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Database: PDB
Entry: 5ES4
LinkDB: 5ES4
Original site: 5ES4 
HEADER    CELL ADHESION                           16-NOV-15   5ES4              
TITLE     RE-REFINEMENT OF INTEGRIN ALPHAXBETA2 ECTODOMAIN IN THE CLOSED/BENT   
TITLE    2 CONFORMATION                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-X;                                          
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 20-1103;                                      
COMPND   5 SYNONYM: CD11 ANTIGEN-LIKE FAMILY MEMBER C,LEU M5,LEUKOCYTE ADHESION 
COMPND   6 GLYCOPROTEIN P150,95 ALPHA CHAIN,LEUKOCYTE ADHESION RECEPTOR P150,95;
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-2;                                           
COMPND  10 CHAIN: B, D, F, H;                                                   
COMPND  11 FRAGMENT: UNP RESIDUES 23-696;                                       
COMPND  12 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA-1/CR3/P150,95       
COMPND  13 SUBUNIT BETA,COMPLEMENT RECEPTOR C3 SUBUNIT BETA;                    
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITGAX, CD11C;                                                  
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ITGB2, CD18, MFI7;                                             
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    COMPLEMENT RECEPTOR-4 ALPHAXBETA2, CELL ADHESION                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SEN,T.A.SPRINGER                                                    
REVDAT   3   11-MAY-16 5ES4    1       JRNL                                     
REVDAT   2   13-APR-16 5ES4    1       JRNL                                     
REVDAT   1   06-APR-16 5ES4    0                                                
JRNL        AUTH   M.SEN,T.A.SPRINGER                                           
JRNL        TITL   LEUKOCYTE INTEGRIN ALPHA L BETA 2 HEADPIECE STRUCTURES: THE  
JRNL        TITL 2 ALPHA I DOMAIN, THE POCKET FOR THE INTERNAL LIGAND, AND      
JRNL        TITL 3 CONCERTED MOVEMENTS OF ITS LOOPS.                            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 113  2940 2016              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   26936951                                                     
JRNL        DOI    10.1073/PNAS.1601379113                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 174325                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.258                           
REMARK   3   R VALUE            (WORKING SET) : 0.257                           
REMARK   3   FREE R VALUE                     : 0.307                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1819                            
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 49.5123 -  7.7502    1.00    13892   136  0.2144 0.2548        
REMARK   3     2  7.7502 -  6.1553    1.00    13539   157  0.2721 0.3119        
REMARK   3     3  6.1553 -  5.3783    1.00    13411   126  0.2474 0.3122        
REMARK   3     4  5.3783 -  4.8870    1.00    13305   139  0.2242 0.2983        
REMARK   3     5  4.8870 -  4.5370    1.00    13264   148  0.2152 0.2764        
REMARK   3     6  4.5370 -  4.2697    1.00    13235   156  0.2366 0.2852        
REMARK   3     7  4.2697 -  4.0560    1.00    13243   140  0.2744 0.3089        
REMARK   3     8  4.0560 -  3.8795    0.99    13120   135  0.2929 0.3470        
REMARK   3     9  3.8795 -  3.7302    0.99    13187   133  0.3154 0.3710        
REMARK   3    10  3.7302 -  3.6015    1.00    13152   129  0.3412 0.3978        
REMARK   3    11  3.6015 -  3.4889    1.00    13110   144  0.3748 0.4323        
REMARK   3    12  3.4889 -  3.3892    0.99    13054   139  0.4038 0.4333        
REMARK   3    13  3.3892 -  3.3000    0.98    12994   137  0.4497 0.4375        
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)     : 0.660            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007          52369                                  
REMARK   3   ANGLE     :  1.183          71193                                  
REMARK   3   CHIRALITY :  0.068           8134                                  
REMARK   3   PLANARITY :  0.006           9200                                  
REMARK   3   DIHEDRAL  : 10.662          31783                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 31                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 356 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -23.8475  19.0553 -13.0643              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0907 T22:   0.8894                                     
REMARK   3      T33:   1.0174 T12:   0.1686                                     
REMARK   3      T13:  -0.1897 T23:   0.0583                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5350 L22:  -0.0194                                     
REMARK   3      L33:   1.9736 L12:  -0.0281                                     
REMARK   3      L13:   0.4240 L23:  -0.0136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0710 S12:   0.2877 S13:   0.1536                       
REMARK   3      S21:   0.5312 S22:   0.0820 S23:  -0.1148                       
REMARK   3      S31:   0.2526 S32:  -0.2792 S33:  -0.0007                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 357 THROUGH 639 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.8387  13.1322  33.4337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1710 T22:   0.9972                                     
REMARK   3      T33:   0.9151 T12:   0.0772                                     
REMARK   3      T13:  -0.0584 T23:   0.0620                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0742 L22:   0.6161                                     
REMARK   3      L33:   1.3861 L12:  -0.2979                                     
REMARK   3      L13:   0.4379 L23:  -0.3662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2080 S12:   0.1018 S13:  -0.0881                       
REMARK   3      S21:  -0.5670 S22:  -0.3229 S23:  -0.0015                       
REMARK   3      S31:   0.6908 S32:   0.6632 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 640 THROUGH 1080 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.9024  24.3481  49.6324              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8846 T22:   0.6125                                     
REMARK   3      T33:   0.9151 T12:  -0.0850                                     
REMARK   3      T13:  -0.0063 T23:   0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8000 L22:   0.7717                                     
REMARK   3      L33:   1.0714 L12:   0.9671                                     
REMARK   3      L13:  -1.4503 L23:  -0.8556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2447 S12:   0.2449 S13:  -0.0668                       
REMARK   3      S21:  -0.2238 S22:   0.1569 S23:  -0.0796                       
REMARK   3      S31:   0.1134 S32:  -0.1145 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 213 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1912 -17.4612  19.7820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.0612 T22:   0.7163                                     
REMARK   3      T33:   1.4059 T12:   0.9727                                     
REMARK   3      T13:   0.3294 T23:  -0.2149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2029 L22:   2.4227                                     
REMARK   3      L33:  -0.2099 L12:   0.4320                                     
REMARK   3      L13:   0.0939 L23:   0.3704                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5014 S12:   0.2700 S13:  -0.3386                       
REMARK   3      S21:  -1.2947 S22:  -0.2348 S23:  -0.3760                       
REMARK   3      S31:   0.7022 S32:   0.7436 S33:  -0.0334                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 214 THROUGH 360 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7293 -10.0144   9.5107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.1564 T22:   1.0246                                     
REMARK   3      T33:   0.9320 T12:   0.5109                                     
REMARK   3      T13:   0.3806 T23:   0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8752 L22:   0.0473                                     
REMARK   3      L33:   0.7341 L12:   1.2470                                     
REMARK   3      L13:   1.0325 L23:   0.2268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3774 S12:  -0.0308 S13:  -0.1027                       
REMARK   3      S21:  -1.2514 S22:   0.3798 S23:   0.1059                       
REMARK   3      S31:   1.4433 S32:  -0.0808 S33:   0.0589                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 361 THROUGH 431 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.1412 -22.6481  33.4044              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.0961 T22:   1.7495                                     
REMARK   3      T33:   1.9777 T12:   0.5934                                     
REMARK   3      T13:   0.3271 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7494 L22:   0.3835                                     
REMARK   3      L33:   0.1826 L12:   0.3679                                     
REMARK   3      L13:   0.2502 L23:   0.4006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4171 S12:   0.1674 S13:  -0.6883                       
REMARK   3      S21:  -0.1816 S22:   0.2605 S23:  -0.2681                       
REMARK   3      S31:   1.2230 S32:   0.1080 S33:   0.0001                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 432 THROUGH 482 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -14.3511 -20.8730  75.9306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.4039 T22:   1.0923                                     
REMARK   3      T33:   1.5191 T12:   0.0771                                     
REMARK   3      T13:   0.0755 T23:   0.2545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2008 L22:   0.0402                                     
REMARK   3      L33:  -0.0507 L12:  -0.0336                                     
REMARK   3      L13:  -0.0496 L23:   0.0939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1815 S12:  -0.9226 S13:  -0.0523                       
REMARK   3      S21:   1.2020 S22:   0.1714 S23:  -0.6247                       
REMARK   3      S31:   0.4945 S32:   0.2607 S33:  -0.0067                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 483 THROUGH 674 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5625   8.5697  31.4036              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6011 T22:   1.3644                                     
REMARK   3      T33:   1.2366 T12:   0.1252                                     
REMARK   3      T13:   0.1033 T23:   0.1948                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0168 L22:   0.3744                                     
REMARK   3      L33:   1.0413 L12:   0.3339                                     
REMARK   3      L13:  -0.2293 L23:   0.0267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1618 S12:   0.0115 S13:  -0.0533                       
REMARK   3      S21:  -0.1410 S22:   0.0330 S23:  -0.0297                       
REMARK   3      S31:  -0.0560 S32:   0.3744 S33:   0.0001                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 691 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  24.2543  52.2123 103.5674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0714 T22:   1.6971                                     
REMARK   3      T33:   1.0304 T12:  -0.2065                                     
REMARK   3      T13:  -0.3427 T23:   0.1277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2791 L22:  -0.0443                                     
REMARK   3      L33:   2.1045 L12:   0.0177                                     
REMARK   3      L13:   0.1562 L23:   0.3331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1392 S12:  -0.5806 S13:  -0.0572                       
REMARK   3      S21:   0.3325 S22:   0.0623 S23:  -0.2993                       
REMARK   3      S31:   0.4669 S32:  -0.4254 S33:   0.0013                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 692 THROUGH 1080 )                
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6626  26.9297  84.6488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9046 T22:   1.1136                                     
REMARK   3      T33:   0.9701 T12:  -0.1400                                     
REMARK   3      T13:  -0.0608 T23:   0.1525                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2728 L22:   1.1934                                     
REMARK   3      L33:  -0.7676 L12:   1.2282                                     
REMARK   3      L13:  -0.6990 L23:  -0.4859                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2280 S12:  -0.7463 S13:  -0.2308                       
REMARK   3      S21:   0.4537 S22:  -0.4739 S23:  -0.2659                       
REMARK   3      S31:  -0.1466 S32:   0.4522 S33:  -0.0001                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 114 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  53.0168  19.1363  84.0506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2710 T22:   1.5064                                     
REMARK   3      T33:   2.5413 T12:   0.5055                                     
REMARK   3      T13:  -0.7395 T23:   0.1006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8622 L22:   0.8054                                     
REMARK   3      L33:   0.2355 L12:  -0.2240                                     
REMARK   3      L13:   0.8319 L23:   0.3244                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0515 S12:  -0.4489 S13:  -0.3119                       
REMARK   3      S21:   0.8712 S22:   0.2873 S23:  -1.9268                       
REMARK   3      S31:   0.5190 S32:   0.2002 S33:   0.4020                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 115 THROUGH 464 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.3557  28.0030 113.6542              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6140 T22:   2.4190                                     
REMARK   3      T33:   1.9485 T12:   0.2874                                     
REMARK   3      T13:  -0.7390 T23:   0.2978                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5375 L22:   0.5466                                     
REMARK   3      L33:   0.8805 L12:   0.4454                                     
REMARK   3      L13:   0.1902 L23:   0.8263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2875 S12:  -0.5803 S13:  -0.1037                       
REMARK   3      S21:   0.9077 S22:   0.1172 S23:  -0.6085                       
REMARK   3      S31:   0.5389 S32:  -0.0545 S33:  -0.0001                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 465 THROUGH 552 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1466  37.3821  65.5840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3118 T22:   1.8725                                     
REMARK   3      T33:   1.6731 T12:  -0.1358                                     
REMARK   3      T13:   0.0436 T23:   0.3005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0651 L22:   0.3716                                     
REMARK   3      L33:   0.0550 L12:   0.3442                                     
REMARK   3      L13:   0.1643 L23:   0.2556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2933 S12:  -1.0831 S13:  -1.3964                       
REMARK   3      S21:   0.6804 S22:  -0.4022 S23:   0.3491                       
REMARK   3      S31:  -0.3445 S32:  -0.2646 S33:   0.0001                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 553 THROUGH 674 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7896  10.3725 111.4364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.4834 T22:   2.3111                                     
REMARK   3      T33:   1.8081 T12:  -0.2761                                     
REMARK   3      T13:  -0.3243 T23:   0.3956                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9561 L22:   0.1425                                     
REMARK   3      L33:   0.6229 L12:  -0.3400                                     
REMARK   3      L13:   0.4030 L23:   0.1446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0236 S12:   0.7308 S13:  -0.6598                       
REMARK   3      S21:  -0.0915 S22:   0.9432 S23:  -0.0275                       
REMARK   3      S31:   1.2925 S32:  -1.8916 S33:   0.0002                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 662 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -32.9778  33.6309 114.0189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8609 T22:   1.4674                                     
REMARK   3      T33:   0.8845 T12:  -0.0844                                     
REMARK   3      T13:  -0.0870 T23:   0.0256                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6397 L22:   0.3888                                     
REMARK   3      L33:   3.2576 L12:   0.2250                                     
REMARK   3      L13:   0.9517 L23:   1.1692                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0589 S12:  -0.9337 S13:   0.0294                       
REMARK   3      S21:   0.3804 S22:  -0.0145 S23:   0.0239                       
REMARK   3      S31:   0.4358 S32:  -0.2393 S33:  -0.0003                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 663 THROUGH 1080 )                
REMARK   3    ORIGIN FOR THE GROUP (A): -23.2323  57.0371  87.2665              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7691 T22:   0.9888                                     
REMARK   3      T33:   0.9558 T12:  -0.1658                                     
REMARK   3      T13:  -0.1993 T23:  -0.0565                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2492 L22:   0.2142                                     
REMARK   3      L33:   0.3393 L12:   0.2898                                     
REMARK   3      L13:  -0.1391 L23:   0.1106                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1475 S12:  -0.2997 S13:  -0.0202                       
REMARK   3      S21:   0.2743 S22:  -0.1453 S23:   0.0107                       
REMARK   3      S31:  -0.0142 S32:   0.0843 S33:   0.0000                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 138 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -68.3457  60.3004 109.9680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5041 T22:   1.8722                                     
REMARK   3      T33:   1.6818 T12:   0.6585                                     
REMARK   3      T13:   0.0796 T23:  -0.5674                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3326 L22:   1.8915                                     
REMARK   3      L33:   0.5562 L12:  -0.2167                                     
REMARK   3      L13:  -0.2469 L23:   0.8752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0904 S12:  -0.8106 S13:   0.0466                       
REMARK   3      S21:   0.0497 S22:   0.0363 S23:   0.8037                       
REMARK   3      S31:   0.1534 S32:  -1.1558 S33:   0.0201                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 139 THROUGH 329 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -50.6236  47.4628 142.2594              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4349 T22:   3.1606                                     
REMARK   3      T33:   1.1526 T12:   0.1980                                     
REMARK   3      T13:  -0.1088 T23:  -0.4680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1143 L22:   1.4565                                     
REMARK   3      L33:  -0.0402 L12:   0.2355                                     
REMARK   3      L13:  -0.2830 L23:  -0.5176                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1709 S12:  -1.1006 S13:  -0.0944                       
REMARK   3      S21:   0.1576 S22:  -0.0144 S23:  -0.0098                       
REMARK   3      S31:  -0.0501 S32:  -0.3321 S33:   0.0000                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 330 THROUGH 482 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -68.2545  56.4141 100.2052              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7418 T22:   1.6206                                     
REMARK   3      T33:   1.1040 T12:   0.0958                                     
REMARK   3      T13:  -0.1781 T23:  -0.3731                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0604 L22:   1.4876                                     
REMARK   3      L33:   0.4418 L12:  -1.4932                                     
REMARK   3      L13:  -0.8512 L23:   0.6118                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2156 S12:  -0.2259 S13:   0.2636                       
REMARK   3      S21:   0.0659 S22:   0.1740 S23:  -0.0708                       
REMARK   3      S31:  -1.3949 S32:  -0.3270 S33:   0.0246                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 483 THROUGH 674 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -35.6508  66.5325 106.0644              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1586 T22:   1.4360                                     
REMARK   3      T33:   1.1849 T12:  -0.1830                                     
REMARK   3      T13:  -0.0556 T23:  -0.3506                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6607 L22:   0.1483                                     
REMARK   3      L33:  -0.0455 L12:   0.9404                                     
REMARK   3      L13:  -0.2852 L23:  -0.3347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2429 S12:  -0.5480 S13:   0.3130                       
REMARK   3      S21:   0.2832 S22:  -0.2751 S23:   0.2845                       
REMARK   3      S31:  -0.1578 S32:  -0.4788 S33:  -0.0000                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 1 THROUGH 595 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5575  71.4845  16.2816              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4847 T22:   0.7402                                     
REMARK   3      T33:   1.0635 T12:   0.1494                                     
REMARK   3      T13:  -0.1690 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6784 L22:   1.0807                                     
REMARK   3      L33:   1.4591 L12:   0.3457                                     
REMARK   3      L13:   0.4159 L23:   0.9257                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0963 S12:   0.2738 S13:   0.0629                       
REMARK   3      S21:  -1.0693 S22:  -0.1938 S23:   0.1216                       
REMARK   3      S31:  -0.6160 S32:   0.2550 S33:  -0.0000                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 596 THROUGH 805 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0874  74.9653  66.7027              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6675 T22:   0.5679                                     
REMARK   3      T33:   0.8916 T12:  -0.0137                                     
REMARK   3      T13:  -0.0620 T23:  -0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9784 L22:   1.0632                                     
REMARK   3      L33:   0.3539 L12:   0.2474                                     
REMARK   3      L13:   1.5811 L23:   1.0393                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0148 S12:  -0.0485 S13:   0.1488                       
REMARK   3      S21:   0.0034 S22:  -0.1111 S23:  -0.0742                       
REMARK   3      S31:  -0.0987 S32:  -0.4240 S33:   0.0002                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 806 THROUGH 1080 )                
REMARK   3    ORIGIN FOR THE GROUP (A): -34.0730  53.8071  44.2472              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7835 T22:   0.9442                                     
REMARK   3      T33:   1.0062 T12:  -0.0169                                     
REMARK   3      T13:  -0.1188 T23:   0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9706 L22:   0.7727                                     
REMARK   3      L33:   2.3246 L12:   0.5957                                     
REMARK   3      L13:   0.5162 L23:   1.4744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1092 S12:   0.4143 S13:  -0.0448                       
REMARK   3      S21:  -0.2586 S22:   0.1849 S23:  -0.1019                       
REMARK   3      S31:  -0.2487 S32:  -0.0071 S33:  -0.0000                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 55 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5760 108.4226  64.3220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2734 T22:   1.3884                                     
REMARK   3      T33:   1.8285 T12:   0.2301                                     
REMARK   3      T13:  -0.3036 T23:  -0.2511                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1702 L22:   0.3981                                     
REMARK   3      L33:   0.1983 L12:   0.0333                                     
REMARK   3      L13:   0.1681 L23:  -0.2580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2828 S12:  -0.4666 S13:   0.3192                       
REMARK   3      S21:  -0.4477 S22:  -0.0498 S23:   0.2422                       
REMARK   3      S31:   0.1035 S32:  -0.2548 S33:  -0.0000                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 56 THROUGH 213 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -16.9773 104.0076   4.3038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.0905 T22:   1.4228                                     
REMARK   3      T33:   1.8870 T12:   0.5616                                     
REMARK   3      T13:  -0.5342 T23:   0.1643                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2741 L22:   0.8021                                     
REMARK   3      L33:   0.5041 L12:  -0.0348                                     
REMARK   3      L13:  -1.1657 L23:  -0.9343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2330 S12:   0.7484 S13:   0.2900                       
REMARK   3      S21:  -0.8764 S22:   0.2901 S23:   0.3229                       
REMARK   3      S31:   0.1891 S32:   0.0376 S33:   0.0001                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 214 THROUGH 363 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.7739  98.1485   9.1884              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.2111 T22:   1.3136                                     
REMARK   3      T33:   1.3701 T12:   0.5228                                     
REMARK   3      T13:  -1.0467 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1534 L22:   0.0345                                     
REMARK   3      L33:   0.3869 L12:   0.4307                                     
REMARK   3      L13:  -0.4171 L23:   0.2500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3587 S12:  -0.2886 S13:  -0.2148                       
REMARK   3      S21:  -2.5386 S22:  -0.0111 S23:   0.0209                       
REMARK   3      S31:  -1.4447 S32:  -0.1086 S33:   0.0058                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 364 THROUGH 413 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -23.3730 107.8770  29.2268              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6134 T22:   1.7754                                     
REMARK   3      T33:   2.5923 T12:   0.8671                                     
REMARK   3      T13:  -0.3576 T23:  -0.4484                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4494 L22:   0.1504                                     
REMARK   3      L33:   0.4770 L12:   0.1389                                     
REMARK   3      L13:  -0.1509 L23:  -0.3885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1498 S12:  -1.2560 S13:  -0.0922                       
REMARK   3      S21:   1.1145 S22:   0.0411 S23:   1.2840                       
REMARK   3      S31:  -2.2460 S32:   0.4997 S33:  -0.0205                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 414 THROUGH 452 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.8792 116.5890  59.0051              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.1130 T22:   1.4163                                     
REMARK   3      T33:   2.3566 T12:  -0.3613                                     
REMARK   3      T13:  -0.4336 T23:  -0.0209                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0949 L22:   0.2749                                     
REMARK   3      L33:   0.0503 L12:   0.2947                                     
REMARK   3      L13:  -0.0151 L23:  -0.1671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1503 S12:   0.0608 S13:   0.5736                       
REMARK   3      S21:  -0.1630 S22:  -0.2782 S23:  -0.5553                       
REMARK   3      S31:  -1.0971 S32:  -0.5152 S33:   0.0002                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 453 THROUGH 497 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6654  99.4284  77.1453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9555 T22:   1.0582                                     
REMARK   3      T33:   1.0899 T12:  -0.3163                                     
REMARK   3      T13:  -0.0717 T23:  -0.2419                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7893 L22:   0.3130                                     
REMARK   3      L33:   0.1212 L12:  -0.4264                                     
REMARK   3      L13:   0.1760 L23:  -0.2825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0216 S12:  -0.4311 S13:  -0.7657                       
REMARK   3      S21:   0.2648 S22:   0.5813 S23:  -0.2499                       
REMARK   3      S31:  -1.3844 S32:   0.2747 S33:   0.0390                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 498 THROUGH 637 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.3029  79.2381  37.6724              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4919 T22:   0.9855                                     
REMARK   3      T33:   1.3437 T12:  -0.0186                                     
REMARK   3      T13:  -0.2150 T23:   0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6602 L22:   0.1200                                     
REMARK   3      L33:   0.6020 L12:  -0.1488                                     
REMARK   3      L13:  -0.4682 L23:  -0.1256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3969 S12:   0.3452 S13:  -0.0067                       
REMARK   3      S21:   0.4741 S22:  -0.0094 S23:  -0.0542                       
REMARK   3      S31:   0.4028 S32:  -0.3233 S33:   0.0000                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 638 THROUGH 674 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -46.7688  63.5464  15.9661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5622 T22:   1.0187                                     
REMARK   3      T33:   1.3418 T12:   0.0051                                     
REMARK   3      T13:  -0.1839 T23:  -0.0572                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0784 L22:   0.0976                                     
REMARK   3      L33:   0.1637 L12:  -0.0442                                     
REMARK   3      L13:  -0.0373 L23:  -0.1413                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3058 S12:   0.9430 S13:  -0.2164                       
REMARK   3      S21:   0.3379 S22:   0.6075 S23:  -0.2494                       
REMARK   3      S31:  -0.0703 S32:   0.6374 S33:  -0.0002                       
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 5ES4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000215429.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97926                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 198644                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.20500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.55M TRI-SODIUM CITRATE, 0.1M           
REMARK 280  IMIDAZOLE, PH 6.5, EVAPORATION, TEMPERATURE 277K, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       66.01500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      268.32500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.74000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      268.32500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       66.01500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.74000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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     TYR A  1081                                                      
REMARK 465     LYS A  1082                                                      
REMARK 465     VAL A  1083                                                      
REMARK 465     HIS A  1084                                                      
REMARK 465     GLY A  1085                                                      
REMARK 465     CYS A  1086                                                      
REMARK 465     GLY A  1087                                                      
REMARK 465     GLY A  1088                                                      
REMARK 465     LEU A  1089                                                      
REMARK 465     GLU A  1090                                                      
REMARK 465     ASN A  1091                                                      
REMARK 465     LEU A  1092                                                      
REMARK 465     TYR A  1093                                                      
REMARK 465     PHE A  1094                                                      
REMARK 465     GLN A  1095                                                      
