13 ILE 2 342  CLA 21202  CLA 21216  CLA 21220                    
SITE     4 JD7 13 CLA 21223                                                     
SITE     1 JD8 17 VAL 2 341  SER 2 344  GLN 2 348  GLN 2 374                    
SITE     2 JD8 17 MET 2 381  PHE 2 385  LEU 2 524  THR 2 527                    
SITE     3 JD8 17 ALA 2 528  LEU 2 531  MET 2 580  LEU 2 587                    
SITE     4 JD8 17 CLA 21223  CLA 21234  CLA 21236  BCR 24010                    
SITE     5 JD8 17 LHG 25004                                                     
SITE     1 JD9 14 VAL 2 341  LEU 2 345  HIS 2 349  SER 2 352                    
SITE     2 JD9 14 CLA 21214  CLA 21215  CLA 21221  CLA 21222                    
SITE     3 JD9 14 CLA 21227  CLA 21231  CLA 21234  BCR 24009                    
SITE     4 JD9 14 BCR 24010  LHG 25004                                          
SITE     1 KD1 12 TRP 2  60  THR 2  64  TYR 2 117  SER 2 118                    
SITE     2 KD1 12 ALA 2 368  THR 2 371  HIS 2 372  LEU 2 716                    
SITE     3 KD1 12 ALA 2 719  LEU 2 722  CLA 21205  CLA 21225                    
SITE     1 KD2 17 TRP 2  60  THR 2  61  GLY 2 119  TRP 2 123                    
SITE     2 KD2 17 ALA 2 189  THR 2 343  MET 2 350  TYR 2 356                    
SITE     3 KD2 17 LEU 2 369  HIS 2 372  HIS 2 373  ILE 2 376                    
SITE     4 KD2 17 CLA 21203  CLA 21210  CLA 21215  CLA 21224                    
SITE     5 KD2 17 BCR 24005                                                     
SITE     1 KD3 17 ILE 2  25  ALA 2  26  HIS 2  29  ASP 2  30                    
SITE     2 KD3 17 HIS 2 329  LEU 2 332  PHE 2 379  GLY 2 383                    
SITE     3 KD3 17 HIS 2 387  ILE 2 390  ARG 2 394  TRP 2 570                    
SITE     4 KD3 17 PHE 2 573  CLA 21201  CLA 21202  CLA 21203                    
SITE     5 KD3 17 LMG 25002                                                     
SITE     1 KD4 14 LEU 2 312  THR 2 313  ARG 2 408  MET 2 409                    
SITE     2 KD4 14 GLU 2 411  HIS 2 412  LEU 2 416  HIS 2 419                    
SITE     3 KD4 14 CLA 21220  CLA 21223  CLA 21228  CLA 21236                    
SITE     4 KD4 14 BCR 24009  LHG 25004                                          
SITE     1 KD5 10 TRP 1 702  LYS 1 706  CLA 11138  HIS 2 419                    
SITE     2 KD5 10 TRP 2 422  CLA 21227  CLA 21229  CLA 21235                    
SITE     3 KD5 10 CLA 21236  LHG 25004                                          
SITE     1 KD6 12 CLA 11138  TRP 2 422  LEU 2 425  PHE 2 426                    
SITE     2 KD6 12 HIS 2 430  CLA 21228  CLA 21230  CLA 21235                    
SITE     3 KD6 12 BCR 24011  BCR 24014  SER 6  51  LEU 6  55                    
SITE     1 KD7  7 CLA 11107  GLY 2 433  VAL 2 436  HIS 2 437                    
SITE     2 KD7  7 LYS 2 449  CLA 21229  BCR 24011                               
SITE     1 KD8 10 ILE 2 461  THR 2 464  SER 2 465  LEU 2 475                    
SITE     2 KD8 10 LEU 2 476  TRP 2 494  CLA 21214  CLA 21223                    
SITE     3 KD8 10 CLA 21232  CLA 21234                                          
SITE     1 KD9  4 LEU 2 475  ILE 2 482  THR 2 486  CLA 21231                    
SITE     1 LD1 19 GLN 2 348  TYR 2 351  TYR 2 370  PHE 2 457                    
SITE     2 LD1 19 ALA 2 458  ILE 2 461  GLN 2 462  PHE 2 506                    
SITE     3 LD1 19 LEU 2 507  HIS 2 517  ILE 2 520  LEU 2 587                    
SITE     4 LD1 19 TYR 2 590  TRP 2 591  CLA 21222  CLA 21223                    
SITE     5 LD1 19 CLA 21231  CLA 21235  BCR 24010                               
SITE     1 LD2 15 VAL 2 423  PHE 2 426  LEU 2 427  GLU 2 454                    
SITE     2 LD2 15 PRO 2 455  VAL 2 456  PHE 2 457  ALA 2 458                    
SITE     3 LD2 15 PHE 2 514  HIS 2 517  HIS 2 518  CLA 21228                    
SITE     4 LD2 15 CLA 21229  CLA 21234  CLA 21236                               
SITE     1 LD3 11 LEU 2 420  TRP 2 422  VAL 2 423  ALA 2 521                    
SITE     2 LD3 11 HIS 2 525  CLA 21222  CLA 21227  CLA 21228                    
SITE     3 LD3 11 CLA 21235  BCR 24010  LHG 25004                               
SITE     1 LD4  6 LYS 2 309  PRO 2 311  LEU 2 312  CLA 21219                    
SITE     2 LD4  6 CLA 21220  LHG 25004                                          
SITE     1 LD5 15 ILE 2 127  GLY 2 128  GLU 2 134  GLY 2 138                    
SITE     2 LD5 15 SER 2 186  ALA 2 189  TRP 2 190  HIS 2 193                    
SITE     3 LD5 15 HIS 2 196  VAL 2 197  GLY 2 208  TRP 2 209                    
SITE     4 LD5 15 PHE 2 212  CLA 21212  BCR 24006                               
SITE     1 LD6 21 CLA 11237  ILE 2  21  TRP 2  22  ILE 2 675                    