REMARK 465     GLY A  1096                                                      
REMARK 465     GLY A  1097                                                      
REMARK 465     GLU A  1098                                                      
REMARK 465     ASN A  1099                                                      
REMARK 465     ALA A  1100                                                      
REMARK 465     GLN A  1101                                                      
REMARK 465     CYS A  1102                                                      
REMARK 465     GLU A  1103                                                      
REMARK 465     LYS A  1104                                                      
REMARK 465     GLU A  1105                                                      
REMARK 465     LEU A  1106                                                      
REMARK 465     GLN A  1107                                                      
REMARK 465     ALA A  1108                                                      
REMARK 465     LEU A  1109                                                      
REMARK 465     GLU A  1110                                                      
REMARK 465     LYS A  1111                                                      
REMARK 465     GLU A  1112                                                      
REMARK 465     ASN A  1113                                                      
REMARK 465     ALA A  1114                                                      
REMARK 465     GLN A  1115                                                      
REMARK 465     LEU A  1116                                                      
REMARK 465     GLU A  1117                                                      
REMARK 465     TRP A  1118                                                      
REMARK 465     GLU A  1119                                                      
REMARK 465     LEU A  1120                                                      
REMARK 465     GLN A  1121                                                      
REMARK 465     ALA A  1122                                                      
REMARK 465     LEU A  1123                                                      
REMARK 465     GLU A  1124                                                      
REMARK 465     LYS A  1125                                                      
REMARK 465     GLU A  1126                                                      
REMARK 465     LEU A  1127                                                      
REMARK 465     ALA A  1128                                                      
REMARK 465     GLN A  1129                                                      
REMARK 465     TRP A  1130                                                      
REMARK 465     SER A  1131                                                      
REMARK 465     HIS A  1132                                                      
REMARK 465     PRO A  1133                                                      
REMARK 465     GLN A  1134                                                      
REMARK 465     PHE A  1135                                                      
REMARK 465     GLU A  1136                                                      
REMARK 465     LYS A  1137                                                      
REMARK 465     ASP B   675                                                      
REMARK 465     GLY B   676                                                      
REMARK 465     CYS B   677                                                      
REMARK 465     GLY B   678                                                      
REMARK 465     LEU B   679                                                      
REMARK 465     GLU B   680                                                      
REMARK 465     ASN B   681                                                      
REMARK 465     LEU B   682                                                      
REMARK 465     TYR B   683                                                      
REMARK 465     PHE B   684                                                      
REMARK 465     GLN B   685                                                      
REMARK 465     GLY B   686                                                      
REMARK 465     GLY B   687                                                      
REMARK 465     LYS B   688                                                      
REMARK 465     ASN B   689                                                      
REMARK 465     ALA B   690                                                      
REMARK 465     GLN B   691                                                      
REMARK 465     CYS B   692                                                      
REMARK 465     LYS B   693                                                      
REMARK 465     LYS B   694                                                      
REMARK 465     LYS B   695                                                      
REMARK 465     LEU B   696                                                      
REMARK 465     GLN B   697                                                      
REMARK 465     ALA B   698                                                      
REMARK 465     LEU B   699                                                      
REMARK 465     LYS B   700                                                      
REMARK 465     LYS B   701                                                      
REMARK 465     LYS B   702                                                      
REMARK 465     ASN B   703                                                      
REMARK 465     ALA B   704                                                      
REMARK 465     GLN B   705                                                      
REMARK 465     LEU B   706                                                      
REMARK 465     LYS B   707                                                      
REMARK 465     TRP B   708                                                      
REMARK 465     LYS B   709                                                      
REMARK 465     LEU B   710                                                      
REMARK 465     GLN B   711                                                      
REMARK 465     ALA B   712                                                      
REMARK 465     LEU B   713                                                      
REMARK 465     LYS B   714                                                      
REMARK 465     LYS B   715                                                      
REMARK 465     LYS B   716                                                      
REMARK 465     LEU B   717                                                      
REMARK 465     ALA B   718                                                      
REMARK 465     GLN B   719                                                      
REMARK 465     GLY B   720                                                      
REMARK 465     GLY B   721                                                      
REMARK 465     HIS B   722                                                      
REMARK 465     HIS B   723                                                      
REMARK 465     HIS B   724                                                      
REMARK 465     HIS B   725                                                      
REMARK 465     HIS B   726                                                      
REMARK 465     HIS B   727                                                      
REMARK 465     GLU C   130                                                      
REMARK 465     GLN C   131                                                      
REMARK 465     ASP C   132                                                      
REMARK 465     ILE C   133                                                      
REMARK 465     VAL C   134                                                      
REMARK 465     PHE C   135                                                      
REMARK 465     LEU C   136                                                      
REMARK 465     ILE C   137                                                      
REMARK 465     ASP C   138                                                      
REMARK 465     GLY C   139                                                      
REMARK 465     SER C   140                                                      
REMARK 465     GLY C   141                                                      
REMARK 465     SER C   142                                                      
REMARK 465     ILE C   143                                                      
REMARK 465     SER C   144                                                      
REMARK 465     SER C   145                                                      
REMARK 465     ARG C   146                                                      
REMARK 465     ASN C   147                                                      
REMARK 465     PHE C   148                                                      
REMARK 465     ALA C   149                                                      
REMARK 465     THR C   150                                                      
REMARK 465     MET C   151                                                      
REMARK 465     MET C   152                                                      
REMARK 465     ASN C   153                                                      
REMARK 465     PHE C   154                                                      
REMARK 465     VAL C   155                                                      
REMARK 465     ARG C   156                                                      
REMARK 465     ALA C   157                                                      
REMARK 465     VAL C   158                                                      
REMARK 465     ILE C   159                                                      
REMARK 465     SER C   160                                                      
REMARK 465     GLN C   161                                                      
REMARK 465     PHE C   162                                                      
REMARK 465     GLN C   163                                                      
REMARK 465     ARG C   164                                                      
REMARK 465     PRO C   165                                                      
REMARK 465     SER C   166                                                      
REMARK 465     THR C   167                                                      
REMARK 465     GLN C   168                                                      
REMARK 465     PHE C   169                                                      
REMARK 465     SER C   170                                                      
REMARK 465     LEU C   171                                                      
REMARK 465     MET C   172                                                      
REMARK 465     GLN C   173                                                      
REMARK 465     PHE C   174                                                      
REMARK 465     SER C   175                                                      
REMARK 465     ASN C   176                                                      
REMARK 465     LYS C   177                                                      
REMARK 465     PHE C   178                                                      
REMARK 465     GLN C   179                                                      
REMARK 465     THR C   180                                                      
REMARK 465     HIS C   181                                                      
REMARK 465     PHE C   182                                                      
REMARK 465     THR C   183                                                      
REMARK 465     PHE C   184                                                      
REMARK 465     GLU C   185                                                      
REMARK 465     GLU C   186                                                      
REMARK 465     PHE C   187                                                      
REMARK 465     ARG C   188                                                      
REMARK 465     ARG C   189                                                      
REMARK 465     SER C   190                                                      
REMARK 465     SER C   191                                                      
REMARK 465     ASN C   192                                                      
REMARK 465     PRO C   193                                                      
REMARK 465     LEU C   194                                                      
REMARK 465     SER C   195                                                      
REMARK 465     LEU C   196                                                      
REMARK 465     LEU C   197                                                      
REMARK 465     ALA C   198                                                      
REMARK 465     SER C   199                                                      
REMARK 465     VAL C   200                                                      
REMARK 465     HIS C   201                                                      
REMARK 465     GLN C   202                                                      
REMARK 465     LEU C   203                                                      
REMARK 465     GLN C   204                                                      
REMARK 465     GLY C   205                                                      
REMARK 465     PHE C   206                                                      
REMARK 465     THR C   207                                                      
REMARK 465     TYR C   208                                                      
REMARK 465     THR C   209                                                      
REMARK 465     ALA C   210                                                      
REMARK 465     THR C   211                                                      
REMARK 465     ALA C   212                                                      
REMARK 465     ILE C   213                                                      
REMARK 465     GLN C   214                                                      
REMARK 465     ASN C   215                                                      
REMARK 465     VAL C   216                                                      
REMARK 465     VAL C   217                                                      
REMARK 465     HIS C   218                                                      
REMARK 465     ARG C   219                                                      
REMARK 465     LEU C   220                                                      
REMARK 465     PHE C   221                                                      
REMARK 465     HIS C   222                                                      
REMARK 465     ALA C   223                                                      
REMARK 465     SER C   224                                                      
REMARK 465     TYR C   225                                                      
REMARK 465     GLY C   226                                                      
REMARK 465     ALA C   227                                                      
REMARK 465     ARG C   228                                                      
REMARK 465     ARG C   229                                                      
REMARK 465     ASP C   230                                                      
REMARK 465     ALA C   231                                                      
REMARK 465     ALA C   232                                                      
REMARK 465     LYS C   233                                                      
REMARK 465     ILE C   234                                                      
REMARK 465     LEU C   235                                                      
REMARK 465     ILE C   236                                                      
REMARK 465     VAL C   237                                                      
REMARK 465     ILE C   238                                                      
REMARK 465     THR C   239                                                      
REMARK 465     ASP C   240                                                      
REMARK 465     GLY C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     LYS C   243                                                      
REMARK 465     GLU C   244                                                      
REMARK 465     GLY C   245                                                      
REMARK 465     ASP C   246                                                      
REMARK 465     SER C   247                                                      
REMARK 465     LEU C   248                                                      
REMARK 465     ASP C   249                                                      
REMARK 465     TYR C   250                                                      
REMARK 465     LYS C   251                                                      
REMARK 465     ASP C   252                                                      
REMARK 465     VAL C   253                                                      
REMARK 465     ILE C   254                                                      
REMARK 465     PRO C   255                                                      
REMARK 465     MET C   256                                                      
REMARK 465     ALA C   257                                                      
REMARK 465     ASP C   258                                                      
REMARK 465     ALA C   259                                                      
REMARK 465     ALA C   260                                                      
REMARK 465     GLY C   261                                                      
REMARK 465     ILE C   262                                                      
REMARK 465     ILE C   263                                                      
REMARK 465     ARG C   264                                                      
REMARK 465     TYR C   265                                                      
REMARK 465     ALA C   266                                                      
REMARK 465     ILE C   267                                                      
REMARK 465     GLY C   268                                                      
REMARK 465     VAL C   269                                                      
REMARK 465     GLY C   270                                                      
REMARK 465     LEU C   271                                                      
REMARK 465     ALA C   272                                                      
REMARK 465     PHE C   273                                                      
REMARK 465     GLN C   274                                                      
REMARK 465     ASN C   275                                                      
REMARK 465     ARG C   276                                                      
REMARK 465     ASN C   277                                                      
REMARK 465     SER C   278                                                      
REMARK 465     TRP C   279                                                      
REMARK 465     LYS C   280                                                      
REMARK 465     GLU C   281                                                      
REMARK 465     LEU C   282                                                      
REMARK 465     ASN C   283                                                      
REMARK 465     ASP C   284                                                      
REMARK 465     ILE C   285                                                      
REMARK 465     ALA C   286                                                      
REMARK 465     SER C   287                                                      
REMARK 465     LYS C   288                                                      
REMARK 465     PRO C   289                                                      
REMARK 465     SER C   290                                                      
REMARK 465     GLN C   291                                                      
REMARK 465     GLU C   292                                                      
REMARK 465     HIS C   293                                                      
REMARK 465     ILE C   294                                                      
REMARK 465     PHE C   295                                                      
REMARK 465     LYS C   296                                                      
REMARK 465     VAL C   297                                                      
REMARK 465     GLU C   298                                                      
REMARK 465     ASP C   299                                                      
REMARK 465     PHE C   300                                                      
REMARK 465     ASP C   301                                                      
REMARK 465     ALA C   302                                                      
REMARK 465     LEU C   303                                                      
REMARK 465     LYS C   304                                                      
REMARK 465     ASP C   305                                                      
REMARK 465     ILE C   306                                                      
REMARK 465     GLN C   307                                                      
REMARK 465     ASN C   308                                                      
REMARK 465     GLN C   309                                                      
REMARK 465     LEU C   310                                                      
REMARK 465     LYS C   311                                                      
REMARK 465     GLU C   312                                                      
REMARK 465     LYS C   313                                                      
REMARK 465     ILE C   314                                                      
REMARK 465     PHE C   315                                                      
REMARK 465     ALA C   316                                                      
REMARK 465     ILE C   317                                                      
REMARK 465     GLU C   318                                                      
REMARK 465     GLY C   319                                                      
REMARK 465     THR C   320                                                      
REMARK 465     GLU C   321                                                      
REMARK 465     THR C   322                                                      
REMARK 465     THR C   323                                                      
REMARK 465     SER C   324                                                      
REMARK 465     SER C   325                                                      
REMARK 465     TYR C  1081                                                      
REMARK 465     LYS C  1082                                                      
REMARK 465     VAL C  1083                                                      
REMARK 465     HIS C  1084                                                      
REMARK 465     GLY C  1085                                                      
REMARK 465     CYS C  1086                                                      
REMARK 465     GLY C  1087                                                      
REMARK 465     GLY C  1088                                                      
REMARK 465     LEU C  1089                                                      
REMARK 465     GLU C  1090                                                      
REMARK 465     ASN C  1091                                                      
REMARK 465     LEU C  1092                                                      
REMARK 465     TYR C  1093                                                      
REMARK 465     PHE C  1094                                                      
REMARK 465     GLN C  1095                                                      
REMARK 465     GLY C  1096                                                      
REMARK 465     GLY C  1097                                                      
REMARK 465     GLU C  1098                                                      
REMARK 465     ASN C  1099                                                      
REMARK 465     ALA C  1100                                                      
REMARK 465     GLN C  1101                                                      
REMARK 465     CYS C  1102                                                      
REMARK 465     GLU C  1103                                                      
REMARK 465     LYS C  1104                                                      
REMARK 465     GLU C  1105                                                      
REMARK 465     LEU C  1106                                                      
REMARK 465     GLN C  1107                                                      
REMARK 465     ALA C  1108                                                      
REMARK 465     LEU C  1109                                                      
REMARK 465     GLU C  1110                                                      
REMARK 465     LYS C  1111                                                      
REMARK 465     GLU C  1112                                                      
REMARK 465     ASN C  1113                                                      
REMARK 465     ALA C  1114                                                      
REMARK 465     GLN C  1115                                                      
REMARK 465     LEU C  1116                                                      
REMARK 465     GLU C  1117                                                      
REMARK 465     TRP C  1118                                                      
REMARK 465     GLU C  1119                                                      
REMARK 465     LEU C  1120                                                      
REMARK 465     GLN C  1121                                                      
REMARK 465     ALA C  1122                                                      
REMARK 465     LEU C  1123                                                      
REMARK 465     GLU C  1124                                                      
REMARK 465     LYS C  1125                                                      
REMARK 465     GLU C  1126                                                      
REMARK 465     LEU C  1127                                                      
REMARK 465     ALA C  1128                                                      
REMARK 465     GLN C  1129                                                      
REMARK 465     TRP C  1130                                                      
REMARK 465     SER C  1131                                                      
REMARK 465     HIS C  1132                                                      
REMARK 465     PRO C  1133                                                      
REMARK 465     GLN C  1134                                                      
REMARK 465     PHE C  1135                                                      
REMARK 465     GLU C  1136                                                      
REMARK 465     LYS C  1137                                                      
REMARK 465     ASP D   675                                                      
REMARK 465     GLY D   676                                                      
REMARK 465     CYS D   677                                                      
REMARK 465     GLY D   678                                                      
REMARK 465     LEU D   679                                                      
REMARK 465     GLU D   680                                                      
REMARK 465     ASN D   681                                                      
REMARK 465     LEU D   682                                                      
REMARK 465     TYR D   683                                                      
REMARK 465     PHE D   684                                                      
REMARK 465     GLN D   685                                                      
REMARK 465     GLY D   686                                                      
REMARK 465     GLY D   687                                                      
REMARK 465     LYS D   688                                                      
REMARK 465     ASN D   689                                                      
REMARK 465     ALA D   690                                                      
REMARK 465     GLN D   691                                                      
REMARK 465     CYS D   692                                                      
REMARK 465     LYS D   693                                                      
REMARK 465     LYS D   694                                                      
REMARK 465     LYS D   695                                                      
REMARK 465     LEU D   696                                                      
REMARK 465     GLN D   697                                                      
REMARK 465     ALA D   698                                                      
REMARK 465     LEU D   699                                                      
REMARK 465     LYS D   700                                                      
REMARK 465     LYS D   701                                                      
REMARK 465     LYS D   702                                                      
REMARK 465     ASN D   703                                                      
REMARK 465     ALA D   704                                                      
REMARK 465     GLN D   705                                                      
REMARK 465     LEU D   706                                                      
REMARK 465     LYS D   707                                                      
REMARK 465     TRP D   708                                                      
REMARK 465     LYS D   709                                                      
REMARK 465     LEU D   710                                                      
REMARK 465     GLN D   711                                                      
REMARK 465     ALA D   712                                                      
REMARK 465     LEU D   713                                                      
REMARK 465     LYS D   714                                                      
REMARK 465     LYS D   715                                                      
REMARK 465     LYS D   716                                                      
REMARK 465     LEU D   717                                                      
REMARK 465     ALA D   718                                                      
REMARK 465     GLN D   719                                                      
REMARK 465     GLY D   720                                                      
REMARK 465     GLY D   721                                                      
REMARK 465     HIS D   722                                                      
REMARK 465     HIS D   723                                                      
REMARK 465     HIS D   724                                                      
REMARK 465     HIS D   725                                                      
REMARK 465     HIS D   726                                                      
REMARK 465     HIS D   727                                                      
REMARK 465     GLU E   130                                                      
REMARK 465     GLN E   131                                                      
REMARK 465     ASP E   132                                                      
REMARK 465     ILE E   133                                                      
REMARK 465     VAL E   134                                                      
REMARK 465     PHE E   135                                                      
REMARK 465     LEU E   136                                                      
REMARK 465     ILE E   137                                                      
REMARK 465     ASP E   138                                                      
REMARK 465     GLY E   139                                                      
REMARK 465     SER E   140                                                      
REMARK 465     GLY E   141                                                      
REMARK 465     SER E   142                                                      
REMARK 465     ILE E   143                                                      
REMARK 465     SER E   144                                                      
REMARK 465     SER E   145                                                      
REMARK 465     ARG E   146                                                      
REMARK 465     ASN E   147                                                      
REMARK 465     PHE E   148                                                      
REMARK 465     ALA E   149                                                      
REMARK 465     THR E   150                                                      
REMARK 465     MET E   151                                                      
REMARK 465     MET E   152                                                      
REMARK 465     ASN E   153                                                      
REMARK 465     PHE E   154                                                      
REMARK 465     VAL E   155                                                      
REMARK 465     ARG E   156                                                      
REMARK 465     ALA E   157                                                      
REMARK 465     VAL E   158                                                      
REMARK 465     ILE E   159                                                      
REMARK 465     SER E   160                                                      
REMARK 465     GLN E   161                                                      
REMARK 465     PHE E   162                                                      
REMARK 465     GLN E   163                                                      
REMARK 465     ARG E   164                                                      
REMARK 465     PRO E   165                                                      
REMARK 465     SER E   166                                                      
REMARK 465     THR E   167                                                      
REMARK 465     GLN E   168                                                      
REMARK 465     PHE E   169                                                      
REMARK 465     SER E   170                                                      
REMARK 465     LEU E   171                                                      
REMARK 465     MET E   172                                                      
REMARK 465     GLN E   173                                                      
REMARK 465     PHE E   174                                                      
REMARK 465     SER E   175                                                      
REMARK 465     ASN E   176                                                      
REMARK 465     LYS E   177                                                      
REMARK 465     PHE E   178                                                      
REMARK 465     GLN E   179                                                      
REMARK 465     THR E   180                                                      
REMARK 465     HIS E   181                                                      
REMARK 465     PHE E   182                                                      
REMARK 465     THR E   183                                                      
REMARK 465     PHE E   184                                                      
REMARK 465     GLU E   185                                                      
REMARK 465     GLU E   186                                                      
REMARK 465     PHE E   187                                                      
REMARK 465     ARG E   188                                                      
REMARK 465     ARG E   189                                                      
REMARK 465     SER E   190                                                      
REMARK 465     SER E   191                                                      
REMARK 465     ASN E   192                                                      
REMARK 465     PRO E   193                                                      
REMARK 465     LEU E   194                                                      
REMARK 465     SER E   195                                                      
REMARK 465     LEU E   196                                                      
REMARK 465     LEU E   197                                                      
REMARK 465     ALA E   198                                                      
REMARK 465     SER E   199                                                      
REMARK 465     VAL E   200                                                      
REMARK 465     HIS E   201                                                      
REMARK 465     GLN E   202                                                      
REMARK 465     LEU E   203                                                      
REMARK 465     GLN E   204                                                      
REMARK 465     GLY E   205                                                      
REMARK 465     PHE E   206                                                      
REMARK 465     THR E   207                                                      
REMARK 465     TYR E   208                                                      
REMARK 465     THR E   209                                                      
REMARK 465     ALA E   210                                                      
REMARK 465     THR E   211                                                      
REMARK 465     ALA E   212                                                      
REMARK 465     ILE E   213                                                      
REMARK 465     GLN E   214                                                      
REMARK 465     ASN E   215                                                      
REMARK 465     VAL E   216                                                      
REMARK 465     VAL E   217                                                      
REMARK 465     HIS E   218                                                      
REMARK 465     ARG E   219                                                      
REMARK 465     LEU E   220                                                      
REMARK 465     PHE E   221                                                      
REMARK 465     HIS E   222                                                      
REMARK 465     ALA E   223                                                      
REMARK 465     SER E   224                                                      
REMARK 465     TYR E   225                                                      
REMARK 465     GLY E   226                                                      
REMARK 465     ALA E   227                                                      
REMARK 465     ARG E   228                                                      
REMARK 465     ARG E   229                                                      
REMARK 465     ASP E   230                                                      
REMARK 465     ALA E   231                                                      
REMARK 465     ALA E   232                                                      
REMARK 465     LYS E   233                                                      
REMARK 465     ILE E   234                                                      
REMARK 465     LEU E   235                                                      
REMARK 465     ILE E   236                                                      
REMARK 465     VAL E   237                                                      
REMARK 465     ILE E   238                                                      
REMARK 465     THR E   239                                                      
REMARK 465     ASP E   240                                                      
REMARK 465     GLY E   241                                                      
REMARK 465     LYS E   242                                                      
REMARK 465     LYS E   243                                                      
REMARK 465     GLU E   244                                                      
REMARK 465     GLY E   245                                                      
REMARK 465     ASP E   246                                                      
REMARK 465     SER E   247                                                      
REMARK 465     LEU E   248                                                      
REMARK 465     ASP E   249                                                      
REMARK 465     TYR E   250                                                      
REMARK 465     LYS E   251                                                      
REMARK 465     ASP E   252                                                      
REMARK 465     VAL E   253                                                      
REMARK 465     ILE E   254                                                      
REMARK 465     PRO E   255                                                      
REMARK 465     MET E   256                                                      
REMARK 465     ALA E   257                                                      
REMARK 465     ASP E   258                                                      
REMARK 465     ALA E   259                                                      
REMARK 465     ALA E   260                                                      
REMARK 465     GLY E   261                                                      
REMARK 465     ILE E   262                                                      
REMARK 465     ILE E   263                                                      
REMARK 465     ARG E   264                                                      
REMARK 465     TYR E   265                                                      
REMARK 465     ALA E   266                                                      
REMARK 465     ILE E   267                                                      
REMARK 465     GLY E   268                                                      
REMARK 465     VAL E   269                                                      
REMARK 465     GLY E   270                                                      
REMARK 465     LEU E   271                                                      
REMARK 465     ALA E   272                                                      
REMARK 465     PHE E   273                                                      
REMARK 465     GLN E   274                                                      
REMARK 465     ASN E   275                                                      
REMARK 465     ARG E   276                                                      
REMARK 465     ASN E   277                                                      
REMARK 465     SER E   278                                                      
REMARK 465     TRP E   279                                                      
REMARK 465     LYS E   280                                                      
REMARK 465     GLU E   281                                                      
REMARK 465     LEU E   282                                                      
REMARK 465     ASN E   283                                                      
REMARK 465     ASP E   284                                                      
REMARK 465     ILE E   285                                                      
REMARK 465     ALA E   286                                                      
REMARK 465     SER E   287                                                      
REMARK 465     LYS E   288                                                      
REMARK 465     PRO E   289                                                      
REMARK 465     SER E   290                                                      
REMARK 465     GLN E   291                                                      
REMARK 465     GLU E   292                                                      
REMARK 465     HIS E   293                                                      
REMARK 465     ILE E   294                                                      
REMARK 465     PHE E   295                                                      
REMARK 465     LYS E   296                                                      
REMARK 465     VAL E   297                                                      
REMARK 465     GLU E   298                                                      
REMARK 465     ASP E   299                                                      
REMARK 465     PHE E   300                                                      
REMARK 465     ASP E   301                                                      
REMARK 465     ALA E   302                                                      
REMARK 465     LEU E   303                                                      
REMARK 465     LYS E   304                                                      
REMARK 465     ASP E   305                                                      
REMARK 465     ILE E   306                                                      
REMARK 465     GLN E   307                                                      
REMARK 465     ASN E   308                                                      
REMARK 465     GLN E   309                                                      
REMARK 465     LEU E   310                                                      
REMARK 465     LYS E   311                                                      
REMARK 465     GLU E   312                                                      
REMARK 465     LYS E   313                                                      
REMARK 465     ILE E   314                                                      
REMARK 465     PHE E   315                                                      
REMARK 465     ALA E   316                                                      
REMARK 465     ILE E   317                                                      
REMARK 465     GLU E   318                                                      
REMARK 465     GLY E   319                                                      
REMARK 465     THR E   320                                                      
REMARK 465     GLU E   321                                                      
REMARK 465     THR E   322                                                      
REMARK 465     THR E   323                                                      
REMARK 465     SER E   324                                                      
REMARK 465     SER E   325                                                      
REMARK 465     TYR E  1081                                                      
REMARK 465     LYS E  1082                                                      
REMARK 465     VAL E  1083                                                      
REMARK 465     HIS E  1084                                                      
REMARK 465     GLY E  1085                                                      
REMARK 465     CYS E  1086                                                      
REMARK 465     GLY E  1087                                                      
REMARK 465     GLY E  1088                                                      
REMARK 465     LEU E  1089                                                      
REMARK 465     GLU E  1090                                                      
REMARK 465     ASN E  1091                                                      
REMARK 465     LEU E  1092                                                      
REMARK 465     TYR E  1093                                                      
REMARK 465     PHE E  1094                                                      
REMARK 465     GLN E  1095                                                      
REMARK 465     GLY E  1096                                                      
REMARK 465     GLY E  1097                                                      
REMARK 465     GLU E  1098                                                      
REMARK 465     ASN E  1099                                                      
REMARK 465     ALA E  1100                                                      
REMARK 465     GLN E  1101                                                      
REMARK 465     CYS E  1102                                                      
REMARK 465     GLU E  1103                                                      
REMARK 465     LYS E  1104                                                      
REMARK 465     GLU E  1105                                                      
REMARK 465     LEU E  1106                                                      
REMARK 465     GLN E  1107                                                      
REMARK 465     ALA E  1108                                                      
REMARK 465     LEU E  1109                                                      
REMARK 465     GLU E  1110                                                      
REMARK 465     LYS E  1111                                                      
REMARK 465     GLU E  1112                                                      
REMARK 465     ASN E  1113                                                      
REMARK 465     ALA E  1114                                                      
REMARK 465     GLN E  1115                                                      
REMARK 465     LEU E  1116                                                      
REMARK 465     GLU E  1117                                                      
REMARK 465     TRP E  1118                                                      
REMARK 465     GLU E  1119                                                      
REMARK 465     LEU E  1120                                                      
REMARK 465     GLN E  1121                                                      
REMARK 465     ALA E  1122                                                      
REMARK 465     LEU E  1123                                                      
REMARK 465     GLU E  1124                                                      
REMARK 465     LYS E  1125                                                      
REMARK 465     GLU E  1126                                                      
REMARK 465     LEU E  1127                                                      
REMARK 465     ALA E  1128                                                      
REMARK 465     GLN E  1129                                                      
REMARK 465     TRP E  1130                                                      
REMARK 465     SER E  1131                                                      
REMARK 465     HIS E  1132                                                      
REMARK 465     PRO E  1133                                                      
REMARK 465     GLN E  1134                                                      
REMARK 465     PHE E  1135                                                      
REMARK 465     GLU E  1136                                                      
REMARK 465     LYS E  1137                                                      
REMARK 465     ASP F   675                                                      
REMARK 465     GLY F   676                                                      
REMARK 465     CYS F   677                                                      
REMARK 465     GLY F   678                                                      
REMARK 465     LEU F   679                                                      
REMARK 465     GLU F   680                                                      
REMARK 465     ASN F   681                                                      
REMARK 465     LEU F   682                                                      
REMARK 465     TYR F   683                                                      
REMARK 465     PHE F   684                                                      
REMARK 465     GLN F   685                                                      
REMARK 465     GLY F   686                                                      
REMARK 465     GLY F   687                                                      
REMARK 465     LYS F   688                                                      
REMARK 465     ASN F   689                                                      
REMARK 465     ALA F   690                                                      
REMARK 465     GLN F   691                                                      
REMARK 465     CYS F   692                                                      
REMARK 465     LYS F   693                                                      
REMARK 465     LYS F   694                                                      
REMARK 465     LYS F   695                                                      
REMARK 465     LEU F   696                                                      
REMARK 465     GLN F   697                                                      
REMARK 465     ALA F   698                                                      
REMARK 465     LEU F   699                                                      
REMARK 465     LYS F   700                                                      
REMARK 465     LYS F   701                                                      
REMARK 465     LYS F   702                                                      
REMARK 465     ASN F   703                                                      
REMARK 465     ALA F   704                                                      
REMARK 465     GLN F   705                                                      
REMARK 465     LEU F   706                                                      
REMARK 465     LYS F   707                                                      
REMARK 465     TRP F   708                                                      
REMARK 465     LYS F   709                                                      
REMARK 465     LEU F   710                                                      
REMARK 465     GLN F   711                                                      
REMARK 465     ALA F   712                                                      
REMARK 465     LEU F   713                                                      
REMARK 465     LYS F   714                                                      
REMARK 465     LYS F   715                                                      
REMARK 465     LYS F   716                                                      
REMARK 465     LEU F   717                                                      
REMARK 465     ALA F   718                                                      
REMARK 465     GLN F   719                                                      
REMARK 465     GLY F   720                                                      
REMARK 465     GLY F   721                                                      
REMARK 465     HIS F   722                                                      
REMARK 465     HIS F   723                                                      
REMARK 465     HIS F   724                                                      
REMARK 465     HIS F   725                                                      
REMARK 465     HIS F   726                                                      
REMARK 465     HIS F   727                                                      
REMARK 465     GLN G   129                                                      
REMARK 465     GLU G   130                                                      
REMARK 465     GLN G   131                                                      
REMARK 465     ASP G   132                                                      
REMARK 465     ILE G   133                                                      
REMARK 465     VAL G   134                                                      
REMARK 465     PHE G   135                                                      
REMARK 465     LEU G   136                                                      
REMARK 465     ILE G   137                                                      
REMARK 465     ASP G   138                                                      
REMARK 465     GLY G   139                                                      
REMARK 465     SER G   140                                                      
REMARK 465     GLY G   141                                                      
REMARK 465     SER G   142                                                      
REMARK 465     ILE G   143                                                      
REMARK 465     SER G   144                                                      
REMARK 465     SER G   145                                                      
REMARK 465     ARG G   146                                                      
REMARK 465     ASN G   147                                                      
REMARK 465     PHE G   148                                                      
REMARK 465     ALA G   149                                                      
REMARK 465     THR G   150                                                      
REMARK 465     MET G   151                                                      
REMARK 465     MET G   152                                                      
REMARK 465     ASN G   153                                                      
REMARK 465     PHE G   154                                                      
REMARK 465     VAL G   155                                                      
REMARK 465     ARG G   156                                                      
REMARK 465     ALA G   157                                                      
REMARK 465     VAL G   158                                                      
REMARK 465     ILE G   159                                                      
REMARK 465     SER G   160                                                      
REMARK 465     GLN G   161                                                      
REMARK 465     PHE G   162                                                      
REMARK 465     GLN G   163                                                      
REMARK 465     ARG G   164                                                      
REMARK 465     PRO G   165                                                      
REMARK 465     SER G   166                                                      
REMARK 465     THR G   167                                                      
REMARK 465     GLN G   168                                                      
REMARK 465     PHE G   169                                                      
REMARK 465     SER G   170                                                      
REMARK 465     LEU G   171                                                      
REMARK 465     MET G   172                                                      
REMARK 465     GLN G   173                                                      
REMARK 465     PHE G   174                                                      
REMARK 465     SER G   175                                                      
REMARK 465     ASN G   176                                                      
REMARK 465     LYS G   177                                                      
REMARK 465     PHE G   178                                                      
REMARK 465     GLN G   179                                                      
REMARK 465     THR G   180                                                      
REMARK 465     HIS G   181                                                      
REMARK 465     PHE G   182                                                      
REMARK 465     THR G   183                                                      
REMARK 465     PHE G   184                                                      
REMARK 465     GLU G   185                                                      
REMARK 465     GLU G   186                                                      
REMARK 465     PHE G   187                                                      
REMARK 465     ARG G   188                                                      
REMARK 465     ARG G   189                                                      
REMARK 465     SER G   190                                                      
REMARK 465     SER G   191                                                      
REMARK 465     ASN G   192                                                      
REMARK 465     PRO G   193                                                      
REMARK 465     LEU G   194                                                      
REMARK 465     SER G   195                                                      
REMARK 465     LEU G   196                                                      
REMARK 465     LEU G   197                                                      
REMARK 465     ALA G   198                                                      
REMARK 465     SER G   199                                                      
REMARK 465     VAL G   200                                                      
REMARK 465     HIS G   201                                                      
REMARK 465     GLN G   202                                                      
REMARK 465     LEU G   203                                                      
REMARK 465     GLN G   204                                                      
REMARK 465     GLY G   205                                                      
REMARK 465     PHE G   206                                                      
REMARK 465     THR G   207                                                      
REMARK 465     TYR G   208                                                      
REMARK 465     THR G   209                                                      
REMARK 465     ALA G   210                                                      
REMARK 465     THR G   211                                                      
REMARK 465     ALA G   212                                                      
REMARK 465     ILE G   213                                                      
REMARK 465     GLN G   214                                                      
REMARK 465     ASN G   215                                                      
REMARK 465     VAL G   216                                                      
REMARK 465     VAL G   217                                                      
REMARK 465     HIS G   218                                                      
REMARK 465     ARG G   219                                                      
REMARK 465     LEU G   220                                                      
REMARK 465     PHE G   221                                                      
REMARK 465     HIS G   222                                                      
REMARK 465     ALA G   223                                                      
REMARK 465     SER G   224                                                      
REMARK 465     TYR G   225                                                      
REMARK 465     GLY G   226                                                      
REMARK 465     ALA G   227                                                      
REMARK 465     ARG G   228                                                      
REMARK 465     ARG G   229                                                      
REMARK 465     ASP G   230                                                      
REMARK 465     ALA G   231                                                      
REMARK 465     ALA G   232                                                      
REMARK 465     LYS G   233                                                      
REMARK 465     ILE G   234                                                      
REMARK 465     LEU G   235                                                      
REMARK 465     ILE G   236                                                      
REMARK 465     VAL G   237                                                      
REMARK 465     ILE G   238                                                      
REMARK 465     THR G   239                                                      
REMARK 465     ASP G   240                                                      
REMARK 465     GLY G   241                                                      
REMARK 465     LYS G   242                                                      
REMARK 465     LYS G   243                                                      
REMARK 465     GLU G   244                                                      
REMARK 465     GLY G   245                                                      
REMARK 465     ASP G   246                                                      
REMARK 465     SER G   247                                                      
REMARK 465     LEU G   248                                                      
REMARK 465     ASP G   249                                                      
REMARK 465     TYR G   250                                                      
REMARK 465     LYS G   251                                                      
REMARK 465     ASP G   252                                                      
REMARK 465     VAL G   253                                                      
REMARK 465     ILE G   254                                                      
REMARK 465     PRO G   255                                                      
REMARK 465     MET G   256                                                      
REMARK 465     ALA G   257                                                      
REMARK 465     ASP G   258                                                      
REMARK 465     ALA G   259                                                      
REMARK 465     ALA G   260                                                      
REMARK 465     GLY G   261                                                      
REMARK 465     ILE G   262                                                      
REMARK 465     ILE G   263                                                      
REMARK 465     ARG G   264                                                      
REMARK 465     TYR G   265                                                      
REMARK 465     ALA G   266                                                      
REMARK 465     ILE G   267                                                      
REMARK 465     GLY G   268                                                      
REMARK 465     VAL G   269                                                      
REMARK 465     GLY G   270                                                      