SITE     2 LD6 21 VAL 2 676  HIS 2 679  VAL 2 688  TRP 2 690                    
SITE     3 LD6 21 LYS 2 691  ASP 2 692  PRO 2 694  VAL 2 695                    
SITE     4 LD6 21 PQN 22002  BCR 64018  BCR 64020  LEU 8  88                    
SITE     5 LD6 21 TYR 8  99  VAL 8 102  THR 8 103  BCR 84019                    
SITE     6 LD6 21 PHE 9  31                                                     
SITE     1 LD7 12 CLA 11022  CLA 11131  PHE 2 649  LEU 2 652                    
SITE     2 LD7 12 VAL 2 653  MET 2 659  PHE 2 660  VAL 2 705                    
SITE     3 LD7 12 HIS 2 709  CLA 21206  PQN 22002  BCR 24017                    
SITE     1 LD8  5 CYS 3  21  CYS 3  48  CYS 3  51  LYS 3  52                    
SITE     2 LD8  5 CYS 3  54                                                     
SITE     1 LD9  7 CYS 3  11  ILE 3  12  GLY 3  13  CYS 3  14                    
SITE     2 LD9  7 THR 3  15  CYS 3  17  CYS 3  58                               
SITE     1 MD1  6 CLA 21204  CLA 21206  CLA 21238  BCR 64020                    
SITE     2 MD1  6 PHE 9  22  PRO 9  23                                          
SITE     1 MD2 11 CLA 11131  CLA 11132  CLA 11237  CLA 21207                    
SITE     2 MD2 11 CLA 21238  BCR 64018  TRP 8  65  ALA 8  87                    
SITE     3 MD2 11 LEU 8  88  CLA 81502  TRP 9  20                               
SITE     1 MD3  7 TRP 1 118  CLA 11105  CLA 11106  CLA 11107                    
SITE     2 MD3  7 CLA 11140  THR 6  10  PRO 6  12                               
SITE     1 MD4 17 PHE 8  33  ARG 8  41  GLU 8  52  MET 8  55                    
SITE     2 MD4 17 ALA 8  56  CLA 81502  CLA 81503  BCR 84022                    
SITE     3 MD4 17 CLA b1207  TYR i   9  ILE i  13  MET i  17                    
SITE     4 MD4 17 LEU i  21  LEU i  29  THR l  93  ALA l  94                    
SITE     5 MD4 17 SER l  97                                                     
SITE     1 MD5 14 CLA 11237  LEU 2 684  BCR 64020  LEU 8  37                    
SITE     2 MD5 14 PRO 8  38  ALA 8  39  GLU 8  52  VAL 8  53                    
SITE     3 MD5 14 ALA 8  56  HIS 8  57  PHE 8  60  CLA 81501                    
SITE     4 MD5 14 BCR 84019  BCR 84022                                          
SITE     1 MD6 10 TYR 8  59  GLY 8  63  THR 8  66  LEU 8 142                    
SITE     2 MD6 10 CLA 81501  BCR 84022  CLA b1207  TRP i  12                    
SITE     3 MD6 10 PRO i  16  TRP i  20                                          
SITE     1 MD7 11 CLA 11237  ILE 2  25  CLA 21238  PQN 22002                    
SITE     2 MD7 11 ALA 8  92  ALA 8  95  LEU 8  96  PHE 8 127                    
SITE     3 MD7 11 CLA 81502  MET 9  27  PHE 9  31                               
SITE     1 MD8 13 CLA 11132  PHE 8  33  MET 8  55  ALA 8  56                    
SITE     2 MD8 13 GLY 8 133  VAL 8 137  CLA 81501  CLA 81502                    
SITE     3 MD8 13 CLA 81503  CLA b1207  PHE l 128  MET l 132                    
SITE     4 MD8 13 BCR l4022                                                     
SITE     1 MD9 10 LEU 2 150  CLA 21201  CLA 21204  LEU 7   9                    
SITE     2 MD9 10 LEU 7  12  VAL 7  13  LEU 7  16  ALA 7  19                    
SITE     3 MD9 10 ALA 7  22  SER 7  26                                          
SITE     1 ND1  7 CLA A1115  CLA A1134  BCR A4001  ILE K 113                    
SITE     2 ND1  7 LEU K 114  GLY K 117  MET K 118                               
SITE     1 ND2  7 PHE A 263  PHE A 264  SER K  59  ILE K  62                    
SITE     2 ND2  7 LEU K  66  MET K 108  HIS K 112                               
SITE     1 ND3  8 CLA a1115  BCR a4001  PHE k 110  ILE k 113                    
SITE     2 ND3  8 LEU k 114  GLY k 117  MET k 118  LEU k 120                    
SITE     1 ND4  5 PHE a 264  SER k  59  ILE k  62  LEU k  66                    
SITE     2 ND4  5 HIS k 112                                                     
SITE     1 ND5  8 PHE 0 110  ILE 0 113  LEU 0 114  GLY 0 117                    
SITE     2 ND5  8 MET 0 118  LEU 0 120  CLA 11115  CLA 11134                    
SITE     1 ND6  7 SER 0  59  ILE 0  62  LEU 0  66  HIS 0 112                    
SITE     2 ND6  7 PHE 1 263  PHE 1 264  BCR 14002                               
CRYST1  214.619  133.680  219.846  90.00 111.14  90.00 P 1 21 1      6          
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      0.004659  0.000000  0.001802        0.00000                         
SCALE2      0.000000  0.007481  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004877        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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