REMARK 465     LEU G   271                                                      
REMARK 465     ALA G   272                                                      
REMARK 465     PHE G   273                                                      
REMARK 465     GLN G   274                                                      
REMARK 465     ASN G   275                                                      
REMARK 465     ARG G   276                                                      
REMARK 465     ASN G   277                                                      
REMARK 465     SER G   278                                                      
REMARK 465     TRP G   279                                                      
REMARK 465     LYS G   280                                                      
REMARK 465     GLU G   281                                                      
REMARK 465     LEU G   282                                                      
REMARK 465     ASN G   283                                                      
REMARK 465     ASP G   284                                                      
REMARK 465     ILE G   285                                                      
REMARK 465     ALA G   286                                                      
REMARK 465     SER G   287                                                      
REMARK 465     LYS G   288                                                      
REMARK 465     PRO G   289                                                      
REMARK 465     SER G   290                                                      
REMARK 465     GLN G   291                                                      
REMARK 465     GLU G   292                                                      
REMARK 465     HIS G   293                                                      
REMARK 465     ILE G   294                                                      
REMARK 465     PHE G   295                                                      
REMARK 465     LYS G   296                                                      
REMARK 465     VAL G   297                                                      
REMARK 465     GLU G   298                                                      
REMARK 465     ASP G   299                                                      
REMARK 465     PHE G   300                                                      
REMARK 465     ASP G   301                                                      
REMARK 465     ALA G   302                                                      
REMARK 465     LEU G   303                                                      
REMARK 465     LYS G   304                                                      
REMARK 465     ASP G   305                                                      
REMARK 465     ILE G   306                                                      
REMARK 465     GLN G   307                                                      
REMARK 465     ASN G   308                                                      
REMARK 465     GLN G   309                                                      
REMARK 465     LEU G   310                                                      
REMARK 465     LYS G   311                                                      
REMARK 465     GLU G   312                                                      
REMARK 465     LYS G   313                                                      
REMARK 465     ILE G   314                                                      
REMARK 465     PHE G   315                                                      
REMARK 465     ALA G   316                                                      
REMARK 465     ILE G   317                                                      
REMARK 465     GLU G   318                                                      
REMARK 465     GLY G   319                                                      
REMARK 465     THR G   320                                                      
REMARK 465     GLU G   321                                                      
REMARK 465     THR G   322                                                      
REMARK 465     THR G   323                                                      
REMARK 465     SER G   324                                                      
REMARK 465     SER G   325                                                      
REMARK 465     TYR G  1081                                                      
REMARK 465     LYS G  1082                                                      
REMARK 465     VAL G  1083                                                      
REMARK 465     HIS G  1084                                                      
REMARK 465     GLY G  1085                                                      
REMARK 465     CYS G  1086                                                      
REMARK 465     GLY G  1087                                                      
REMARK 465     GLY G  1088                                                      
REMARK 465     LEU G  1089                                                      
REMARK 465     GLU G  1090                                                      
REMARK 465     ASN G  1091                                                      
REMARK 465     LEU G  1092                                                      
REMARK 465     TYR G  1093                                                      
REMARK 465     PHE G  1094                                                      
REMARK 465     GLN G  1095                                                      
REMARK 465     GLY G  1096                                                      
REMARK 465     GLY G  1097                                                      
REMARK 465     GLU G  1098                                                      
REMARK 465     ASN G  1099                                                      
REMARK 465     ALA G  1100                                                      
REMARK 465     GLN G  1101                                                      
REMARK 465     CYS G  1102                                                      
REMARK 465     GLU G  1103                                                      
REMARK 465     LYS G  1104                                                      
REMARK 465     GLU G  1105                                                      
REMARK 465     LEU G  1106                                                      
REMARK 465     GLN G  1107                                                      
REMARK 465     ALA G  1108                                                      
REMARK 465     LEU G  1109                                                      
REMARK 465     GLU G  1110                                                      
REMARK 465     LYS G  1111                                                      
REMARK 465     GLU G  1112                                                      
REMARK 465     ASN G  1113                                                      
REMARK 465     ALA G  1114                                                      
REMARK 465     GLN G  1115                                                      
REMARK 465     LEU G  1116                                                      
REMARK 465     GLU G  1117                                                      
REMARK 465     TRP G  1118                                                      
REMARK 465     GLU G  1119                                                      
REMARK 465     LEU G  1120                                                      
REMARK 465     GLN G  1121                                                      
REMARK 465     ALA G  1122                                                      
REMARK 465     LEU G  1123                                                      
REMARK 465     GLU G  1124                                                      
REMARK 465     LYS G  1125                                                      
REMARK 465     GLU G  1126                                                      
REMARK 465     LEU G  1127                                                      
REMARK 465     ALA G  1128                                                      
REMARK 465     GLN G  1129                                                      
REMARK 465     TRP G  1130                                                      
REMARK 465     SER G  1131                                                      
REMARK 465     HIS G  1132                                                      
REMARK 465     PRO G  1133                                                      
REMARK 465     GLN G  1134                                                      
REMARK 465     PHE G  1135                                                      
REMARK 465     GLU G  1136                                                      
REMARK 465     LYS G  1137                                                      
REMARK 465     ASP H   675                                                      
REMARK 465     GLY H   676                                                      
REMARK 465     CYS H   677                                                      
REMARK 465     GLY H   678                                                      
REMARK 465     LEU H   679                                                      
REMARK 465     GLU H   680                                                      
REMARK 465     ASN H   681                                                      
REMARK 465     LEU H   682                                                      
REMARK 465     TYR H   683                                                      
REMARK 465     PHE H   684                                                      
REMARK 465     GLN H   685                                                      
REMARK 465     GLY H   686                                                      
REMARK 465     GLY H   687                                                      
REMARK 465     LYS H   688                                                      
REMARK 465     ASN H   689                                                      
REMARK 465     ALA H   690                                                      
REMARK 465     GLN H   691                                                      
REMARK 465     CYS H   692                                                      
REMARK 465     LYS H   693                                                      
REMARK 465     LYS H   694                                                      
REMARK 465     LYS H   695                                                      
REMARK 465     LEU H   696                                                      
REMARK 465     GLN H   697                                                      
REMARK 465     ALA H   698                                                      
REMARK 465     LEU H   699                                                      
REMARK 465     LYS H   700                                                      
REMARK 465     LYS H   701                                                      
REMARK 465     LYS H   702                                                      
REMARK 465     ASN H   703                                                      
REMARK 465     ALA H   704                                                      
REMARK 465     GLN H   705                                                      
REMARK 465     LEU H   706                                                      
REMARK 465     LYS H   707                                                      
REMARK 465     TRP H   708                                                      
REMARK 465     LYS H   709                                                      
REMARK 465     LEU H   710                                                      
REMARK 465     GLN H   711                                                      
REMARK 465     ALA H   712                                                      
REMARK 465     LEU H   713                                                      
REMARK 465     LYS H   714                                                      
REMARK 465     LYS H   715                                                      
REMARK 465     LYS H   716                                                      
REMARK 465     LEU H   717                                                      
REMARK 465     ALA H   718                                                      
REMARK 465     GLN H   719                                                      
REMARK 465     GLY H   720                                                      
REMARK 465     GLY H   721                                                      
REMARK 465     HIS H   722                                                      
REMARK 465     HIS H   723                                                      
REMARK 465     HIS H   724                                                      
REMARK 465     HIS H   725                                                      
REMARK 465     HIS H   726                                                      
REMARK 465     HIS H   727                                                      
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     ARG D 143    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER E 326    OG                                                  
REMARK 470     ARG G 480    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP G 482    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP G 482    CZ3  CH2                                            
REMARK 470     ARG G 483    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G 484    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G1080    CG   CD   CE   NZ                                   
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   ND2  ASN E   920     O5   NAG E  3920              1.94            
REMARK 500   ND2  ASN H   190     O5   NAG H  3190              1.98            
REMARK 500   ND2  ASN E   678     O5   NAG E  3678              2.04            
REMARK 500   ND2  ASN C   678     O5   NAG C  3678              2.05            
REMARK 500   ND2  ASN F   190     O5   NAG F  3190              2.07            
REMARK 500   O2   BMA G  3375     O6   MAN G  3380              2.11            
REMARK 500   OH   TYR C   741     O5   NAG C  3716              2.11            
REMARK 500   ND2  ASN E   678     C2   NAG E  3678              2.12            
REMARK 500   ND2  ASN E   716     O5   NAG E  3716              2.13            
REMARK 500   OD2  ASP E   451     O    HOH E  4001              2.15            
REMARK 500   OG   SER A   929     O7   NAG A  3031              2.15            
REMARK 500   ND2  ASN G   678     O5   NAG G  3678              2.16            
REMARK 500   ND2  ASN G   678     C2   NAG G  3678              2.17            
REMARK 500   OG   SER C   929     O7   NAG C  3031              2.17            
REMARK 500   O    THR C   411     O    HOH C  4001              2.17            
REMARK 500   O3   NAG C  3071     O2   BMA C  3072              2.17            
REMARK 500   ND2  ASN C   920     C2   NAG C  3920              2.17            
REMARK 500   ND2  ASN A   678     O5   NAG A  3678              2.17            
REMARK 500   OE2  GLU E   335     OH   TYR E   363              2.18            
REMARK 500   O4   NAG E  3070     C2   NAG E  3071              2.18            
REMARK 500   ND2  ASN C   880     C2   NAG C  3880              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU D    64     O4   MAN E  3719     1655     2.02            
REMARK 500   ND2  ASN A   192     O    PRO A   986     4455     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS C 722   C     PRO C 723   N       0.213                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 663   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 663   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    LEU B 654   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    CYS C 703   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES          
REMARK 500    LEU D 266   CA  -  CB  -  CG  ANGL. DEV. = -15.4 DEGREES          
REMARK 500    CYS D 448   CA  -  CB  -  SG  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    LEU E  73   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LEU E 115   CA  -  CB  -  CG  ANGL. DEV. =  18.4 DEGREES          
REMARK 500    LEU G  73   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ARG H 432   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    CYS H 609   CA  -  CB  -  SG  ANGL. DEV. =  10.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  28      -38.86   -142.26                                   
REMARK 500    ASN A  42       44.31     37.53                                   
REMARK 500    ASN A  70       61.58     17.12                                   
REMARK 500    CYS A  97       61.97   -105.98                                   
REMARK 500    ARG A 128      170.14     64.67                                   
REMARK 500    SER A 175     -105.93   -167.67                                   
REMARK 500    ASN A 192       59.50   -142.52                                   
REMARK 500    SER A 199       41.37    -76.51                                   
REMARK 500    GLN A 204     -162.46     57.36                                   
REMARK 500    PHE A 206     -152.72    -75.18                                   
REMARK 500    TYR A 208       69.82   -112.94                                   
REMARK 500    ARG A 219      -63.60   -122.27                                   
REMARK 500    ARG A 229      -77.63    -45.79                                   
REMARK 500    GLU A 298      -73.24    -66.47                                   
REMARK 500    ASP A 299     -137.48   -110.40                                   
REMARK 500    ALA A 316       65.57    -68.75                                   
REMARK 500    THR A 323       68.87     21.28                                   
REMARK 500    SER A 324       49.92     22.99                                   
REMARK 500    SER A 326       65.72   -104.57                                   
REMARK 500    GLU A 329     -126.72   -138.96                                   
REMARK 500    VAL A 340      108.91   -161.48                                   
REMARK 500    VAL A 351      -67.01   -107.60                                   
REMARK 500    PRO A 365       95.41    -60.62                                   
REMARK 500    TYR A 385       18.25     90.53                                   
REMARK 500    LEU A 386      106.65    -49.25                                   
REMARK 500    TRP A 395     -146.97    -94.62                                   
REMARK 500    PRO A 406      -34.08    -38.75                                   
REMARK 500    TYR A 408      107.24    -53.84                                   
REMARK 500    HIS A 410       -3.76     67.21                                   
REMARK 500    THR A 411      -74.10    -96.68                                   
REMARK 500    SER A 421     -118.14     50.13                                   
REMARK 500    THR A 433      -61.48   -130.80                                   
REMARK 500    ALA A 461       58.43   -164.72                                   
REMARK 500    GLN A 472      164.52    174.14                                   
REMARK 500    ALA A 504      -76.43    -59.82                                   
REMARK 500    THR A 507      146.90   -176.12                                   
REMARK 500    PRO A 547        5.62    -67.20                                   
REMARK 500    GLN A 551      134.78   -172.18                                   
REMARK 500    ARG A 588       89.22    -64.18                                   
REMARK 500    GLU A 622      -37.74     74.21                                   
REMARK 500    LYS A 641      -26.46     86.99                                   
REMARK 500    LYS A 644      -78.13     59.09                                   
REMARK 500    ARG A 650      -39.60     80.10                                   
REMARK 500    LEU A 652     -110.33    -67.20                                   
REMARK 500    SER A 654      118.16   -160.24                                   
REMARK 500    ASN A 678      152.49    142.40                                   
REMARK 500    LEU A 689      -73.08    -63.53                                   
REMARK 500    VAL A 708      -61.56   -108.80                                   
REMARK 500    ARG A 731      109.59    -53.04                                   
REMARK 500    CYS A 758       93.56     74.66                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     409 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 SER A   82     PRO A   83                  136.87                    
REMARK 500 ARG A  480     GLY A  481                 -146.95                    
REMARK 500 LEU A  724     LEU A  725                 -149.68                    
REMARK 500 ASN A  885     ASN A  886                  144.86                    
REMARK 500 GLU B  173     LYS B  174                  144.44                    
REMARK 500 ARG B  231     ASN B  232                  137.41                    
REMARK 500 SER C   82     PRO C   83                  134.69                    
REMARK 500 LEU C  600     TRP C  601                 -148.49                    
REMARK 500 TRP C  601     VAL C  602                 -147.86                    
REMARK 500 GLU C  622     GLN C  623                  144.20                    
REMARK 500 LYS C  690     ALA C  691                 -148.02                    
REMARK 500 GLU C  884     ASN C  885                 -148.42                    
REMARK 500 GLY D  102     TYR D  103                  143.24                    
REMARK 500 ASP D  433     ARG D  434                  137.64                    
REMARK 500 LEU D  436     CYS D  437                 -144.82                    
REMARK 500 CYS D  437     HIS D  438                 -145.65                    
REMARK 500 ASN D  620     CYS D  621                 -147.49                    
REMARK 500 SER E   82     PRO E   83                  139.46                    
REMARK 500 TYR E  465     GLU E  466                  148.07                    
REMARK 500 ASP E  640     LYS E  641                  138.89                    
REMARK 500 SER G   82     PRO G   83                  139.60                    
REMARK 500 ARG G  642     SER G  643                  144.59                    
REMARK 500 ASN G  729     LEU G  730                 -147.65                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              MG A2009  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 140   OG                                                     
REMARK 620 2 SER A 142   OG  101.2                                              
REMARK 620 3 ASP A 240   OD1 118.9  96.6                                        
REMARK 620 4 HOH A4008   O   156.8  96.2  73.8                                  
REMARK 620 5 HOH A4012   O    86.7 167.3  88.1  73.7                            
REMARK 620 6 HOH A4011   O    84.6 106.6 143.2  75.6  63.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 447   OD1                                                    
REMARK 620 2 ASP A 449   OD1  83.1                                              
REMARK 620 3 ASP A 451   OD1  80.9  79.8                                        
REMARK 620 4 ASP A 451   OD2 125.0  77.6  45.4                                  
REMARK 620 5 SER A 453   O    66.3 145.5  80.0 106.5                            
REMARK 620 6 ASP A 455   OD1 129.6 120.8 142.0 104.3  92.0                      
REMARK 620 7 ASP A 455   OD2  81.4  91.9 161.3 149.1  98.6  56.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 511   OD1                                                    
REMARK 620 2 ASN A 513   OD1  89.3                                              
REMARK 620 3 ASP A 515   OD1  84.3  63.0                                        
REMARK 620 4 LEU A 517   O    84.5 141.1  78.2                                  
REMARK 620 5 ASP A 519   OD2 120.8 120.0 153.7  95.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 574   OD1                                                    
REMARK 620 2 THR A 576   OG1 100.3                                              
REMARK 620 3 ASP A 578   OD1  98.2  86.1                                        
REMARK 620 4 LEU A 580   O    77.7 175.5  98.1                                  
REMARK 620 5 ASP A 582   OD1 137.3  85.4 124.5  93.4                            
REMARK 620 6 ASP A 582   OD2  89.8  87.0 170.3  89.0  47.9                      
REMARK 620 7 HOH A4020   O   151.2 100.9  64.0  82.4  64.0 110.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 116   O                                                      
REMARK 620 2 ASP B 120   OD2 120.7                                              
REMARK 620 3 GLU B 325   OE2  83.7 115.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 447   OD1                                                    
REMARK 620 2 ASP C 449   OD1  59.9                                              
REMARK 620 3 ASP C 449   OD2 104.5  47.1                                        
REMARK 620 4 ASP C 451   OD1  77.1  80.8 104.7                                  
REMARK 620 5 ASP C 451   OD2 119.2  80.2  67.5  51.2                            
REMARK 620 6 ASP C 455   OD1 115.2 134.4 103.6 144.8 125.4                      
REMARK 620 7 ASP C 455   OD2  69.9  91.5  93.8 145.2 160.4  51.1                
REMARK 620 8 HOH C4003   O   171.3 116.5  74.5  94.7  52.3  73.2 118.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 511   OD1                                                    
REMARK 620 2 ASN C 513   OD1  79.6                                              
REMARK 620 3 ASP C 515   OD1  94.1  69.7                                        
REMARK 620 4 LEU C 517   O    87.6 149.0  83.4                                  
REMARK 620 5 ASP C 519   OD2  97.9 103.8 165.1 105.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 574   OD1                                                    
REMARK 620 2 THR C 576   OG1  83.3                                              
REMARK 620 3 ASP C 578   OD1  95.1  88.0                                        
REMARK 620 4 LEU C 580   O    87.3 167.8 100.6                                  
REMARK 620 5 ASP C 582   OD1 127.7  78.0 132.0 101.9                            
REMARK 620 6 ASP C 582   OD2  79.3  71.9 159.6  98.8  48.5                      
REMARK 620 7 HOH C4007   O   167.3 102.2  73.9  88.6  64.9 113.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D 116   O                                                      
REMARK 620 2 GLU D 325   OE2 105.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 447   OD1                                                    
REMARK 620 2 ASP E 451   OD1  66.5                                              
REMARK 620 3 ASP E 451   OD2 116.4  51.3                                        
REMARK 620 4 SER E 453   O    61.2  76.2 109.4                                  
REMARK 620 5 ASP E 455   OD1 123.4 169.4 119.8 104.3                            
REMARK 620 6 ASP E 455   OD2  73.2 138.9 159.1  91.5  51.6                      
REMARK 620 7 HOH E4001   O   167.8 102.3  51.6 122.3  68.3 117.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 511   OD1                                                    
REMARK 620 2 ASN E 513   OD1  73.6                                              
REMARK 620 3 ASP E 515   OD1  82.4  68.0                                        
REMARK 620 4 LEU E 517   O    87.1 146.8  83.1                                  
REMARK 620 5 ASP E 519   OD1 153.6 121.5 122.4  87.4                            
REMARK 620 6 ASP E 519   OD2 111.1 116.8 166.3  95.2  43.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 574   OD1                                                    
REMARK 620 2 THR E 576   OG1  95.6                                              
REMARK 620 3 ASP E 578   OD1  90.2  89.6                                        
REMARK 620 4 LEU E 580   O    86.0 174.3  84.9                                  
REMARK 620 5 ASP E 582   OD1 145.8  82.7 123.8  99.1                            
REMARK 620 6 ASP E 582   OD2  92.0  81.6 171.0 103.9  53.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER F 116   O                                                      
REMARK 620 2 ASP F 120   OD2  90.7                                              
REMARK 620 3 GLU F 325   OE1 108.0 131.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 447   OD1                                                    
REMARK 620 2 ASP G 449   OD1  70.8                                              
REMARK 620 3 ASP G 451   OD1  84.0  71.7                                        
REMARK 620 4 SER G 453   O    78.8 140.1  80.2                                  
REMARK 620 5 ASP G 455   OD1 128.5 125.3 145.5  93.7                            
REMARK 620 6 ASP G 455   OD2  79.2  93.7 160.7 105.3  53.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 511   OD1                                                    
REMARK 620 2 ASN G 513   OD1  79.2                                              
REMARK 620 3 ASP G 515   OD1  98.2  80.4                                        
REMARK 620 4 LEU G 517   O    91.5 157.8  81.0                                  
REMARK 620 5 ASP G 519   OD1 138.1 117.6 121.5  82.8                            
REMARK 620 6 ASP G 519   OD2  95.3 108.7 165.0  92.1  43.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G 576   OG1                                                    
REMARK 620 2 ASP G 578   OD1  86.1                                              
REMARK 620 3 LEU G 580   O   120.2  95.1                                        
REMARK 620 4 ASP G 582   OD1  72.4 157.3 101.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER H 116   O                                                      
REMARK 620 2 ASP H 120   OD2 101.6                                              
REMARK 620 3 GLU H 325   O   170.5  69.9                                        
REMARK 620 4 GLU H 325   OE2 103.7 154.4  84.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 2009                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 3042        
REMARK 800  bound to ASN A 42                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  3070 through MAN A 3074 bound to ASN A 70                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  3373 through MAN A 3382 bound to ASN A 373                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 3678        
REMARK 800  bound to ASN A 678                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  3716 through MAN A 3719 bound to ASN A 716                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  3880 through BMA A 3882 bound to ASN A 880                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 3920        
REMARK 800  bound to ASN A 920                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 3031        
REMARK 800  bound to ASN A 1031                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  3094 through NAG B 3095 bound to ASN B 94                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 3232        
REMARK 800  bound to ASN B 232                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 3620        
REMARK 800  bound to ASN B 620                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 3042        
REMARK 800  bound to ASN C 42                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  3070 through MAN C 3073 bound to ASN C 70                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  3373 through MAN C 3380 bound to ASN C 373                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 3678        
REMARK 800  bound to ASN C 678                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  3716 through MAN C 3720 bound to ASN C 716                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  3880 through MAN C 3884 bound to ASN C 880                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 3920        
REMARK 800  bound to ASN C 920                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 3031        
REMARK 800  bound to ASN C 1031                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 3232        
REMARK 800  bound to ASN D 232                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 3620        
REMARK 800  bound to ASN D 620                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG E 3042        
REMARK 800  bound to ASN E 42                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG E    
REMARK 800  3070 through MAN E 3075 bound to ASN E 70                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG E    
REMARK 800  3373 through MAN E 3380 bound to ASN E 373                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG E 3678        
REMARK 800  bound to ASN E 678                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG E    
REMARK 800  3716 through MAN E 3719 bound to ASN E 716                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG E    
REMARK 800  3880 through MAN E 3884 bound to ASN E 880                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG E 3920        
REMARK 800  bound to ASN E 920                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG E 3031        
REMARK 800  bound to ASN E 1031                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG F 3094        
REMARK 800  bound to ASN F 94                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG F 3190        
REMARK 800  bound to ASN F 190                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG F 3620        
REMARK 800  bound to ASN F 620                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 3042        
REMARK 800  bound to ASN G 42                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G    
REMARK 800  3070 through MAN G 3074 bound to ASN G 70                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G    
REMARK 800  3373 through MAN G 3380 bound to ASN G 373                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 3678        
REMARK 800  bound to ASN G 678                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G    
REMARK 800  3716 through MAN G 3719 bound to ASN G 716                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G    
REMARK 800  3880 through MAN G 3884 bound to ASN G 880                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 3920        
REMARK 800  bound to ASN G 920                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 3031        
REMARK 800  bound to ASN G 1031                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG H 3094        
REMARK 800  bound to ASN H 94                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG H 3190        
REMARK 800  bound to ASN H 190                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG H 3232        
REMARK 800  bound to ASN H 232                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG H 3620        
REMARK 800  bound to ASN H 620                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3K6S   RELATED DB: PDB                                   
REMARK 900 RE-REFINEMENT OF INTEGRIN ALPHAXBETA2 ECTODOMAIN IN THE CLOSED/BENT  
REMARK 900 CONFORMATION                                                         
DBREF  5ES4 A    1  1084  UNP    P20702   ITAX_HUMAN      20   1103             
DBREF  5ES4 B    1   674  UNP    P05107   ITB2_HUMAN      23    696             
DBREF  5ES4 C    1  1084  UNP    P20702   ITAX_HUMAN      20   1103             
DBREF  5ES4 D    1   674  UNP    P05107   ITB2_HUMAN      23    696             
DBREF  5ES4 E    1  1084  UNP    P20702   ITAX_HUMAN      20   1103             
DBREF  5ES4 F    1   674  UNP    P05107   ITB2_HUMAN      23    696             
DBREF  5ES4 G    1  1084  UNP    P20702   ITAX_HUMAN      20   1103             
DBREF  5ES4 H    1   674  UNP    P05107   ITB2_HUMAN      23    696             
SEQADV 5ES4 GLY A 1085  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 CYS A 1086  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY A 1087  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY A 1088  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU A 1089  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1090  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN A 1091  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU A 1092  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TYR A 1093  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PHE A 1094  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN A 1095  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY A 1096  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY A 1097  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1098  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN A 1099  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA A 1100  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN A 1101  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 CYS A 1102  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1103  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS A 1104  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1105  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU A 1106  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN A 1107  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA A 1108  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU A 1109  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1110  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS A 1111  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1112  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN A 1113  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA A 1114  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN A 1115  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU A 1116  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1117  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TRP A 1118  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1119  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU A 1120  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN A 1121  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA A 1122  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU A 1123  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1124  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS A 1125  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1126  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU A 1127  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA A 1128  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN A 1129  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TRP A 1130  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 SER A 1131  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 HIS A 1132  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PRO A 1133  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN A 1134  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PHE A 1135  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU A 1136  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS A 1137  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASP B  675  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY B  676  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 CYS B  677  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY B  678  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU B  679  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLU B  680  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN B  681  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU B  682  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 TYR B  683  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 PHE B  684  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN B  685  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY B  686  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY B  687  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  688  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN B  689  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA B  690  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN B  691  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 CYS B  692  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  693  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  694  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  695  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU B  696  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN B  697  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA B  698  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU B  699  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  700  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  701  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  702  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN B  703  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA B  704  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN B  705  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU B  706  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  707  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 TRP B  708  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  709  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU B  710  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN B  711  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA B  712  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU B  713  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  714  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  715  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS B  716  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU B  717  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA B  718  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN B  719  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY B  720  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY B  721  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS B  722  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS B  723  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS B  724  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS B  725  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS B  726  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS B  727  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY C 1085  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 CYS C 1086  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY C 1087  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY C 1088  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU C 1089  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1090  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN C 1091  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU C 1092  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TYR C 1093  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PHE C 1094  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN C 1095  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY C 1096  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY C 1097  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1098  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN C 1099  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA C 1100  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN C 1101  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 CYS C 1102  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1103  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS C 1104  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1105  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU C 1106  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN C 1107  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA C 1108  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU C 1109  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1110  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS C 1111  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1112  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN C 1113  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA C 1114  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN C 1115  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU C 1116  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1117  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TRP C 1118  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1119  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU C 1120  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN C 1121  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA C 1122  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU C 1123  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1124  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS C 1125  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1126  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU C 1127  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA C 1128  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN C 1129  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TRP C 1130  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 SER C 1131  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 HIS C 1132  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PRO C 1133  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN C 1134  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PHE C 1135  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU C 1136  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS C 1137  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASP D  675  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY D  676  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 CYS D  677  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY D  678  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU D  679  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLU D  680  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN D  681  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU D  682  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 TYR D  683  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 PHE D  684  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN D  685  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY D  686  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY D  687  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  688  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN D  689  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA D  690  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN D  691  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 CYS D  692  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  693  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  694  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  695  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU D  696  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN D  697  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA D  698  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU D  699  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  700  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  701  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  702  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN D  703  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA D  704  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN D  705  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU D  706  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  707  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 TRP D  708  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  709  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU D  710  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN D  711  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA D  712  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU D  713  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  714  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  715  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS D  716  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU D  717  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA D  718  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN D  719  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY D  720  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY D  721  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS D  722  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS D  723  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS D  724  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS D  725  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS D  726  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS D  727  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY E 1085  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 CYS E 1086  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY E 1087  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY E 1088  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU E 1089  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1090  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN E 1091  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU E 1092  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TYR E 1093  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PHE E 1094  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN E 1095  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY E 1096  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY E 1097  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1098  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN E 1099  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA E 1100  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN E 1101  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 CYS E 1102  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1103  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS E 1104  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1105  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU E 1106  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN E 1107  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA E 1108  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU E 1109  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1110  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS E 1111  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1112  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN E 1113  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA E 1114  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN E 1115  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU E 1116  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1117  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TRP E 1118  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1119  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU E 1120  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN E 1121  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA E 1122  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU E 1123  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1124  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS E 1125  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1126  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU E 1127  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA E 1128  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN E 1129  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TRP E 1130  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 SER E 1131  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 HIS E 1132  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PRO E 1133  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN E 1134  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PHE E 1135  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU E 1136  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS E 1137  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASP F  675  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY F  676  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 CYS F  677  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY F  678  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU F  679  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLU F  680  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN F  681  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU F  682  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 TYR F  683  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 PHE F  684  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN F  685  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY F  686  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY F  687  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  688  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN F  689  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA F  690  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN F  691  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 CYS F  692  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  693  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  694  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  695  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU F  696  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN F  697  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA F  698  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU F  699  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  700  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  701  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  702  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN F  703  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA F  704  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN F  705  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU F  706  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  707  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 TRP F  708  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  709  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU F  710  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN F  711  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA F  712  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU F  713  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  714  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  715  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS F  716  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU F  717  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA F  718  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN F  719  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY F  720  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY F  721  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS F  722  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS F  723  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS F  724  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS F  725  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS F  726  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS F  727  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY G 1085  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 CYS G 1086  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY G 1087  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY G 1088  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU G 1089  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1090  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN G 1091  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU G 1092  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TYR G 1093  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PHE G 1094  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN G 1095  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY G 1096  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLY G 1097  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1098  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN G 1099  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA G 1100  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN G 1101  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 CYS G 1102  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1103  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS G 1104  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1105  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU G 1106  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN G 1107  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA G 1108  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU G 1109  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1110  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS G 1111  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1112  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASN G 1113  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA G 1114  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN G 1115  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU G 1116  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1117  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TRP G 1118  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1119  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU G 1120  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN G 1121  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA G 1122  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU G 1123  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1124  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS G 1125  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1126  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LEU G 1127  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ALA G 1128  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN G 1129  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 TRP G 1130  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 SER G 1131  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 HIS G 1132  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PRO G 1133  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLN G 1134  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 PHE G 1135  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 GLU G 1136  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 LYS G 1137  UNP  P20702              EXPRESSION TAG                 
SEQADV 5ES4 ASP H  675  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY H  676  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 CYS H  677  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY H  678  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU H  679  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLU H  680  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN H  681  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU H  682  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 TYR H  683  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 PHE H  684  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN H  685  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY H  686  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY H  687  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  688  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN H  689  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA H  690  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN H  691  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 CYS H  692  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  693  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  694  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  695  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU H  696  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN H  697  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA H  698  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU H  699  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  700  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  701  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  702  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ASN H  703  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA H  704  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN H  705  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU H  706  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  707  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 TRP H  708  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  709  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU H  710  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN H  711  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA H  712  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU H  713  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  714  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  715  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LYS H  716  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 LEU H  717  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 ALA H  718  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLN H  719  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY H  720  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 GLY H  721  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS H  722  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS H  723  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS H  724  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS H  725  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS H  726  UNP  P05107              EXPRESSION TAG                 
SEQADV 5ES4 HIS H  727  UNP  P05107              EXPRESSION TAG                 
SEQRES   1 A 1137  PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL          
SEQRES   2 A 1137  ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA          
SEQRES   3 A 1137  ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR          
SEQRES   4 A 1137  ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR          
SEQRES   5 A 1137  SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO          
SEQRES   6 A 1137  PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA          
SEQRES   7 A 1137  SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO          
SEQRES   8 A 1137  THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR          
SEQRES   9 A 1137  GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN          
SEQRES  10 A 1137  ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU          
SEQRES  11 A 1137  GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE          
SEQRES  12 A 1137  SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG          
SEQRES  13 A 1137  ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE          
SEQRES  14 A 1137  SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE          
SEQRES  15 A 1137  THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER          
SEQRES  16 A 1137  LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR          
SEQRES  17 A 1137  THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE          
SEQRES  18 A 1137  HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE          
SEQRES  19 A 1137  LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER          
SEQRES  20 A 1137  LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA          
SEQRES  21 A 1137  GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE          
SEQRES  22 A 1137  GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA          
SEQRES  23 A 1137  SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP          
SEQRES  24 A 1137  PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU          
SEQRES  25 A 1137  LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER          
SEQRES  26 A 1137  SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER          
SEQRES  27 A 1137  ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL          
SEQRES  28 A 1137  GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO          
SEQRES  29 A 1137  PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU          
SEQRES  30 A 1137  ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR          
SEQRES  31 A 1137  GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU          
SEQRES  32 A 1137  GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE          
SEQRES  33 A 1137  PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU          
SEQRES  34 A 1137  VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER          
SEQRES  35 A 1137  LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP          
SEQRES  36 A 1137  LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR          
SEQRES  37 A 1137  ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY          
SEQRES  38 A 1137  TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU          
SEQRES  39 A 1137  GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR          
SEQRES  40 A 1137  VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL          
SEQRES  41 A 1137  VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA          
SEQRES  42 A 1137  VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER          
SEQRES  43 A 1137  PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER          
SEQRES  44 A 1137  SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY          
SEQRES  45 A 1137  GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL          
SEQRES  46 A 1137  GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO          
SEQRES  47 A 1137  VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA          
SEQRES  48 A 1137  GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL          
SEQRES  49 A 1137  VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU          
SEQRES  50 A 1137  TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG          
SEQRES  51 A 1137  ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP          
SEQRES  52 A 1137  PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR          
SEQRES  53 A 1137  LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU          
SEQRES  54 A 1137  LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER          
SEQRES  55 A 1137  CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU          
SEQRES  56 A 1137  ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG          
SEQRES  57 A 1137  ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR          
SEQRES  58 A 1137  PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA          
SEQRES  59 A 1137  ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER          
SEQRES  60 A 1137  PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU          
SEQRES  61 A 1137  GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU          
SEQRES  62 A 1137  ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA          
SEQRES  63 A 1137  GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN          
SEQRES  64 A 1137  GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA          
SEQRES  65 A 1137  PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG          
SEQRES  66 A 1137  ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR          
SEQRES  67 A 1137  PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU          
SEQRES  68 A 1137  GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU          
SEQRES  69 A 1137  ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU          
SEQRES  70 A 1137  GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER          
SEQRES  71 A 1137  SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU          
SEQRES  72 A 1137  SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR          
SEQRES  73 A 1137  GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER          
SEQRES  74 A 1137  ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA          
SEQRES  75 A 1137  VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO          
SEQRES  76 A 1137  SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA          
SEQRES  77 A 1137  SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU          
SEQRES  78 A 1137  ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP          
SEQRES  79 A 1137  VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR          
SEQRES  80 A 1137  LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE          
SEQRES  81 A 1137  LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE          
SEQRES  82 A 1137  THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN          
SEQRES  83 A 1137  GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU          
SEQRES  84 A 1137  LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU          
SEQRES  85 A 1137  TYR PHE GLN GLY GLY GLU ASN ALA GLN CYS GLU LYS GLU          
SEQRES  86 A 1137  LEU GLN ALA LEU GLU LYS GLU ASN ALA GLN LEU GLU TRP          
SEQRES  87 A 1137  GLU LEU GLN ALA LEU GLU LYS GLU LEU ALA GLN TRP SER          
SEQRES  88 A 1137  HIS PRO GLN PHE GLU LYS                                      
SEQRES   1 B  727  GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU          
SEQRES   2 B  727  CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS          
SEQRES   3 B  727  LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG          
SEQRES   4 B  727  CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA          
SEQRES   5 B  727  ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR          
SEQRES   6 B  727  GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO          
SEQRES   7 B  727  GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA          
SEQRES   8 B  727  ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO          
SEQRES   9 B  727  ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET          
SEQRES  10 B  727  LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP          
SEQRES  11 B  727  LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG          
SEQRES  12 B  727  ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO          
SEQRES  13 B  727  PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS          
SEQRES  14 B  727  PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE          
SEQRES  15 B  727  ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE          
SEQRES  16 B  727  GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU          
SEQRES  17 B  727  ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL          
SEQRES  18 B  727  ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR          
SEQRES  19 B  727  ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE          
SEQRES  20 B  727  ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN          
SEQRES  21 B  727  ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG          
SEQRES  22 B  727  SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA          
SEQRES  23 B  727  HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA          
SEQRES  24 B  727  VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR          
SEQRES  25 B  727  GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU          
SEQRES  26 B  727  ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR          
SEQRES  27 B  727  ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA          
SEQRES  28 B  727  LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS          
SEQRES  29 B  727  SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP          
SEQRES  30 B  727  CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN          
SEQRES  31 B  727  VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER          
SEQRES  32 B  727  PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR          
SEQRES  33 B  727  VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP          
SEQRES  34 B  727  GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE          
SEQRES  35 B  727  LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE          
SEQRES  36 B  727  GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER          
SEQRES  37 B  727  GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER          
SEQRES  38 B  727  ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN          
SEQRES  39 B  727  CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE          
SEQRES  40 B  727  TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU          
SEQRES  41 B  727  ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY          
SEQRES  42 B  727  LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE          
SEQRES  43 B  727  GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY          
SEQRES  44 B  727  CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY          
SEQRES  45 B  727  ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR          
SEQRES  46 B  727  GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER          
SEQRES  47 B  727  PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS          
SEQRES  48 B  727  PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA          
SEQRES  49 B  727  CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY          
SEQRES  50 B  727  ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL          
SEQRES  51 B  727  ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR          
SEQRES  52 B  727  LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ASP GLY          
SEQRES  53 B  727  CYS GLY LEU GLU ASN LEU TYR PHE GLN GLY GLY LYS ASN          
SEQRES  54 B  727  ALA GLN CYS LYS LYS LYS LEU GLN ALA LEU LYS LYS LYS          
SEQRES  55 B  727  ASN ALA GLN LEU LYS TRP LYS LEU GLN ALA LEU LYS LYS          
SEQRES  56 B  727  LYS LEU ALA GLN GLY GLY HIS HIS HIS HIS HIS HIS              
SEQRES   1 C 1137  PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL          
SEQRES   2 C 1137  ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA          
SEQRES   3 C 1137  ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR          
SEQRES   4 C 1137  ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR          
SEQRES   5 C 1137  SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO          
SEQRES   6 C 1137  PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA          
SEQRES   7 C 1137  SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO          
SEQRES   8 C 1137  THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR          
SEQRES   9 C 1137  GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN          
SEQRES  10 C 1137  ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU          
SEQRES  11 C 1137  GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE          
SEQRES  12 C 1137  SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG          
SEQRES  13 C 1137  ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE          
SEQRES  14 C 1137  SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE          
SEQRES  15 C 1137  THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER          
SEQRES  16 C 1137  LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR          
SEQRES  17 C 1137  THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE          
SEQRES  18 C 1137  HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE          
SEQRES  19 C 1137  LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER          
SEQRES  20 C 1137  LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA          
SEQRES  21 C 1137  GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE          
SEQRES  22 C 1137  GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA          
SEQRES  23 C 1137  SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP          
SEQRES  24 C 1137  PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU          
SEQRES  25 C 1137  LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER          
SEQRES  26 C 1137  SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER          
SEQRES  27 C 1137  ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL          
SEQRES  28 C 1137  GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO          
SEQRES  29 C 1137  PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU          
SEQRES  30 C 1137  ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR          
SEQRES  31 C 1137  GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU          
SEQRES  32 C 1137  GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE          
SEQRES  33 C 1137  PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU          
SEQRES  34 C 1137  VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER          
SEQRES  35 C 1137  LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP          
SEQRES  36 C 1137  LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR          
SEQRES  37 C 1137  ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY          
SEQRES  38 C 1137  TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU          
SEQRES  39 C 1137  GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR          
SEQRES  40 C 1137  VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL          
SEQRES  41 C 1137  VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA          
SEQRES  42 C 1137  VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER          
SEQRES  43 C 1137  PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER          
SEQRES  44 C 1137  SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY          
SEQRES  45 C 1137  GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL          
SEQRES  46 C 1137  GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO          
SEQRES  47 C 1137  VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA          
SEQRES  48 C 1137  GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL          
SEQRES  49 C 1137  VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU          
SEQRES  50 C 1137  TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG          
SEQRES  51 C 1137  ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP          
SEQRES  52 C 1137  PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR          
SEQRES  53 C 1137  LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU          
SEQRES  54 C 1137  LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER          
SEQRES  55 C 1137  CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU          
SEQRES  56 C 1137  ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG          
SEQRES  57 C 1137  ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR          
SEQRES  58 C 1137  PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA          
SEQRES  59 C 1137  ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER          
SEQRES  60 C 1137  PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU          
SEQRES  61 C 1137  GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU          
SEQRES  62 C 1137  ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA          
SEQRES  63 C 1137  GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN          
SEQRES  64 C 1137  GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA          
SEQRES  65 C 1137  PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG          
SEQRES  66 C 1137  ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR          
SEQRES  67 C 1137  PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU          
SEQRES  68 C 1137  GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU          
SEQRES  69 C 1137  ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU          
SEQRES  70 C 1137  GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER          
SEQRES  71 C 1137  SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU          
SEQRES  72 C 1137  SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR          
SEQRES  73 C 1137  GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER          
SEQRES  74 C 1137  ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA          
SEQRES  75 C 1137  VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO          
SEQRES  76 C 1137  SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA          
SEQRES  77 C 1137  SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU          
SEQRES  78 C 1137  ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP          
SEQRES  79 C 1137  VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR          
SEQRES  80 C 1137  LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE          
SEQRES  81 C 1137  LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE          
SEQRES  82 C 1137  THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN          
SEQRES  83 C 1137  GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU          
SEQRES  84 C 1137  LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU          
SEQRES  85 C 1137  TYR PHE GLN GLY GLY GLU ASN ALA GLN CYS GLU LYS GLU          
SEQRES  86 C 1137  LEU GLN ALA LEU GLU LYS GLU ASN ALA GLN LEU GLU TRP          
SEQRES  87 C 1137  GLU LEU GLN ALA LEU GLU LYS GLU LEU ALA GLN TRP SER          
SEQRES  88 C 1137  HIS PRO GLN PHE GLU LYS                                      
SEQRES   1 D  727  GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU          
SEQRES   2 D  727  CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS          
SEQRES   3 D  727  LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG          
SEQRES   4 D  727  CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA          
SEQRES   5 D  727  ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR          
SEQRES   6 D  727  GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO          
SEQRES   7 D  727  GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA          
SEQRES   8 D  727  ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO          
SEQRES   9 D  727  ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET          
SEQRES  10 D  727  LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP          
SEQRES  11 D  727  LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG          
SEQRES  12 D  727  ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO          
SEQRES  13 D  727  PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS          
SEQRES  14 D  727  PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE          
SEQRES  15 D  727  ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE          
SEQRES  16 D  727  GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU          
SEQRES  17 D  727  ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL          
SEQRES  18 D  727  ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR          
SEQRES  19 D  727  ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE          
SEQRES  20 D  727  ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN          
SEQRES  21 D  727  ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG          
SEQRES  22 D  727  SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA          
SEQRES  23 D  727  HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA          
SEQRES  24 D  727  VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR          
SEQRES  25 D  727  GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU          
SEQRES  26 D  727  ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR          
SEQRES  27 D  727  ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA          
SEQRES  28 D  727  LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS          
SEQRES  29 D  727  SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP          
SEQRES  30 D  727  CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN          
SEQRES  31 D  727  VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER          
SEQRES  32 D  727  PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR          
SEQRES  33 D  727  VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP          
SEQRES  34 D  727  GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE          
SEQRES  35 D  727  LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE          
SEQRES  36 D  727  GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER          
SEQRES  37 D  727  GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER          
SEQRES  38 D  727  ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN          
SEQRES  39 D  727  CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE          
SEQRES  40 D  727  TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU          
SEQRES  41 D  727  ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY          
SEQRES  42 D  727  LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE          
SEQRES  43 D  727  GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY          
SEQRES  44 D  727  CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY          
SEQRES  45 D  727  ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR          
SEQRES  46 D  727  GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER          
SEQRES  47 D  727  PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS          
SEQRES  48 D  727  PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA          
SEQRES  49 D  727  CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY          
SEQRES  50 D  727  ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL          
SEQRES  51 D  727  ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR          
SEQRES  52 D  727  LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ASP GLY          
SEQRES  53 D  727  CYS GLY LEU GLU ASN LEU TYR PHE GLN GLY GLY LYS ASN          
SEQRES  54 D  727  ALA GLN CYS LYS LYS LYS LEU GLN ALA LEU LYS LYS LYS          
SEQRES  55 D  727  ASN ALA GLN LEU LYS TRP LYS LEU GLN ALA LEU LYS LYS          
SEQRES  56 D  727  LYS LEU ALA GLN GLY GLY HIS HIS HIS HIS HIS HIS              
SEQRES   1 E 1137  PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL          
SEQRES   2 E 1137  ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA          
SEQRES   3 E 1137  ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR          
SEQRES   4 E 1137  ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR          
SEQRES   5 E 1137  SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO          
SEQRES   6 E 1137  PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA          
SEQRES   7 E 1137  SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO          
SEQRES   8 E 1137  THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR          
SEQRES   9 E 1137  GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN          
SEQRES  10 E 1137  ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU          
SEQRES  11 E 1137  GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE          
SEQRES  12 E 1137  SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG          
SEQRES  13 E 1137  ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE          
SEQRES  14 E 1137  SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE          
SEQRES  15 E 1137  THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER          
SEQRES  16 E 1137  LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR          
SEQRES  17 E 1137  THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE          
SEQRES  18 E 1137  HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE          
SEQRES  19 E 1137  LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER          
SEQRES  20 E 1137  LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA          
SEQRES  21 E 1137  GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE          
SEQRES  22 E 1137  GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA          
SEQRES  23 E 1137  SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP          
SEQRES  24 E 1137  PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU          
SEQRES  25 E 1137  LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER          
SEQRES  26 E 1137  SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER          
SEQRES  27 E 1137  ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL          
SEQRES  28 E 1137  GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO          
SEQRES  29 E 1137  PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU          
SEQRES  30 E 1137  ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR          
SEQRES  31 E 1137  GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU          
SEQRES  32 E 1137  GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE          
SEQRES  33 E 1137  PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU          
SEQRES  34 E 1137  VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER          
SEQRES  35 E 1137  LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP          
SEQRES  36 E 1137  LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR          
SEQRES  37 E 1137  ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY          
SEQRES  38 E 1137  TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU          
SEQRES  39 E 1137  GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR          
SEQRES  40 E 1137  VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL          
SEQRES  41 E 1137  VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA          
SEQRES  42 E 1137  VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER          
SEQRES  43 E 1137  PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER          
SEQRES  44 E 1137  SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY          
SEQRES  45 E 1137  GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL          
SEQRES  46 E 1137  GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO          
SEQRES  47 E 1137  VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA          
SEQRES  48 E 1137  GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL          
SEQRES  49 E 1137  VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU          
SEQRES  50 E 1137  TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG          
SEQRES  51 E 1137  ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP          
SEQRES  52 E 1137  PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR          
SEQRES  53 E 1137  LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU          
SEQRES  54 E 1137  LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER          
SEQRES  55 E 1137  CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU          
SEQRES  56 E 1137  ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG          
SEQRES  57 E 1137  ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR          
SEQRES  58 E 1137  PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA          
SEQRES  59 E 1137  ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER          
SEQRES  60 E 1137  PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU          
SEQRES  61 E 1137  GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU          
SEQRES  62 E 1137  ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA          
SEQRES  63 E 1137  GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN          
SEQRES  64 E 1137  GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA          
SEQRES  65 E 1137  PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG          
SEQRES  66 E 1137  ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR          
SEQRES  67 E 1137  PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU          
SEQRES  68 E 1137  GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU          
SEQRES  69 E 1137  ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU          
SEQRES  70 E 1137  GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER          
SEQRES  71 E 1137  SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU          
SEQRES  72 E 1137  SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR          
SEQRES  73 E 1137  GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER          
SEQRES  74 E 1137  ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA          
SEQRES  75 E 1137  VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO          
SEQRES  76 E 1137  SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA          
SEQRES  77 E 1137  SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU          
SEQRES  78 E 1137  ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP          
SEQRES  79 E 1137  VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR          
SEQRES  80 E 1137  LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE          
SEQRES  81 E 1137  LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE          
SEQRES  82 E 1137  THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN          
SEQRES  83 E 1137  GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU          
SEQRES  84 E 1137  LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU          
SEQRES  85 E 1137  TYR PHE GLN GLY GLY GLU ASN ALA GLN CYS GLU LYS GLU          
SEQRES  86 E 1137  LEU GLN ALA LEU GLU LYS GLU ASN ALA GLN LEU GLU TRP          
SEQRES  87 E 1137  GLU LEU GLN ALA LEU GLU LYS GLU LEU ALA GLN TRP SER          
SEQRES  88 E 1137  HIS PRO GLN PHE GLU LYS                                      
SEQRES   1 F  727  GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU          
SEQRES   2 F  727  CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS          
SEQRES   3 F  727  LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG          
SEQRES   4 F  727  CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA          
SEQRES   5 F  727  ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR          
SEQRES   6 F  727  GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO          
SEQRES   7 F  727  GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA          
SEQRES   8 F  727  ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO          
SEQRES   9 F  727  ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET          
SEQRES  10 F  727  LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP          
SEQRES  11 F  727  LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG          
SEQRES  12 F  727  ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO          
SEQRES  13 F  727  PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS          
SEQRES  14 F  727  PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE          
SEQRES  15 F  727  ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE          
SEQRES  16 F  727  GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU          
SEQRES  17 F  727  ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL          
SEQRES  18 F  727  ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR          
SEQRES  19 F  727  ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE          
SEQRES  20 F  727  ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN          
SEQRES  21 F  727  ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG          
SEQRES  22 F  727  SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA          
SEQRES  23 F  727  HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA          
SEQRES  24 F  727  VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR          
SEQRES  25 F  727  GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU          
SEQRES  26 F  727  ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR          
SEQRES  27 F  727  ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA          
SEQRES  28 F  727  LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS          
SEQRES  29 F  727  SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP          
SEQRES  30 F  727  CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN          
SEQRES  31 F  727  VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER          
SEQRES  32 F  727  PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR          
SEQRES  33 F  727  VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP          
SEQRES  34 F  727  GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE          
SEQRES  35 F  727  LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE          
SEQRES  36 F  727  GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER          
SEQRES  37 F  727  GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER          
SEQRES  38 F  727  ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN          
SEQRES  39 F  727  CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE          
SEQRES  40 F  727  TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU          
SEQRES  41 F  727  ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY          
SEQRES  42 F  727  LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE          
SEQRES  43 F  727  GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY          
SEQRES  44 F  727  CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY          
SEQRES  45 F  727  ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR          
SEQRES  46 F  727  GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER          
SEQRES  47 F  727  PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS          
SEQRES  48 F  727  PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA          
SEQRES  49 F  727  CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY          
SEQRES  50 F  727  ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL          
SEQRES  51 F  727  ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR          
SEQRES  52 F  727  LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ASP GLY          
SEQRES  53 F  727  CYS GLY LEU GLU ASN LEU TYR PHE GLN GLY GLY LYS ASN          
SEQRES  54 F  727  ALA GLN CYS LYS LYS LYS LEU GLN ALA LEU LYS LYS LYS          
SEQRES  55 F  727  ASN ALA GLN LEU LYS TRP LYS LEU GLN ALA LEU LYS LYS          
SEQRES  56 F  727  LYS LEU ALA GLN GLY GLY HIS HIS HIS HIS HIS HIS              
SEQRES   1 G 1137  PHE ASN LEU ASP THR GLU GLU LEU THR ALA PHE ARG VAL          
SEQRES   2 G 1137  ASP SER ALA GLY PHE GLY ASP SER VAL VAL GLN TYR ALA          
SEQRES   3 G 1137  ASN SER TRP VAL VAL VAL GLY ALA PRO GLN LYS ILE THR          
SEQRES   4 G 1137  ALA ALA ASN GLN THR GLY GLY LEU TYR GLN CYS GLY TYR          
SEQRES   5 G 1137  SER THR GLY ALA CYS GLU PRO ILE GLY LEU GLN VAL PRO          
SEQRES   6 G 1137  PRO GLU ALA VAL ASN MET SER LEU GLY LEU SER LEU ALA          
SEQRES   7 G 1137  SER THR THR SER PRO SER GLN LEU LEU ALA CYS GLY PRO          
SEQRES   8 G 1137  THR VAL HIS HIS GLU CYS GLY ARG ASN MET TYR LEU THR          
SEQRES   9 G 1137  GLY LEU CYS PHE LEU LEU GLY PRO THR GLN LEU THR GLN          
SEQRES  10 G 1137  ARG LEU PRO VAL SER ARG GLN GLU CYS PRO ARG GLN GLU          
SEQRES  11 G 1137  GLN ASP ILE VAL PHE LEU ILE ASP GLY SER GLY SER ILE          
SEQRES  12 G 1137  SER SER ARG ASN PHE ALA THR MET MET ASN PHE VAL ARG          
SEQRES  13 G 1137  ALA VAL ILE SER GLN PHE GLN ARG PRO SER THR GLN PHE          
SEQRES  14 G 1137  SER LEU MET GLN PHE SER ASN LYS PHE GLN THR HIS PHE          
SEQRES  15 G 1137  THR PHE GLU GLU PHE ARG ARG SER SER ASN PRO LEU SER          
SEQRES  16 G 1137  LEU LEU ALA SER VAL HIS GLN LEU GLN GLY PHE THR TYR          
SEQRES  17 G 1137  THR ALA THR ALA ILE GLN ASN VAL VAL HIS ARG LEU PHE          
SEQRES  18 G 1137  HIS ALA SER TYR GLY ALA ARG ARG ASP ALA ALA LYS ILE          
SEQRES  19 G 1137  LEU ILE VAL ILE THR ASP GLY LYS LYS GLU GLY ASP SER          
SEQRES  20 G 1137  LEU ASP TYR LYS ASP VAL ILE PRO MET ALA ASP ALA ALA          
SEQRES  21 G 1137  GLY ILE ILE ARG TYR ALA ILE GLY VAL GLY LEU ALA PHE          
SEQRES  22 G 1137  GLN ASN ARG ASN SER TRP LYS GLU LEU ASN ASP ILE ALA          
SEQRES  23 G 1137  SER LYS PRO SER GLN GLU HIS ILE PHE LYS VAL GLU ASP          
SEQRES  24 G 1137  PHE ASP ALA LEU LYS ASP ILE GLN ASN GLN LEU LYS GLU          
SEQRES  25 G 1137  LYS ILE PHE ALA ILE GLU GLY THR GLU THR THR SER SER          
SEQRES  26 G 1137  SER SER PHE GLU LEU GLU MET ALA GLN GLU GLY PHE SER          
SEQRES  27 G 1137  ALA VAL PHE THR PRO ASP GLY PRO VAL LEU GLY ALA VAL          
SEQRES  28 G 1137  GLY SER PHE THR TRP SER GLY GLY ALA PHE LEU TYR PRO          
SEQRES  29 G 1137  PRO ASN MET SER PRO THR PHE ILE ASN MET SER GLN GLU          
SEQRES  30 G 1137  ASN VAL ASP MET ARG ASP SER TYR LEU GLY TYR SER THR          
SEQRES  31 G 1137  GLU LEU ALA LEU TRP LYS GLY VAL GLN SER LEU VAL LEU          
SEQRES  32 G 1137  GLY ALA PRO ARG TYR GLN HIS THR GLY LYS ALA VAL ILE          
SEQRES  33 G 1137  PHE THR GLN VAL SER ARG GLN TRP ARG MET LYS ALA GLU          
SEQRES  34 G 1137  VAL THR GLY THR GLN ILE GLY SER TYR PHE GLY ALA SER          
SEQRES  35 G 1137  LEU CYS SER VAL ASP VAL ASP SER ASP GLY SER THR ASP          
SEQRES  36 G 1137  LEU VAL LEU ILE GLY ALA PRO HIS TYR TYR GLU GLN THR          
SEQRES  37 G 1137  ARG GLY GLY GLN VAL SER VAL CYS PRO LEU PRO ARG GLY          
SEQRES  38 G 1137  TRP ARG ARG TRP TRP CYS ASP ALA VAL LEU TYR GLY GLU          
SEQRES  39 G 1137  GLN GLY HIS PRO TRP GLY ARG PHE GLY ALA ALA LEU THR          
SEQRES  40 G 1137  VAL LEU GLY ASP VAL ASN GLY ASP LYS LEU THR ASP VAL          
SEQRES  41 G 1137  VAL ILE GLY ALA PRO GLY GLU GLU GLU ASN ARG GLY ALA          
SEQRES  42 G 1137  VAL TYR LEU PHE HIS GLY VAL LEU GLY PRO SER ILE SER          
SEQRES  43 G 1137  PRO SER HIS SER GLN ARG ILE ALA GLY SER GLN LEU SER          
SEQRES  44 G 1137  SER ARG LEU GLN TYR PHE GLY GLN ALA LEU SER GLY GLY          
SEQRES  45 G 1137  GLN ASP LEU THR GLN ASP GLY LEU VAL ASP LEU ALA VAL          
SEQRES  46 G 1137  GLY ALA ARG GLY GLN VAL LEU LEU LEU ARG THR ARG PRO          
SEQRES  47 G 1137  VAL LEU TRP VAL GLY VAL SER MET GLN PHE ILE PRO ALA          
SEQRES  48 G 1137  GLU ILE PRO ARG SER ALA PHE GLU CYS ARG GLU GLN VAL          
SEQRES  49 G 1137  VAL SER GLU GLN THR LEU VAL GLN SER ASN ILE CYS LEU          
SEQRES  50 G 1137  TYR ILE ASP LYS ARG SER LYS ASN LEU LEU GLY SER ARG          
SEQRES  51 G 1137  ASP LEU GLN SER SER VAL THR LEU ASP LEU ALA LEU ASP          
SEQRES  52 G 1137  PRO GLY ARG LEU SER PRO ARG ALA THR PHE GLN GLU THR          
SEQRES  53 G 1137  LYS ASN ARG SER LEU SER ARG VAL ARG VAL LEU GLY LEU          
SEQRES  54 G 1137  LYS ALA HIS CYS GLU ASN PHE ASN LEU LEU LEU PRO SER          
SEQRES  55 G 1137  CYS VAL GLU ASP SER VAL THR PRO ILE THR LEU ARG LEU          
SEQRES  56 G 1137  ASN PHE THR LEU VAL GLY LYS PRO LEU LEU ALA PHE ARG          
SEQRES  57 G 1137  ASN LEU ARG PRO MET LEU ALA ALA ASP ALA GLN ARG TYR          
SEQRES  58 G 1137  PHE THR ALA SER LEU PRO PHE GLU LYS ASN CYS GLY ALA          
SEQRES  59 G 1137  ASP HIS ILE CYS GLN ASP ASN LEU GLY ILE SER PHE SER          
SEQRES  60 G 1137  PHE PRO GLY LEU LYS SER LEU LEU VAL GLY SER ASN LEU          
SEQRES  61 G 1137  GLU LEU ASN ALA GLU VAL MET VAL TRP ASN ASP GLY GLU          
SEQRES  62 G 1137  ASP SER TYR GLY THR THR ILE THR PHE SER HIS PRO ALA          
SEQRES  63 G 1137  GLY LEU SER TYR ARG TYR VAL ALA GLU GLY GLN LYS GLN          
SEQRES  64 G 1137  GLY GLN LEU ARG SER LEU HIS LEU THR CYS ASP SER ALA          
SEQRES  65 G 1137  PRO VAL GLY SER GLN GLY THR TRP SER THR SER CYS ARG          
SEQRES  66 G 1137  ILE ASN HIS LEU ILE PHE ARG GLY GLY ALA GLN ILE THR          
SEQRES  67 G 1137  PHE LEU ALA THR PHE ASP VAL SER PRO LYS ALA VAL LEU          
SEQRES  68 G 1137  GLY ASP ARG LEU LEU LEU THR ALA ASN VAL SER SER GLU          
SEQRES  69 G 1137  ASN ASN THR PRO ARG THR SER LYS THR THR PHE GLN LEU          
SEQRES  70 G 1137  GLU LEU PRO VAL LYS TYR ALA VAL TYR THR VAL VAL SER          
SEQRES  71 G 1137  SER HIS GLU GLN PHE THR LYS TYR LEU ASN PHE SER GLU          
SEQRES  72 G 1137  SER GLU GLU LYS GLU SER HIS VAL ALA MET HIS ARG TYR          
SEQRES  73 G 1137  GLN VAL ASN ASN LEU GLY GLN ARG ASP LEU PRO VAL SER          
SEQRES  74 G 1137  ILE ASN PHE TRP VAL PRO VAL GLU LEU ASN GLN GLU ALA          
SEQRES  75 G 1137  VAL TRP MET ASP VAL GLU VAL SER HIS PRO GLN ASN PRO          
SEQRES  76 G 1137  SER LEU ARG CYS SER SER GLU LYS ILE ALA PRO PRO ALA          
SEQRES  77 G 1137  SER ASP PHE LEU ALA HIS ILE GLN LYS ASN PRO VAL LEU          
SEQRES  78 G 1137  ASP CYS SER ILE ALA GLY CYS LEU ARG PHE ARG CYS ASP          
SEQRES  79 G 1137  VAL PRO SER PHE SER VAL GLN GLU GLU LEU ASP PHE THR          
SEQRES  80 G 1137  LEU LYS GLY ASN LEU SER PHE GLY TRP VAL ARG GLN ILE          
SEQRES  81 G 1137  LEU GLN LYS LYS VAL SER VAL VAL SER VAL ALA GLU ILE          
SEQRES  82 G 1137  THR PHE ASP THR SER VAL TYR SER GLN LEU PRO GLY GLN          
SEQRES  83 G 1137  GLU ALA PHE MET ARG ALA GLN THR THR THR VAL LEU GLU          
SEQRES  84 G 1137  LYS TYR LYS VAL HIS GLY CYS GLY GLY LEU GLU ASN LEU          
SEQRES  85 G 1137  TYR PHE GLN GLY GLY GLU ASN ALA GLN CYS GLU LYS GLU          
SEQRES  86 G 1137  LEU GLN ALA LEU GLU LYS GLU ASN ALA GLN LEU GLU TRP          
SEQRES  87 G 1137  GLU LEU GLN ALA LEU GLU LYS GLU LEU ALA GLN TRP SER          
SEQRES  88 G 1137  HIS PRO GLN PHE GLU LYS                                      
SEQRES   1 H  727  GLN GLU CYS THR LYS PHE LYS VAL SER SER CYS ARG GLU          
SEQRES   2 H  727  CYS ILE GLU SER GLY PRO GLY CYS THR TRP CYS GLN LYS          
SEQRES   3 H  727  LEU ASN PHE THR GLY PRO GLY ASP PRO ASP SER ILE ARG          
SEQRES   4 H  727  CYS ASP THR ARG PRO GLN LEU LEU MET ARG GLY CYS ALA          
SEQRES   5 H  727  ALA ASP ASP ILE MET ASP PRO THR SER LEU ALA GLU THR          
SEQRES   6 H  727  GLN GLU ASP HIS ASN GLY GLY GLN LYS GLN LEU SER PRO          
SEQRES   7 H  727  GLN LYS VAL THR LEU TYR LEU ARG PRO GLY GLN ALA ALA          
SEQRES   8 H  727  ALA PHE ASN VAL THR PHE ARG ARG ALA LYS GLY TYR PRO          
SEQRES   9 H  727  ILE ASP LEU TYR TYR LEU MET ASP LEU SER TYR SER MET          
SEQRES  10 H  727  LEU ASP ASP LEU ARG ASN VAL LYS LYS LEU GLY GLY ASP          
SEQRES  11 H  727  LEU LEU ARG ALA LEU ASN GLU ILE THR GLU SER GLY ARG          
SEQRES  12 H  727  ILE GLY PHE GLY SER PHE VAL ASP LYS THR VAL LEU PRO          
SEQRES  13 H  727  PHE VAL ASN THR HIS PRO ASP LYS LEU ARG ASN PRO CYS          
SEQRES  14 H  727  PRO ASN LYS GLU LYS GLU CYS GLN PRO PRO PHE ALA PHE          
SEQRES  15 H  727  ARG HIS VAL LEU LYS LEU THR ASN ASN SER ASN GLN PHE          
SEQRES  16 H  727  GLN THR GLU VAL GLY LYS GLN LEU ILE SER GLY ASN LEU          
SEQRES  17 H  727  ASP ALA PRO GLU GLY GLY LEU ASP ALA MET MET GLN VAL          
SEQRES  18 H  727  ALA ALA CYS PRO GLU GLU ILE GLY TRP ARG ASN VAL THR          
SEQRES  19 H  727  ARG LEU LEU VAL PHE ALA THR ASP ASP GLY PHE HIS PHE          
SEQRES  20 H  727  ALA GLY ASP GLY LYS LEU GLY ALA ILE LEU THR PRO ASN          
SEQRES  21 H  727  ASP GLY ARG CYS HIS LEU GLU ASP ASN LEU TYR LYS ARG          
SEQRES  22 H  727  SER ASN GLU PHE ASP TYR PRO SER VAL GLY GLN LEU ALA          
SEQRES  23 H  727  HIS LYS LEU ALA GLU ASN ASN ILE GLN PRO ILE PHE ALA          
SEQRES  24 H  727  VAL THR SER ARG MET VAL LYS THR TYR GLU LYS LEU THR          
SEQRES  25 H  727  GLU ILE ILE PRO LYS SER ALA VAL GLY GLU LEU SER GLU          
SEQRES  26 H  727  ASP SER SER ASN VAL VAL GLN LEU ILE LYS ASN ALA TYR          
SEQRES  27 H  727  ASN LYS LEU SER SER ARG VAL PHE LEU ASP HIS ASN ALA          
SEQRES  28 H  727  LEU PRO ASP THR LEU LYS VAL THR TYR ASP SER PHE CYS          
SEQRES  29 H  727  SER ASN GLY VAL THR HIS ARG ASN GLN PRO ARG GLY ASP          
SEQRES  30 H  727  CYS ASP GLY VAL GLN ILE ASN VAL PRO ILE THR PHE GLN          
SEQRES  31 H  727  VAL LYS VAL THR ALA THR GLU CYS ILE GLN GLU GLN SER          
SEQRES  32 H  727  PHE VAL ILE ARG ALA LEU GLY PHE THR ASP ILE VAL THR          
SEQRES  33 H  727  VAL GLN VAL LEU PRO GLN CYS GLU CYS ARG CYS ARG ASP          
SEQRES  34 H  727  GLN SER ARG ASP ARG SER LEU CYS HIS GLY LYS GLY PHE          
SEQRES  35 H  727  LEU GLU CYS GLY ILE CYS ARG CYS ASP THR GLY TYR ILE          
SEQRES  36 H  727  GLY LYS ASN CYS GLU CYS GLN THR GLN GLY ARG SER SER          
SEQRES  37 H  727  GLN GLU LEU GLU GLY SER CYS ARG LYS ASP ASN ASN SER          
SEQRES  38 H  727  ILE ILE CYS SER GLY LEU GLY ASP CYS VAL CYS GLY GLN          
SEQRES  39 H  727  CYS LEU CYS HIS THR SER ASP VAL PRO GLY LYS LEU ILE          
SEQRES  40 H  727  TYR GLY GLN TYR CYS GLU CYS ASP THR ILE ASN CYS GLU          
SEQRES  41 H  727  ARG TYR ASN GLY GLN VAL CYS GLY GLY PRO GLY ARG GLY          
SEQRES  42 H  727  LEU CYS PHE CYS GLY LYS CYS ARG CYS HIS PRO GLY PHE          
SEQRES  43 H  727  GLU GLY SER ALA CYS GLN CYS GLU ARG THR THR GLU GLY          
SEQRES  44 H  727  CYS LEU ASN PRO ARG ARG VAL GLU CYS SER GLY ARG GLY          
SEQRES  45 H  727  ARG CYS ARG CYS ASN VAL CYS GLU CYS HIS SER GLY TYR          
SEQRES  46 H  727  GLN LEU PRO LEU CYS GLN GLU CYS PRO GLY CYS PRO SER          
SEQRES  47 H  727  PRO CYS GLY LYS TYR ILE SER CYS ALA GLU CYS LEU LYS          
SEQRES  48 H  727  PHE GLU LYS GLY PRO PHE GLY LYS ASN CYS SER ALA ALA          
SEQRES  49 H  727  CYS PRO GLY LEU GLN LEU SER ASN ASN PRO VAL LYS GLY          
SEQRES  50 H  727  ARG THR CYS LYS GLU ARG ASP SER GLU GLY CYS TRP VAL          
SEQRES  51 H  727  ALA TYR THR LEU GLU GLN GLN ASP GLY MET ASP ARG TYR          
SEQRES  52 H  727  LEU ILE TYR VAL ASP GLU SER ARG GLU CYS VAL ASP GLY          
SEQRES  53 H  727  CYS GLY LEU GLU ASN LEU TYR PHE GLN GLY GLY LYS ASN          
SEQRES  54 H  727  ALA GLN CYS LYS LYS LYS LEU GLN ALA LEU LYS LYS LYS          
SEQRES  55 H  727  ASN ALA GLN LEU LYS TRP LYS LEU GLN ALA LEU LYS LYS          
SEQRES  56 H  727  LYS LEU ALA GLN GLY GLY HIS HIS HIS HIS HIS HIS              
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET     MG  A2009       1                                                       
HET    NAG  A3031      14                                                       
HET    NAG  A3042      14                                                       
HET    NAG  A3070      14                                                       
HET    NAG  A3071      14                                                       
HET    BMA  A3072      11                                                       
HET    MAN  A3073      11                                                       
HET    MAN  A3074      11                                                       
HET    NAG  A3373      14                                                       
HET    NAG  A3374      14                                                       
HET    BMA  A3375      11                                                       
HET    MAN  A3376      11                                                       
HET    MAN  A3377      11                                                       
HET    MAN  A3378      11                                                       
HET    MAN  A3379      11                                                       
HET    MAN  A3380      11                                                       
HET    MAN  A3381      11                                                       
HET    MAN  A3382      11                                                       
HET    NAG  A3678      14                                                       
HET    NAG  A3716      14                                                       
HET    NAG  A3717      14                                                       
HET    BMA  A3718      11                                                       
HET    MAN  A3719      11                                                       
HET    NAG  A3880      14                                                       
HET    NAG  A3881      14                                                       
HET    BMA  A3882      11                                                       
HET    NAG  A3920      14                                                       
HET     CA  B2002       1                                                       
HET    NAG  B3094      14                                                       
HET    NAG  B3095      14                                                       
HET    NAG  B3232      14                                                       
HET    NAG  B3620      14                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET    NAG  C3031      14                                                       
HET    NAG  C3042      14                                                       
HET    NAG  C3070      14                                                       
HET    NAG  C3071      14                                                       
HET    BMA  C3072      11                                                       
HET    MAN  C3073      11                                                       
HET    NAG  C3373      14                                                       
HET    NAG  C3374      14                                                       
HET    BMA  C3375      11                                                       
HET    MAN  C3376      11                                                       
HET    MAN  C3377      11                                                       
HET    MAN  C3378      11                                                       
HET    MAN  C3380      11                                                       
HET    NAG  C3678      14                                                       
HET    NAG  C3716      14                                                       
HET    NAG  C3717      14                                                       
HET    BMA  C3718      11                                                       
HET    MAN  C3719      11                                                       
HET    MAN  C3720      11                                                       
HET    NAG  C3880      14                                                       
HET    NAG  C3881      14                                                       
HET    BMA  C3882      11                                                       
HET    MAN  C3883      11                                                       
HET    MAN  C3884      11                                                       
HET    NAG  C3920      14                                                       
HET    NAG  D3232      14                                                       
HET    NAG  D3620      14                                                       
HET     CA  D2002       1                                                       
HET     CA  E2005       1                                                       
HET     CA  E2006       1                                                       
HET     CA  E2007       1                                                       
HET    NAG  E3031      14                                                       
HET    NAG  E3042      14                                                       
HET    NAG  E3070      14                                                       
HET    NAG  E3071      14                                                       
HET    BMA  E3072      11                                                       
HET    MAN  E3073      11                                                       
HET    MAN  E3074      11                                                       
HET    MAN  E3075      11                                                       
HET    NAG  E3373      14                                                       
HET    NAG  E3374      14                                                       
HET    BMA  E3375      11                                                       
HET    MAN  E3380      11                                                       
HET    NAG  E3678      14                                                       
HET    NAG  E3716      14                                                       
HET    NAG  E3717      14                                                       
HET    BMA  E3718      11                                                       
HET    MAN  E3719      11                                                       
HET    NAG  E3880      14                                                       
HET    NAG  E3881      14                                                       
HET    BMA  E3882      11                                                       
HET    MAN  E3883      11                                                       
HET    MAN  E3884      11                                                       
HET    NAG  E3920      14                                                       
HET     CA  F2002       1                                                       
HET    NAG  F3094      14                                                       
HET    NAG  F3190      14                                                       
HET    NAG  F3620      14                                                       
HET     CA  G2005       1                                                       
HET     CA  G2006       1                                                       
HET     CA  G2007       1                                                       
HET    NAG  G3031      14                                                       
HET    NAG  G3042      14                                                       
HET    NAG  G3070      14                                                       
HET    NAG  G3071      14                                                       
HET    BMA  G3072      11                                                       
HET    MAN  G3073      11                                                       
HET    MAN  G3074      11                                                       
HET    NAG  G3373      14                                                       
HET    NAG  G3374      14                                                       
HET    BMA  G3375      11                                                       
HET    MAN  G3376      11                                                       
HET    MAN  G3377      11                                                       
HET    MAN  G3379      11                                                       
HET    MAN  G3380      11                                                       
HET    NAG  G3678      14                                                       
HET    NAG  G3716      14                                                       
HET    NAG  G3717      14                                                       
HET    BMA  G3718      11                                                       
HET    MAN  G3719      11                                                       
HET    NAG  G3880      14                                                       
HET    NAG  G3881      14                                                       
HET    BMA  G3882      11                                                       
HET    MAN  G3883      11                                                       
HET    MAN  G3884      11                                                       
HET    NAG  G3920      14                                                       
HET     CA  H2002       1                                                       
HET    NAG  H3094      14                                                       
HET    NAG  H3190      14                                                       
HET    NAG  H3232      14                                                       
HET    NAG  H3620      14                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   9   CA    16(CA 2+)                                                    
FORMUL  12   MG    MG 2+                                                        
FORMUL  13  NAG    61(C8 H15 N O6)                                              
FORMUL  15  BMA    16(C6 H12 O6)                                                
FORMUL  15  MAN    35(C6 H12 O6)                                                
FORMUL  70  HOH   *67(H2 O)                                                     
HELIX    1 AA1 SER A  144  SER A  160  1                                  17    
HELIX    2 AA2 THR A  183  SER A  190  1                                   8    
HELIX    3 AA3 PRO A  193  SER A  199  1                                   7    
HELIX    4 AA4 TYR A  208  ARG A  219  1                                  12    
HELIX    5 AA5 HIS A  222  GLY A  226  5                                   5    
HELIX    6 AA6 ASP A  249  GLY A  261  1                                  13    
HELIX    7 AA7 LEU A  271  GLN A  274  5                                   4    
HELIX    8 AA8 ASN A  275  ALA A  286  1                                  12    
HELIX    9 AA9 PRO A  289  HIS A  293  1                                   5    
HELIX   10 AB1 ALA A  302  ALA A  316  1                                  15    
HELIX   11 AB2 GLY A  352  SER A  357  1                                   6    
HELIX   12 AB3 ASN A  378  ARG A  382  5                                   5    
HELIX   13 AB4 ARG A  407  THR A  411  5                                   5    
HELIX   14 AB5 GLY A  526  ARG A  531  1                                   6    
HELIX   15 AB6 GLY A  555  SER A  559  1                                   5    
HELIX   16 AB7 PRO A  614  GLU A  619  1                                   6    
HELIX   17 AB8 ASP A  990  LYS A  997  1                                   8    
HELIX   18 AB9 TRP A 1036  LEU A 1041  1                                   6    
HELIX   19 AC1 GLU A 1067  PHE A 1069  5                                   3    
HELIX   20 AC2 SER B   10  GLU B   16  1                                   7    
HELIX   21 AC3 PRO B   35  ILE B   38  5                                   4    
HELIX   22 AC4 THR B   42  ARG B   49  1                                   8    
HELIX   23 AC5 ALA B   52  ASP B   54  5                                   3    
HELIX   24 AC6 SER B  114  SER B  116  5                                   3    
HELIX   25 AC7 MET B  117  LYS B  125  1                                   9    
HELIX   26 AC8 LEU B  127  ASN B  136  1                                  10    
HELIX   27 AC9 HIS B  161  ASN B  167  1                                   7    
HELIX   28 AD1 ASN B  191  GLY B  200  1                                  10    
HELIX   29 AD2 GLY B  213  ALA B  222  1                                  10    
HELIX   30 AD3 ASP B  250  ALA B  255  5                                   6    
HELIX   31 AD4 LYS B  272  PHE B  277  5                                   6    
HELIX   32 AD5 SER B  281  ASN B  292  1                                  12    
HELIX   33 AD6 MET B  304  LYS B  310  1                                   7    
HELIX   34 AD7 ASN B  329  SER B  342  1                                  14    
HELIX   35 AD8 SER B  435  GLY B  439  5                                   5    
HELIX   36 AD9 GLU B  470  SER B  474  5                                   5    
HELIX   37 AE1 ILE B  482  GLY B  486  5                                   5    
HELIX   38 AE2 PRO B  599  LYS B  602  5                                   4    
HELIX   39 AE3 TYR B  603  LYS B  611  1                                   9    
HELIX   40 AE4 ASN B  620  CYS B  625  1                                   6    
HELIX   41 AE5 GLY C  352  SER C  357  1                                   6    
HELIX   42 AE6 ARG C  407  THR C  411  5                                   5    
HELIX   43 AE7 GLY C  526  ARG C  531  1                                   6    
HELIX   44 AE8 GLY C  555  SER C  559  1                                   5    
HELIX   45 AE9 PRO C  614  PHE C  618  5                                   5    
HELIX   46 AF1 SER C  922  GLU C  926  5                                   5    
HELIX   47 AF2 ASP C  990  ASN C  998  1                                   9    
HELIX   48 AF3 GLY C 1035  LEU C 1041  5                                   7    
HELIX   49 AF4 GLU C 1067  PHE C 1069  5                                   3    
HELIX   50 AF5 SER D   10  GLU D   16  1                                   7    
HELIX   51 AF6 PRO D   35  ILE D   38  5                                   4    
HELIX   52 AF7 THR D   42  GLY D   50  1                                   9    
HELIX   53 AF8 ALA D   52  ASP D   54  5                                   3    
HELIX   54 AF9 SER D  114  SER D  116  5                                   3    
HELIX   55 AG1 MET D  117  LYS D  125  1                                   9    
HELIX   56 AG2 LEU D  127  ASN D  136  1                                  10    
HELIX   57 AG3 HIS D  161  ASN D  167  1                                   7    
HELIX   58 AG4 ASN D  191  GLY D  200  1                                  10    
HELIX   59 AG5 GLY D  213  ALA D  222  1                                  10    
HELIX   60 AG6 CYS D  224  GLY D  229  1                                   6    
HELIX   61 AG7 ASP D  250  ALA D  255  5                                   6    
HELIX   62 AG8 TYR D  271  GLU D  276  5                                   6    
HELIX   63 AG9 SER D  281  ASN D  292  1                                  12    
HELIX   64 AH1 MET D  304  ILE D  315  1                                  12    
HELIX   65 AH2 ASN D  329  SER D  342  1                                  14    
HELIX   66 AH3 ILE D  482  GLY D  486  5                                   5    
HELIX   67 AH4 TYR D  603  LYS D  611  1                                   9    
HELIX   68 AH5 ASN D  620  CYS D  625  1                                   6    
HELIX   69 AH6 GLY E  352  SER E  357  1                                   6    
HELIX   70 AH7 ASN E  378  ARG E  382  5                                   5    
HELIX   71 AH8 ARG E  407  THR E  411  5                                   5    
HELIX   72 AH9 GLY E  526  ARG E  531  1                                   6    
HELIX   73 AI1 GLY E  555  SER E  559  1                                   5    
HELIX   74 AI2 LEU E  725  ASN E  729  5                                   5    
HELIX   75 AI3 ASP E  990  ILE E  995  1                                   6    
HELIX   76 AI4 GLY E 1035  LEU E 1041  5                                   7    
HELIX   77 AI5 GLU E 1067  PHE E 1069  5                                   3    
HELIX   78 AI6 SER F   10  GLU F   16  1                                   7    
HELIX   79 AI7 PRO F   35  ILE F   38  5                                   4    
HELIX   80 AI8 THR F   42  ARG F   49  1                                   8    
HELIX   81 AI9 ALA F   52  ASP F   54  5                                   3    
HELIX   82 AJ1 SER F  114  SER F  116  5                                   3    
HELIX   83 AJ2 MET F  117  LYS F  125  1                                   9    
HELIX   84 AJ3 LEU F  127  THR F  139  1                                  13    
HELIX   85 AJ4 HIS F  161  ASN F  167  1                                   7    
HELIX   86 AJ5 ASN F  191  LYS F  201  1                                  11    
HELIX   87 AJ6 GLY F  213  ALA F  223  1                                  11    
HELIX   88 AJ7 CYS F  224  GLY F  229  1                                   6    
HELIX   89 AJ8 ASP F  250  ALA F  255  5                                   6    
HELIX   90 AJ9 TYR F  271  GLU F  276  5                                   6    
HELIX   91 AK1 SER F  281  ASN F  292  1                                  12    
HELIX   92 AK2 THR F  301  LYS F  310  1                                  10    
HELIX   93 AK3 LYS F  310  ILE F  315  1                                   6    
HELIX   94 AK4 ASN F  329  ARG F  344  1                                  16    
HELIX   95 AK5 GLU F  470  CYS F  475  5                                   6    
HELIX   96 AK6 ILE F  482  GLY F  486  5                                   5    
HELIX   97 AK7 CYS F  600  LYS F  602  5                                   3    
HELIX   98 AK8 TYR F  603  PHE F  612  1                                  10    
HELIX   99 AK9 LYS F  614  GLY F  618  5                                   5    
HELIX  100 AL1 GLY G  352  SER G  357  1                                   6    
HELIX  101 AL2 ASN G  378  ARG G  382  5                                   5    
HELIX  102 AL3 ARG G  407  THR G  411  5                                   5    
HELIX  103 AL4 GLY G  526  ARG G  531  1                                   6    
HELIX  104 AL5 GLY G  555  SER G  559  1                                   5    
HELIX  105 AL6 PRO G  614  GLU G  619  1                                   6    
HELIX  106 AL7 LEU G  647  LEU G  652  1                                   6    
HELIX  107 AL8 LEU G  725  ASN G  729  5                                   5    
HELIX  108 AL9 ASP G  990  LYS G  997  1                                   8    
HELIX  109 AM1 GLY G 1035  GLN G 1039  5                                   5    
HELIX  110 AM2 GLU G 1067  PHE G 1069  5                                   3    
HELIX  111 AM3 SER H   10  GLU H   16  1                                   7    
HELIX  112 AM4 PRO H   35  ILE H   38  5                                   4    
HELIX  113 AM5 THR H   42  ARG H   49  1                                   8    
HELIX  114 AM6 ALA H   52  ASP H   54  5                                   3    
HELIX  115 AM7 SER H  114  SER H  116  5                                   3    
HELIX  116 AM8 MET H  117  LYS H  125  1                                   9    
HELIX  117 AM9 LEU H  127  ASN H  136  1                                  10    
HELIX  118 AN1 HIS H  161  ASN H  167  1                                   7    
HELIX  119 AN2 ASN H  191  GLY H  200  1                                  10    
HELIX  120 AN3 GLY H  213  CYS H  224  1                                  12    
HELIX  121 AN4 ASP H  250  ALA H  255  5                                   6    
HELIX  122 AN5 TYR H  271  GLU H  276  5                                   6    
HELIX  123 AN6 SER H  281  ASN H  292  1                                  12    
HELIX  124 AN7 MET H  304  GLU H  313  1                                  10    
HELIX  125 AN8 ASN H  329  SER H  342  1                                  14    
HELIX  126 AN9 GLN H  469  CYS H  475  5                                   7    
HELIX  127 AO1 ILE H  482  GLY H  486  5                                   5    
HELIX  128 AO2 PRO H  599  LYS H  602  5                                   4    
HELIX  129 AO3 TYR H  603  GLU H  613  1                                  11    
SHEET    1 AA1 4 LEU A   3  ARG A  12  0                                        
SHEET    2 AA1 4 GLN A 590  THR A 596 -1  O  VAL A 591   N  PHE A  11           
SHEET    3 AA1 4 ASP A 582  ALA A 587 -1  N  VAL A 585   O  LEU A 592           
SHEET    4 AA1 4 LEU A 569  GLN A 573 -1  N  GLN A 573   O  ASP A 582           
SHEET    1 AA2 4 SER A  21  TYR A  25  0                                        
SHEET    2 AA2 4 TRP A  29  ALA A  40 -1  O  TRP A  29   N  TYR A  25           
SHEET    3 AA2 4 GLN A  43  GLY A  51 -1  O  TYR A  48   N  VAL A  32           
SHEET    4 AA2 4 CYS A  57  PRO A  59 -1  O  GLU A  58   N  GLN A  49           
SHEET    1 AA3 4 SER A  76  THR A  80  0                                        
SHEET    2 AA3 4 GLN A  85  CYS A  97 -1  O  LEU A  87   N  ALA A  78           
SHEET    3 AA3 4 ASN A 100  LEU A 110 -1  O  ASN A 100   N  CYS A  97           
SHEET    4 AA3 4 GLN A 117  LEU A 119 -1  O  LEU A 119   N  CYS A 107           
SHEET    1 AA4 6 PHE A 178  PHE A 182  0                                        
SHEET    2 AA4 6 THR A 167  PHE A 174 -1  N  GLN A 173   O  GLN A 179           
SHEET    3 AA4 6 GLN A 131  ASP A 138  1  N  ILE A 137   O  PHE A 174           
SHEET    4 AA4 6 ALA A 232  THR A 239  1  O  ILE A 236   N  LEU A 136           
SHEET    5 AA4 6 ILE A 262  VAL A 269  1  O  ILE A 263   N  LYS A 233           
SHEET    6 AA4 6 ILE A 294  VAL A 297  1  O  VAL A 297   N  GLY A 268           
SHEET    1 AA5 3 VAL A 347  ALA A 350  0                                        
SHEET    2 AA5 3 GLY A 359  LEU A 362 -1  O  GLY A 359   N  ALA A 350           
SHEET    3 AA5 3 THR A 370  ILE A 372 -1  O  ILE A 372   N  ALA A 360           
SHEET    1 AA6 4 SER A 389  LEU A 394  0                                        
SHEET    2 AA6 4 GLN A 399  ALA A 405 -1  O  SER A 400   N  ALA A 393           
SHEET    3 AA6 4 LYS A 413  VAL A 420 -1  O  LYS A 413   N  ALA A 405           
SHEET    4 AA6 4 GLN A 423  THR A 431 -1  O  GLN A 423   N  VAL A 420           
SHEET    1 AA7 4 LEU A 443  VAL A 446  0                                        
SHEET    2 AA7 4 LEU A 456  GLY A 460 -1  O  LEU A 458   N  CYS A 444           
SHEET    3 AA7 4 VAL A 473  PRO A 477 -1  O  SER A 474   N  ILE A 459           
SHEET    4 AA7 4 ALA A 489  LEU A 491 -1  O  ALA A 489   N  VAL A 475           
SHEET    1 AA8 2 ARG A 469  GLY A 471  0                                        
SHEET    2 AA8 2 HIS A 497  PHE A 502  1  O  HIS A 497   N  GLY A 470           
SHEET    1 AA9 4 LEU A 506  GLY A 510  0                                        
SHEET    2 AA9 4 ASP A 519  ALA A 524 -1  O  ASP A 519   N  GLY A 510           
SHEET    3 AA9 4 ALA A 533  VAL A 540 -1  O  PHE A 537   N  VAL A 520           
SHEET    4 AA9 4 SER A 544  ILE A 545 -1  O  SER A 544   N  VAL A 540           
SHEET    1 AB1 4 LEU A 506  GLY A 510  0                                        
SHEET    2 AB1 4 ASP A 519  ALA A 524 -1  O  ASP A 519   N  GLY A 510           
SHEET    3 AB1 4 ALA A 533  VAL A 540 -1  O  PHE A 537   N  VAL A 520           
SHEET    4 AB1 4 GLN A 551  ALA A 554 -1  O  ILE A 553   N  VAL A 534           
SHEET    1 AB2 2 VAL A 599  LEU A 600  0                                        
SHEET    2 AB2 2 MET A 733  LEU A 734  1  O  MET A 733   N  LEU A 600           
SHEET    1 AB3 4 VAL A 602  ILE A 609  0                                        
SHEET    2 AB3 4 THR A 629  ILE A 639 -1  O  GLN A 632   N  ILE A 609           
SHEET    3 AB3 4 HIS A 692  LEU A 700 -1  O  LEU A 698   N  VAL A 631           
SHEET    4 AB3 4 THR A 672  PHE A 673 -1  N  THR A 672   O  LEU A 699           
SHEET    1 AB4 4 SER A 680  LEU A 687  0                                        
SHEET    2 AB4 4 SER A 654  LEU A 662 -1  N  LEU A 660   O  LEU A 681           
SHEET    3 AB4 4 ILE A 711  LEU A 719 -1  O  THR A 718   N  THR A 657           
SHEET    4 AB4 4 TYR A 741  LEU A 746 -1  O  LEU A 746   N  ILE A 711           
SHEET    1 AB5 4 LEU A 762  SER A 767  0                                        
SHEET    2 AB5 4 GLU A 781  ASN A 790 -1  O  MET A 787   N  SER A 765           
SHEET    3 AB5 4 GLN A 856  VAL A 865 -1  O  ILE A 857   N  VAL A 788           
SHEET    4 AB5 4 LEU A 808  ARG A 811 -1  N  SER A 809   O  ASP A 864           
SHEET    1 AB6 7 THR C 828  PRO C 833  0                                        
SHEET    2 AB6 7 THR C 839  ARG C 845 -1  O  SER C 841   N  ALA C 832           
SHEET    3 AB6 7 THR C 799  PRO C 805 -1  N  HIS C 804   O  TRP C 840           
SHEET    4 AB6 7 ARG C 874  SER C 882 -1  O  ASN C 880   N  THR C 801           
SHEET    5 AB6 7 PHE C 895  VAL C 905 -1  O  LEU C 897   N  LEU C 877           
SHEET    6 AB6 7 PHE A 895  VAL A 905 -1  N  GLU A 898   O  GLN C 896           
SHEET    7 AB6 7 TYR A1060  GLN A1062  1  O  SER A1061   N  TYR A 903           
SHEET    1 AB7 7 THR C 828  PRO C 833  0                                        
SHEET    2 AB7 7 THR C 839  ARG C 845 -1  O  SER C 841   N  ALA C 832           
SHEET    3 AB7 7 THR C 799  PRO C 805 -1  N  HIS C 804   O  TRP C 840           
SHEET    4 AB7 7 ARG C 874  SER C 882 -1  O  ASN C 880   N  THR C 801           
SHEET    5 AB7 7 PHE C 895  VAL C 905 -1  O  LEU C 897   N  LEU C 877           
SHEET    6 AB7 7 PHE A 895  VAL A 905 -1  N  GLU A 898   O  GLN C 896           
SHEET    7 AB7 7 LEU A 774  VAL A 776  1  N  VAL A 776   O  LYS A 902           
SHEET    1 AB8 4 LEU C 774  VAL C 776  0                                        
SHEET    2 AB8 4 PHE C 895  VAL C 905  1  O  LYS C 902   N  VAL C 776           
SHEET    3 AB8 4 PHE A 895  VAL A 905 -1  N  GLU A 898   O  GLN C 896           
SHEET    4 AB8 4 TYR A1060  GLN A1062  1  O  SER A1061   N  TYR A 903           
SHEET    1 AB9 7 TYR C1060  GLN C1062  0                                        
SHEET    2 AB9 7 PHE C 895  VAL C 905  1  N  TYR C 903   O  SER C1061           
SHEET    3 AB9 7 PHE A 895  VAL A 905 -1  N  GLU A 898   O  GLN C 896           
SHEET    4 AB9 7 ARG A 874  SER A 882 -1  N  LEU A 875   O  LEU A 899           
SHEET    5 AB9 7 THR A 799  PRO A 805 -1  N  THR A 801   O  ASN A 880           
SHEET    6 AB9 7 THR A 839  ILE A 846 -1  O  CYS A 844   N  ILE A 800           
SHEET    7 AB9 7 LEU A 827  VAL A 834 -1  N  ASP A 830   O  SER A 843           
SHEET    1 AC1 7 LEU A 827  VAL A 834  0                                        
SHEET    2 AC1 7 THR A 839  ILE A 846 -1  O  SER A 843   N  ASP A 830           
SHEET    3 AC1 7 THR A 799  PRO A 805 -1  N  ILE A 800   O  CYS A 844           
SHEET    4 AC1 7 ARG A 874  SER A 882 -1  O  ASN A 880   N  THR A 801           
SHEET    5 AC1 7 PHE A 895  VAL A 905 -1  O  LEU A 899   N  LEU A 875           
SHEET    6 AC1 7 PHE C 895  VAL C 905 -1  O  GLN C 896   N  GLU A 898           
SHEET    7 AC1 7 TYR C1060  GLN C1062  1  O  SER C1061   N  TYR C 903           
SHEET    1 AC2 2 SER A 795  TYR A 796  0                                        
SHEET    2 AC2 2 ILE A 850  PHE A 851 -1  O  PHE A 851   N  SER A 795           
SHEET    1 AC3 4 THR A 907  SER A 911  0                                        
SHEET    2 AC3 4 SER A 929  ASN A 940 -1  O  GLN A 937   N  SER A 910           
SHEET    3 AC3 4 GLU A1023  SER A1033 -1  O  LEU A1032   N  HIS A 930           
SHEET    4 AC3 4 GLU A 968  SER A 970 -1  N  SER A 970   O  THR A1027           
SHEET    1 AC4 4 GLU A 961  ALA A 962  0                                        
SHEET    2 AC4 4 LEU A 946  LEU A 958 -1  N  LEU A 958   O  GLU A 961           
SHEET    3 AC4 4 SER A1046  THR A1054 -1  O  THR A1054   N  SER A 949           
SHEET    4 AC4 4 VAL A1000  LEU A1001  1  N  LEU A1001   O  SER A1046           
SHEET    1 AC5 5 SER A 980  ILE A 984  0                                        
SHEET    2 AC5 5 GLY A1007  PHE A1018 -1  O  ARG A1012   N  SER A 980           
SHEET    3 AC5 5 LEU A 946  LEU A 958 -1  N  GLU A 957   O  GLY A1007           
SHEET    4 AC5 5 SER A1046  THR A1054 -1  O  THR A1054   N  SER A 949           
SHEET    5 AC5 5 ARG A1071  VAL A1077 -1  O  THR A1076   N  VAL A1047           
SHEET    1 AC6 3 CYS B  40  ASP B  41  0                                        
SHEET    2 AC6 3 THR B  22  CYS B  24 -1  N  THR B  22   O  ASP B  41           
SHEET    3 AC6 3 ILE B  56  MET B  57 -1  O  MET B  57   N  TRP B  23           
SHEET    1 AC7 6 LEU B  62  THR B  65  0                                        
SHEET    2 AC7 6 LYS B  80  LEU B  85 -1  O  THR B  82   N  GLU B  64           
SHEET    3 AC7 6 ILE B 414  PRO B 421  1  O  GLN B 418   N  LEU B  83           
SHEET    4 AC7 6 GLN B 402  LEU B 409 -1  N  GLN B 402   O  VAL B 419           
SHEET    5 AC7 6 VAL B 345  HIS B 349 -1  N  ASP B 348   O  ARG B 407           
SHEET    6 AC7 6 GLY B 376  CYS B 378 -1  O  GLY B 376   N  LEU B 347           
SHEET    1 AC8 4 LEU B  76  SER B  77  0                                        
SHEET    2 AC8 4 ALA B  91  PHE B  97 -1  O  THR B  96   N  SER B  77           
SHEET    3 AC8 4 ILE B 387  ALA B 395 -1  O  VAL B 393   N  ALA B  91           
SHEET    4 AC8 4 LEU B 356  TYR B 360 -1  N  THR B 359   O  LYS B 392           
SHEET    1 AC9 6 PHE B 182  THR B 189  0                                        
SHEET    2 AC9 6 ARG B 143  PHE B 149 -1  N  SER B 148   O  ARG B 183           
SHEET    3 AC9 6 ILE B 105  ASP B 112  1  N  MET B 111   O  PHE B 149           
SHEET    4 AC9 6 THR B 234  THR B 241  1  O  THR B 234   N  ASP B 106           
SHEET    5 AC9 6 ILE B 294  VAL B 300  1  O  ILE B 297   N  PHE B 239           
SHEET    6 AC9 6 ALA B 319  GLU B 322  1  O  ALA B 319   N  PHE B 298           
SHEET    1 AD1 2 GLY B 441  LEU B 443  0                                        
SHEET    2 AD1 2 CYS B 448  CYS B 450 -1  O  ARG B 449   N  PHE B 442           
SHEET    1 AD2 2 TYR B 454  ILE B 455  0                                        
SHEET    2 AD2 2 CYS B 461  GLN B 462 -1  O  CYS B 461   N  ILE B 455           
SHEET    1 AD3 2 ILE B 507  TYR B 508  0                                        
SHEET    2 AD3 2 CYS B 514  ASP B 515 -1  O  CYS B 514   N  TYR B 508           
SHEET    1 AD4 2 ARG B 521  TYR B 522  0                                        
SHEET    2 AD4 2 GLN B 525  VAL B 526 -1  O  GLN B 525   N  TYR B 522           
SHEET    1 AD5 2 GLY B 533  PHE B 536  0                                        
SHEET    2 AD5 2 LYS B 539  CYS B 542 -1  O  LYS B 539   N  PHE B 536           
SHEET    1 AD6 2 PHE B 546  GLU B 547  0                                        
SHEET    2 AD6 2 CYS B 553  GLU B 554 -1  O  CYS B 553   N  GLU B 547           
SHEET    1 AD7 2 ARG B 573  CYS B 574  0                                        
SHEET    2 AD7 2 CYS B 579  GLU B 580 -1  O  GLU B 580   N  ARG B 573           
SHEET    1 AD8 4 LEU B 628  LEU B 630  0                                        
SHEET    2 AD8 4 TYR B 663  VAL B 667  1  O  ILE B 665   N  GLN B 629           
SHEET    3 AD8 4 TRP B 649  GLN B 656 -1  N  GLU B 655   O  LEU B 664           
SHEET    4 AD8 4 ARG B 638  ARG B 643 -1  N  ARG B 638   O  LEU B 654           
SHEET    1 AD9 4 THR C   9  ARG C  12  0                                        
SHEET    2 AD9 4 GLN C 590  ARG C 595 -1  O  LEU C 593   N  THR C   9           
SHEET    3 AD9 4 ASP C 582  GLY C 586 -1  N  LEU C 583   O  LEU C 594           
SHEET    4 AD9 4 LEU C 569  GLN C 573 -1  N  SER C 570   O  ALA C 584           
SHEET    1 AE1 4 SER C  21  TYR C  25  0                                        
SHEET    2 AE1 4 TRP C  29  GLY C  33 -1  O  GLY C  33   N  SER C  21           
SHEET    3 AE1 4 LEU C  47  GLY C  51 -1  O  CYS C  50   N  VAL C  30           
SHEET    4 AE1 4 CYS C  57  PRO C  59 -1  O  GLU C  58   N  GLN C  49           
SHEET    1 AE2 4 SER C  76  THR C  80  0                                        
SHEET    2 AE2 4 GLN C  85  GLU C  96 -1  O  LEU C  87   N  ALA C  78           
SHEET    3 AE2 4 MET C 101  GLY C 111 -1  O  PHE C 108   N  ALA C  88           
SHEET    4 AE2 4 GLN C 114  LEU C 119 -1  O  LEU C 119   N  CYS C 107           
SHEET    1 AE3 4 SER C 338  VAL C 340  0                                        
SHEET    2 AE3 4 VAL C 347  ALA C 350 -1  O  GLY C 349   N  SER C 338           
SHEET    3 AE3 4 GLY C 359  LEU C 362 -1  O  PHE C 361   N  LEU C 348           
SHEET    4 AE3 4 THR C 370  ILE C 372 -1  O  ILE C 372   N  ALA C 360           
SHEET    1 AE4 4 THR C 390  ALA C 393  0                                        
SHEET    2 AE4 4 SER C 400  ALA C 405 -1  O  VAL C 402   N  GLU C 391           
SHEET    3 AE4 4 LYS C 413  VAL C 420 -1  O  LYS C 413   N  ALA C 405           
SHEET    4 AE4 4 GLN C 423  THR C 431 -1  O  ALA C 428   N  ILE C 416           
SHEET    1 AE5 4 SER C 442  VAL C 446  0                                        
SHEET    2 AE5 4 LEU C 456  GLU C 466 -1  O  LEU C 456   N  VAL C 446           
SHEET    3 AE5 4 ARG C 469  PRO C 477 -1  O  GLY C 471   N  TYR C 464           
SHEET    4 AE5 4 ALA C 489  LEU C 491 -1  O  LEU C 491   N  VAL C 473           
SHEET    1 AE6 4 SER C 442  VAL C 446  0                                        
SHEET    2 AE6 4 LEU C 456  GLU C 466 -1  O  LEU C 456   N  VAL C 446           
SHEET    3 AE6 4 ARG C 469  PRO C 477 -1  O  GLY C 471   N  TYR C 464           
SHEET    4 AE6 4 HIS C 497  PHE C 502  1  O  HIS C 497   N  GLY C 470           
SHEET    1 AE7 4 LEU C 506  GLY C 510  0                                        
SHEET    2 AE7 4 ASP C 519  ALA C 524 -1  O  ASP C 519   N  GLY C 510           
SHEET    3 AE7 4 ALA C 533  VAL C 540 -1  O  PHE C 537   N  VAL C 520           
SHEET    4 AE7 4 SER C 544  ILE C 545 -1  O  SER C 544   N  VAL C 540           
SHEET    1 AE8 4 LEU C 506  GLY C 510  0                                        
SHEET    2 AE8 4 ASP C 519  ALA C 524 -1  O  ASP C 519   N  GLY C 510           
SHEET    3 AE8 4 ALA C 533  VAL C 540 -1  O  PHE C 537   N  VAL C 520           
SHEET    4 AE8 4 ARG C 552  ALA C 554 -1  O  ILE C 553   N  VAL C 534           
SHEET    1 AE9 2 VAL C 599  LEU C 600  0                                        
SHEET    2 AE9 2 MET C 733  LEU C 734  1  O  MET C 733   N  LEU C 600           
SHEET    1 AF1 4 GLY C 603  ILE C 609  0                                        
SHEET    2 AF1 4 THR C 629  TYR C 638 -1  O  GLN C 632   N  ILE C 609           
SHEET    3 AF1 4 HIS C 692  LEU C 700 -1  O  LEU C 698   N  VAL C 631           
SHEET    4 AF1 4 THR C 672  PHE C 673 -1  N  THR C 672   O  LEU C 699           
SHEET    1 AF2 4 SER C 680  LEU C 687  0                                        
SHEET    2 AF2 4 SER C 654  LEU C 662 -1  N  LEU C 660   O  LEU C 681           
SHEET    3 AF2 4 ILE C 711  LEU C 719 -1  O  THR C 718   N  THR C 657           
SHEET    4 AF2 4 TYR C 741  LEU C 746 -1  O  LEU C 746   N  ILE C 711           
SHEET    1 AF3 4 LEU C 762  SER C 767  0                                        
SHEET    2 AF3 4 GLU C 781  ASN C 790 -1  O  TRP C 789   N  GLY C 763           
SHEET    3 AF3 4 GLN C 856  VAL C 865 -1  O  ALA C 861   N  ALA C 784           
SHEET    4 AF3 4 LEU C 808  ARG C 811 -1  N  SER C 809   O  ASP C 864           
SHEET    1 AF4 2 SER C 795  TYR C 796  0                                        
SHEET    2 AF4 2 ILE C 850  PHE C 851 -1  O  PHE C 851   N  SER C 795           
SHEET    1 AF5 4 THR C 907  SER C 911  0                                        
SHEET    2 AF5 4 SER C 929  ASN C 940 -1  O  GLN C 937   N  SER C 910           
SHEET    3 AF5 4 GLU C1023  SER C1033 -1  O  LEU C1032   N  HIS C 930           
SHEET    4 AF5 4 TRP C 964  SER C 970 -1  N  SER C 970   O  THR C1027           
SHEET    1 AF6 4 GLU C 961  ALA C 962  0                                        
SHEET    2 AF6 4 LEU C 946  LEU C 958 -1  N  LEU C 958   O  GLU C 961           
SHEET    3 AF6 4 SER C1046  THR C1054 -1  O  THR C1054   N  SER C 949           
SHEET    4 AF6 4 VAL C1000  LEU C1001  1  N  LEU C1001   O  VAL C1048           
SHEET    1 AF7 5 CYS C 979  ILE C 984  0                                        
SHEET    2 AF7 5 GLY C1007  PHE C1018 -1  O  ARG C1010   N  GLU C 982           
SHEET    3 AF7 5 LEU C 946  LEU C 958 -1  N  ILE C 950   O  CYS C1013           
SHEET    4 AF7 5 SER C1046  THR C1054 -1  O  THR C1054   N  SER C 949           
SHEET    5 AF7 5 ARG C1071  VAL C1077 -1  O  ALA C1072   N  ALA C1051           
SHEET    1 AF8 3 CYS D  40  ASP D  41  0                                        
SHEET    2 AF8 3 THR D  22  CYS D  24 -1  N  THR D  22   O  ASP D  41           
SHEET    3 AF8 3 ILE D  56  MET D  57 -1  O  MET D  57   N  TRP D  23           
SHEET    1 AF9 5 LEU D  62  THR D  65  0                                        
SHEET    2 AF9 5 LYS D  80  LEU D  85 -1  O  THR D  82   N  GLU D  64           
SHEET    3 AF9 5 ILE D 414  PRO D 421  1  O  GLN D 418   N  LEU D  83           
SHEET    4 AF9 5 GLN D 402  ALA D 408 -1  N  PHE D 404   O  VAL D 417           
SHEET    5 AF9 5 LEU D 347  HIS D 349 -1  N  ASP D 348   O  ARG D 407           
SHEET    1 AG1 5 LEU D  76  SER D  77  0                                        
SHEET    2 AG1 5 ALA D  91  PHE D  97 -1  O  THR D  96   N  SER D  77           
SHEET    3 AG1 5 ILE D 387  ALA D 395 -1  O  VAL D 391   N  PHE D  93           
SHEET    4 AG1 5 LEU D 356  PHE D 363 -1  N  THR D 359   O  LYS D 392           
SHEET    5 AG1 5 THR D 369  GLN D 373 -1  O  GLN D 373   N  TYR D 360           
SHEET    1 AG2 6 PHE D 182  THR D 189  0                                        
SHEET    2 AG2 6 ARG D 143  PHE D 149 -1  N  SER D 148   O  ARG D 183           
SHEET    3 AG2 6 ASP D 106  ASP D 112  1  N  LEU D 107   O  GLY D 145           
SHEET    4 AG2 6 ARG D 235  ALA D 240  1  O  ALA D 240   N  LEU D 110           
SHEET    5 AG2 6 ILE D 294  THR D 301  1  O  ILE D 297   N  LEU D 237           
SHEET    6 AG2 6 ALA D 319  LEU D 323  1  O  LEU D 323   N  VAL D 300           
SHEET    1 AG3 2 PHE D 442  GLU D 444  0                                        
SHEET    2 AG3 2 ILE D 447  ARG D 449 -1  O  ARG D 449   N  PHE D 442           
SHEET    1 AG4 2 TYR D 454  ILE D 455  0                                        
SHEET    2 AG4 2 CYS D 461  GLN D 462 -1  O  CYS D 461   N  ILE D 455           
SHEET    1 AG5 2 GLY D 488  VAL D 491  0                                        
SHEET    2 AG5 2 GLN D 494  CYS D 497 -1  O  GLN D 494   N  VAL D 491           
SHEET    1 AG6 2 ARG D 521  TYR D 522  0                                        
SHEET    2 AG6 2 GLN D 525  VAL D 526 -1  O  GLN D 525   N  TYR D 522           
SHEET    1 AG7 2 GLY D 533  PHE D 536  0                                        
SHEET    2 AG7 2 LYS D 539  CYS D 542 -1  O  ARG D 541   N  LEU D 534           
SHEET    1 AG8 2 PHE D 546  GLU D 547  0                                        
SHEET    2 AG8 2 CYS D 553  GLU D 554 -1  O  CYS D 553   N  GLU D 547           
SHEET    1 AG9 4 LEU D 628  LEU D 630  0                                        
SHEET    2 AG9 4 TYR D 663  VAL D 667  1  O  ILE D 665   N  GLN D 629           
SHEET    3 AG9 4 TRP D 649  GLN D 656 -1  N  GLU D 655   O  LEU D 664           
SHEET    4 AG9 4 ARG D 638  ARG D 643 -1  N  CYS D 640   O  TYR D 652           
SHEET    1 AH1 4 THR E   9  ARG E  12  0                                        
SHEET    2 AH1 4 GLN E 590  ARG E 595 -1  O  LEU E 593   N  THR E   9           
SHEET    3 AH1 4 ASP E 582  ALA E 587 -1  N  VAL E 585   O  LEU E 592           
SHEET    4 AH1 4 LEU E 569  GLN E 573 -1  N  GLN E 573   O  ASP E 582           
SHEET    1 AH2 4 SER E  21  TYR E  25  0                                        
SHEET    2 AH2 4 TRP E  29  ALA E  34 -1  O  TRP E  29   N  TYR E  25           
SHEET    3 AH2 4 GLY E  46  GLY E  51 -1  O  GLY E  46   N  ALA E  34           
SHEET    4 AH2 4 ALA E  56  PRO E  59 -1  O  GLU E  58   N  GLN E  49           
SHEET    1 AH3 4 SER E  76  THR E  80  0                                        
SHEET    2 AH3 4 GLN E  85  CYS E  97 -1  O  LEU E  87   N  ALA E  78           
SHEET    3 AH3 4 ASN E 100  LEU E 110 -1  O  PHE E 108   N  ALA E  88           
SHEET    4 AH3 4 GLN E 117  LEU E 119 -1  O  LEU E 119   N  CYS E 107           
SHEET    1 AH4 4 ALA E 339  VAL E 340  0                                        
SHEET    2 AH4 4 VAL E 347  ALA E 350 -1  O  VAL E 347   N  VAL E 340           
SHEET    3 AH4 4 GLY E 359  LEU E 362 -1  O  PHE E 361   N  LEU E 348           
SHEET    4 AH4 4 THR E 370  ILE E 372 -1  O  ILE E 372   N  ALA E 360           
SHEET    1 AH5 4 THR E 390  LEU E 394  0                                        
SHEET    2 AH5 4 GLN E 399  ALA E 405 -1  O  VAL E 402   N  GLU E 391           
SHEET    3 AH5 4 LYS E 413  VAL E 420 -1  O  LYS E 413   N  ALA E 405           
SHEET    4 AH5 4 GLN E 423  THR E 431 -1  O  GLN E 423   N  VAL E 420           
SHEET    1 AH6 4 SER E 442  VAL E 446  0                                        
SHEET    2 AH6 4 LEU E 456  GLY E 460 -1  O  LEU E 458   N  CYS E 444           
SHEET    3 AH6 4 VAL E 473  PRO E 477 -1  O  SER E 474   N  ILE E 459           
SHEET    4 AH6 4 ALA E 489  LEU E 491 -1  O  ALA E 489   N  VAL E 475           
SHEET    1 AH7 3 TYR E 465  GLU E 466  0                                        
SHEET    2 AH7 3 ARG E 469  GLY E 471 -1  O  ARG E 469   N  GLU E 466           
SHEET    3 AH7 3 HIS E 497  PHE E 502  1  O  PHE E 502   N  GLY E 470           
SHEET    1 AH8 4 LEU E 506  GLY E 510  0                                        
SHEET    2 AH8 4 ASP E 519  ALA E 524 -1  O  ASP E 519   N  LEU E 509           
SHEET    3 AH8 4 ALA E 533  VAL E 540 -1  O  TYR E 535   N  ILE E 522           
SHEET    4 AH8 4 SER E 544  ILE E 545 -1  O  SER E 544   N  VAL E 540           
SHEET    1 AH9 4 LEU E 506  GLY E 510  0                                        
SHEET    2 AH9 4 ASP E 519  ALA E 524 -1  O  ASP E 519   N  LEU E 509           
SHEET    3 AH9 4 ALA E 533  VAL E 540 -1  O  TYR E 535   N  ILE E 522           
SHEET    4 AH9 4 GLN E 551  ALA E 554 -1  O  GLN E 551   N  LEU E 536           
SHEET    1 AI1 2 VAL E 599  LEU E 600  0                                        
SHEET    2 AI1 2 MET E 733  LEU E 734  1  O  MET E 733   N  LEU E 600           
SHEET    1 AI2 4 VAL E 602  ILE E 609  0                                        
SHEET    2 AI2 4 THR E 629  ILE E 639 -1  O  GLN E 632   N  ILE E 609           
SHEET    3 AI2 4 HIS E 692  LEU E 700 -1  O  LEU E 698   N  VAL E 631           
SHEET    4 AI2 4 THR E 672  PHE E 673 -1  N  THR E 672   O  LEU E 699           
SHEET    1 AI3 4 SER E 680  LEU E 687  0                                        
SHEET    2 AI3 4 SER E 654  LEU E 662 -1  N  LEU E 660   O  LEU E 681           
SHEET    3 AI3 4 ILE E 711  THR E 718 -1  O  ARG E 714   N  ALA E 661           
SHEET    4 AI3 4 PHE E 742  LEU E 746 -1  O  LEU E 746   N  ILE E 711           
SHEET    1 AI4 4 LEU E 762  SER E 767  0                                        
SHEET    2 AI4 4 GLU E 781  ASN E 790 -1  O  GLU E 785   N  SER E 767           
SHEET    3 AI4 4 GLN E 856  VAL E 865 -1  O  ALA E 861   N  ALA E 784           
SHEET    4 AI4 4 LEU E 808  ARG E 811 -1  N  SER E 809   O  ASP E 864           
SHEET    1 AI5 7 LEU G 827  PRO G 833  0                                        
SHEET    2 AI5 7 THR G 839  ILE G 846 -1  O  SER G 841   N  ALA G 832           
SHEET    3 AI5 7 THR G 799  PRO G 805 -1  N  ILE G 800   O  CYS G 844           
SHEET    4 AI5 7 ARG G 874  SER G 882 -1  O  ASN G 880   N  THR G 801           
SHEET    5 AI5 7 PHE G 895  VAL G 905 -1  O  LEU G 899   N  LEU G 875           
SHEET    6 AI5 7 PHE E 895  VAL E 905 -1  N  GLN E 896   O  GLU G 898           
SHEET    7 AI5 7 TYR E1060  GLN E1062  1  O  SER E1061   N  TYR E 903           
SHEET    1 AI6 7 LEU G 827  PRO G 833  0                                        
SHEET    2 AI6 7 THR G 839  ILE G 846 -1  O  SER G 841   N  ALA G 832           
SHEET    3 AI6 7 THR G 799  PRO G 805 -1  N  ILE G 800   O  CYS G 844           
SHEET    4 AI6 7 ARG G 874  SER G 882 -1  O  ASN G 880   N  THR G 801           
SHEET    5 AI6 7 PHE G 895  VAL G 905 -1  O  LEU G 899   N  LEU G 875           
SHEET    6 AI6 7 PHE E 895  VAL E 905 -1  N  GLN E 896   O  GLU G 898           
SHEET    7 AI6 7 LEU E 774  VAL E 776  1  N  VAL E 776   O  LYS E 902           
SHEET    1 AI7 4 LEU G 774  VAL G 776  0                                        
SHEET    2 AI7 4 PHE G 895  VAL G 905  1  O  LYS G 902   N  VAL G 776           
SHEET    3 AI7 4 PHE E 895  VAL E 905 -1  N  GLN E 896   O  GLU G 898           
SHEET    4 AI7 4 TYR E1060  GLN E1062  1  O  SER E1061   N  TYR E 903           
SHEET    1 AI8 7 TYR G1060  GLN G1062  0                                        
SHEET    2 AI8 7 PHE G 895  VAL G 905  1  N  TYR G 903   O  SER G1061           
SHEET    3 AI8 7 PHE E 895  VAL E 905 -1  N  GLN E 896   O  GLU G 898           
SHEET    4 AI8 7 ARG E 874  SER E 882 -1  N  LEU E 875   O  LEU E 899           
SHEET    5 AI8 7 THR E 799  PRO E 805 -1  N  THR E 801   O  ASN E 880           
SHEET    6 AI8 7 THR E 839  ILE E 846 -1  O  CYS E 844   N  ILE E 800           
SHEET    7 AI8 7 LEU E 827  PRO E 833 -1  N  THR E 828   O  ARG E 845           
SHEET    1 AI9 7 LEU E 827  PRO E 833  0                                        
SHEET    2 AI9 7 THR E 839  ILE E 846 -1  O  ARG E 845   N  THR E 828           
SHEET    3 AI9 7 THR E 799  PRO E 805 -1  N  ILE E 800   O  CYS E 844           
SHEET    4 AI9 7 ARG E 874  SER E 882 -1  O  ASN E 880   N  THR E 801           
SHEET    5 AI9 7 PHE E 895  VAL E 905 -1  O  LEU E 899   N  LEU E 875           
SHEET    6 AI9 7 PHE G 895  VAL G 905 -1  O  GLU G 898   N  GLN E 896           
SHEET    7 AI9 7 TYR G1060  GLN G1062  1  O  SER G1061   N  TYR G 903           
SHEET    1 AJ1 4 THR E 907  SER E 911  0                                        
SHEET    2 AJ1 4 SER E 929  ASN E 940 -1  O  GLN E 937   N  SER E 910           
SHEET    3 AJ1 4 GLU E1023  SER E1033 -1  O  PHE E1026   N  TYR E 936           
SHEET    4 AJ1 4 TRP E 964  SER E 970 -1  N  MET E 965   O  ASN E1031           
SHEET    1 AJ2 4 GLU E 961  ALA E 962  0                                        
SHEET    2 AJ2 4 LEU E 946  LEU E 958 -1  N  LEU E 958   O  GLU E 961           
SHEET    3 AJ2 4 SER E1046  THR E1054 -1  O  THR E1054   N  SER E 949           
SHEET    4 AJ2 4 VAL E1000  LEU E1001  1  N  LEU E1001   O  SER E1046           
SHEET    1 AJ3 5 SER E 980  ILE E 984  0                                        
SHEET    2 AJ3 5 GLY E1007  PHE E1018 -1  O  ARG E1010   N  GLU E 982           
SHEET    3 AJ3 5 LEU E 946  LEU E 958 -1  N  ILE E 950   O  CYS E1013           
SHEET    4 AJ3 5 SER E1046  THR E1054 -1  O  THR E1054   N  SER E 949           
SHEET    5 AJ3 5 ARG E1071  VAL E1077 -1  O  THR E1076   N  VAL E1047           
SHEET    1 AJ4 3 CYS F  40  ASP F  41  0                                        
SHEET    2 AJ4 3 THR F  22  CYS F  24 -1  N  THR F  22   O  ASP F  41           
SHEET    3 AJ4 3 ILE F  56  MET F  57 -1  O  MET F  57   N  TRP F  23           
SHEET    1 AJ5 5 LEU F  62  THR F  65  0                                        
SHEET    2 AJ5 5 LYS F  80  LEU F  85 -1  O  THR F  82   N  GLU F  64           
SHEET    3 AJ5 5 ILE F 414  PRO F 421  1  O  GLN F 418   N  LEU F  83           
SHEET    4 AJ5 5 GLN F 402  ALA F 408 -1  N  PHE F 404   O  VAL F 417           
SHEET    5 AJ5 5 LEU F 347  HIS F 349 -1  N  ASP F 348   O  ARG F 407           
SHEET    1 AJ6 5 LEU F  76  SER F  77  0                                        
SHEET    2 AJ6 5 ALA F  91  PHE F  97 -1  O  THR F  96   N  SER F  77           
SHEET    3 AJ6 5 ILE F 387  ALA F 395 -1  O  VAL F 391   N  PHE F  93           
SHEET    4 AJ6 5 LEU F 356  PHE F 363 -1  N  LYS F 357   O  THR F 394           
SHEET    5 AJ6 5 THR F 369  GLN F 373 -1  O  HIS F 370   N  SER F 362           
SHEET    1 AJ7 6 PHE F 182  THR F 189  0                                        
SHEET    2 AJ7 6 ARG F 143  PHE F 149 -1  N  SER F 148   O  ARG F 183           
SHEET    3 AJ7 6 ILE F 105  ASP F 112  1  N  TYR F 109   O  GLY F 147           
SHEET    4 AJ7 6 THR F 234  THR F 241  1  O  VAL F 238   N  LEU F 110           
SHEET    5 AJ7 6 ILE F 294  VAL F 300  1  O  ALA F 299   N  PHE F 239           
SHEET    6 AJ7 6 ALA F 319  GLU F 322  1  O  ALA F 319   N  PHE F 298           
SHEET    1 AJ8 2 GLY F 441  GLU F 444  0                                        
SHEET    2 AJ8 2 ILE F 447  CYS F 450 -1  O  ILE F 447   N  GLU F 444           
SHEET    1 AJ9 2 TYR F 454  ILE F 455  0                                        
SHEET    2 AJ9 2 CYS F 461  GLN F 462 -1  O  CYS F 461   N  ILE F 455           
SHEET    1 AK1 2 GLY F 488  VAL F 491  0                                        
SHEET    2 AK1 2 GLN F 494  CYS F 497 -1  O  LEU F 496   N  ASP F 489           
SHEET    1 AK2 2 ILE F 507  TYR F 508  0                                        
SHEET    2 AK2 2 CYS F 514  ASP F 515 -1  O  CYS F 514   N  TYR F 508           
SHEET    1 AK3 2 ARG F 521  TYR F 522  0                                        
SHEET    2 AK3 2 GLN F 525  VAL F 526 -1  O  GLN F 525   N  TYR F 522           
SHEET    1 AK4 2 GLY F 533  PHE F 536  0                                        
SHEET    2 AK4 2 LYS F 539  CYS F 542 -1  O  LYS F 539   N  PHE F 536           
SHEET    1 AK5 2 PHE F 546  GLU F 547  0                                        
SHEET    2 AK5 2 CYS F 553  GLU F 554 -1  O  CYS F 553   N  GLU F 547           
SHEET    1 AK6 2 GLY F 572  CYS F 574  0                                        
SHEET    2 AK6 2 CYS F 579  CYS F 581 -1  O  GLU F 580   N  ARG F 573           
SHEET    1 AK7 4 LEU F 628  LEU F 630  0                                        
SHEET    2 AK7 4 ARG F 662  GLU F 672  1  O  ILE F 665   N  GLN F 629           
SHEET    3 AK7 4 TRP F 649  GLN F 657 -1  N  GLU F 655   O  LEU F 664           
SHEET    4 AK7 4 CYS F 640  ARG F 643 -1  N  CYS F 640   O  TYR F 652           
SHEET    1 AK8 4 THR G   9  ARG G  12  0                                        
SHEET    2 AK8 4 GLN G 590  ARG G 595 -1  O  LEU G 593   N  THR G   9           
SHEET    3 AK8 4 ASP G 582  ALA G 587 -1  N  LEU G 583   O  LEU G 594           
SHEET    4 AK8 4 LEU G 569  GLN G 573 -1  N  SER G 570   O  ALA G 584           
SHEET    1 AK9 4 VAL G  22  TYR G  25  0                                        
SHEET    2 AK9 4 TRP G  29  GLY G  33 -1  O  TRP G  29   N  TYR G  25           
SHEET    3 AK9 4 LEU G  47  CYS G  50 -1  O  CYS G  50   N  VAL G  30           
SHEET    4 AK9 4 CYS G  57  PRO G  59 -1  O  GLU G  58   N  GLN G  49           
SHEET    1 AL1 2 ILE G  38  ALA G  40  0                                        
SHEET    2 AL1 2 GLN G  43  THR G  44 -1  O  GLN G  43   N  THR G  39           
SHEET    1 AL2 4 SER G  76  THR G  80  0                                        
SHEET    2 AL2 4 GLN G  85  GLU G  96 -1  O  LEU G  87   N  ALA G  78           
SHEET    3 AL2 4 MET G 101  LEU G 110 -1  O  PHE G 108   N  ALA G  88           
SHEET    4 AL2 4 GLN G 117  LEU G 119 -1  O  LEU G 119   N  CYS G 107           
SHEET    1 AL3 4 ALA G 339  VAL G 340  0                                        
SHEET    2 AL3 4 VAL G 347  GLY G 349 -1  O  VAL G 347   N  VAL G 340           
SHEET    3 AL3 4 ALA G 360  LEU G 362 -1  O  PHE G 361   N  LEU G 348           
SHEET    4 AL3 4 THR G 370  ILE G 372 -1  O  THR G 370   N  LEU G 362           
SHEET    1 AL4 4 THR G 390  TRP G 395  0                                        
SHEET    2 AL4 4 VAL G 398  ALA G 405 -1  O  SER G 400   N  ALA G 393           
SHEET    3 AL4 4 LYS G 413  VAL G 420 -1  O  LYS G 413   N  ALA G 405           
SHEET    4 AL4 4 GLN G 423  THR G 431 -1  O  LYS G 427   N  ILE G 416           
SHEET    1 AL5 4 LEU G 443  VAL G 446  0                                        
SHEET    2 AL5 4 LEU G 456  GLY G 460 -1  O  LEU G 456   N  VAL G 446           
SHEET    3 AL5 4 VAL G 473  PRO G 477 -1  O  SER G 474   N  ILE G 459           
SHEET    4 AL5 4 ALA G 489  LEU G 491 -1  O  ALA G 489   N  VAL G 475           
SHEET    1 AL6 2 ARG G 469  GLY G 471  0                                        
SHEET    2 AL6 2 HIS G 497  PHE G 502  1  O  HIS G 497   N  GLY G 470           
SHEET    1 AL7 4 LEU G 506  GLY G 510  0                                        
SHEET    2 AL7 4 ASP G 519  GLY G 523 -1  O  ASP G 519   N  GLY G 510           
SHEET    3 AL7 4 ALA G 533  VAL G 540 -1  O  TYR G 535   N  ILE G 522           
SHEET    4 AL7 4 SER G 544  ILE G 545 -1  O  SER G 544   N  VAL G 540           
SHEET    1 AL8 4 LEU G 506  GLY G 510  0                                        
SHEET    2 AL8 4 ASP G 519  GLY G 523 -1  O  ASP G 519   N  GLY G 510           
SHEET    3 AL8 4 ALA G 533  VAL G 540 -1  O  TYR G 535   N  ILE G 522           
SHEET    4 AL8 4 ARG G 552  ALA G 554 -1  O  ILE G 553   N  VAL G 534           
SHEET    1 AL9 2 VAL G 599  LEU G 600  0                                        
SHEET    2 AL9 2 MET G 733  LEU G 734  1  O  MET G 733   N  LEU G 600           
SHEET    1 AM1 4 VAL G 602  ILE G 609  0                                        
SHEET    2 AM1 4 THR G 629  ILE G 639 -1  O  GLN G 632   N  ILE G 609           
SHEET    3 AM1 4 HIS G 692  LEU G 700 -1  O  PHE G 696   N  SER G 633           
SHEET    4 AM1 4 THR G 672  PHE G 673 -1  N  THR G 672   O  LEU G 699           
SHEET    1 AM2 3 SER G 680  LEU G 681  0                                        
SHEET    2 AM2 3 SER G 655  LEU G 662 -1  N  LEU G 660   O  LEU G 681           
SHEET    3 AM2 3 VAL G 684  VAL G 686 -1  O  ARG G 685   N  VAL G 656           
SHEET    1 AM3 4 SER G 680  LEU G 681  0                                        
SHEET    2 AM3 4 SER G 655  LEU G 662 -1  N  LEU G 660   O  LEU G 681           
SHEET    3 AM3 4 ILE G 711  LEU G 719 -1  O  ASN G 716   N  ASP G 659           
SHEET    4 AM3 4 TYR G 741  LEU G 746 -1  O  PHE G 742   N  LEU G 715           
SHEET    1 AM4 4 LEU G 762  SER G 767  0                                        
SHEET    2 AM4 4 GLU G 781  ASN G 790 -1  O  MET G 787   N  SER G 765           
SHEET    3 AM4 4 GLN G 856  VAL G 865 -1  O  ALA G 861   N  ALA G 784           
SHEET    4 AM4 4 LEU G 808  TYR G 810 -1  N  SER G 809   O  ASP G 864           
SHEET    1 AM5 4 THR G 907  SER G 911  0                                        
SHEET    2 AM5 4 SER G 929  ASN G 940 -1  O  GLN G 937   N  SER G 910           
SHEET    3 AM5 4 GLU G1023  SER G1033 -1  O  LEU G1028   N  HIS G 934           
SHEET    4 AM5 4 TRP G 964  SER G 970 -1  N  GLU G 968   O  LYS G1029           
SHEET    1 AM6 4 GLU G 961  ALA G 962  0                                        
SHEET    2 AM6 4 VAL G 948  LEU G 958 -1  N  LEU G 958   O  GLU G 961           
SHEET    3 AM6 4 SER G1046  THR G1054 -1  O  GLU G1052   N  ASN G 951           
SHEET    4 AM6 4 VAL G1000  LEU G1001  1  N  LEU G1001   O  SER G1046           
SHEET    1 AM7 5 CYS G 979  ILE G 984  0                                        
SHEET    2 AM7 5 GLY G1007  VAL G1015 -1  O  ARG G1012   N  SER G 980           
SHEET    3 AM7 5 VAL G 948  LEU G 958 -1  N  ILE G 950   O  CYS G1013           
SHEET    4 AM7 5 SER G1046  THR G1054 -1  O  GLU G1052   N  ASN G 951           
SHEET    5 AM7 5 ARG G1071  VAL G1077 -1  O  ALA G1072   N  ALA G1051           
SHEET    1 AM8 3 CYS H  40  ASP H  41  0                                        
SHEET    2 AM8 3 THR H  22  CYS H  24 -1  N  THR H  22   O  ASP H  41           
SHEET    3 AM8 3 ILE H  56  MET H  57 -1  O  MET H  57   N  TRP H  23           
SHEET    1 AM9 5 LEU H  62  THR H  65  0                                        
SHEET    2 AM9 5 LYS H  80  LEU H  85 -1  O  THR H  82   N  GLU H  64           
SHEET    3 AM9 5 ILE H 414  PRO H 421  1  O  GLN H 418   N  LEU H  83           
SHEET    4 AM9 5 GLN H 402  ALA H 408 -1  N  PHE H 404   O  VAL H 417           
SHEET    5 AM9 5 LEU H 347  HIS H 349 -1  N  ASP H 348   O  ARG H 407           
SHEET    1 AN1 4 LEU H  76  SER H  77  0                                        
SHEET    2 AN1 4 ALA H  91  PHE H  97 -1  O  THR H  96   N  SER H  77           
SHEET    3 AN1 4 ILE H 387  ALA H 395 -1  O  VAL H 391   N  PHE H  93           
SHEET    4 AN1 4 LEU H 356  PHE H 363 -1  N  THR H 359   O  LYS H 392           
SHEET    1 AN2 6 PHE H 182  HIS H 184  0                                        
SHEET    2 AN2 6 ARG H 143  PHE H 149 -1  N  SER H 148   O  ARG H 183           
SHEET    3 AN2 6 ASP H 106  ASP H 112  1  N  LEU H 107   O  GLY H 145           
SHEET    4 AN2 6 ARG H 235  THR H 241  1  O  LEU H 236   N  TYR H 108           
SHEET    5 AN2 6 ILE H 294  THR H 301  1  O  ALA H 299   N  PHE H 239           
SHEET    6 AN2 6 ALA H 319  LEU H 323  1  O  ALA H 319   N  PHE H 298           
SHEET    1 AN3 2 LEU H 443  GLU H 444  0                                        
SHEET    2 AN3 2 ILE H 447  CYS H 448 -1  O  ILE H 447   N  GLU H 444           
SHEET    1 AN4 2 TYR H 454  ILE H 455  0                                        
SHEET    2 AN4 2 CYS H 461  GLN H 462 -1  O  CYS H 461   N  ILE H 455           
SHEET    1 AN5 2 GLY H 488  VAL H 491  0                                        
SHEET    2 AN5 2 GLN H 494  CYS H 497 -1  O  GLN H 494   N  VAL H 491           
SHEET    1 AN6 2 ARG H 521  TYR H 522  0                                        
SHEET    2 AN6 2 GLN H 525  VAL H 526 -1  O  GLN H 525   N  TYR H 522           
SHEET    1 AN7 2 GLY H 533  PHE H 536  0                                        
SHEET    2 AN7 2 LYS H 539  CYS H 542 -1  O  ARG H 541   N  LEU H 534           
SHEET    1 AN8 2 PHE H 546  GLU H 547  0                                        
SHEET    2 AN8 2 CYS H 553  GLU H 554 -1  O  CYS H 553   N  GLU H 547           
SHEET    1 AN9 2 GLY H 572  CYS H 574  0                                        
SHEET    2 AN9 2 CYS H 579  CYS H 581 -1  O  GLU H 580   N  ARG H 573           
SHEET    1 AO1 4 LEU H 628  LEU H 630  0                                        
SHEET    2 AO1 4 TYR H 663  VAL H 667  1  O  ILE H 665   N  GLN H 629           
SHEET    3 AO1 4 TRP H 649  GLN H 656 -1  N  GLU H 655   O  LEU H 664           
SHEET    4 AO1 4 ARG H 638  ARG H 643 -1  N  ARG H 638   O  LEU H 654           
SSBOND   1 CYS A   50    CYS A   57                          1555   1555  2.03  
SSBOND   2 CYS A   89    CYS A  107                          1555   1555  2.03  
SSBOND   3 CYS A   97    CYS A  126                          1555   1555  2.03  
SSBOND   4 CYS A  476    CYS A  487                          1555   1555  2.03  
SSBOND   5 CYS A  620    CYS A  703                          1555   1555  2.03  
SSBOND   6 CYS A  636    CYS A  693                          1555   1555  2.03  
SSBOND   7 CYS A  752    CYS A  758                          1555   1555  2.03  
SSBOND   8 CYS A  829    CYS A  844                          1555   1555  2.03  
SSBOND   9 CYS A  979    CYS A 1013                          1555   1555  2.04  
SSBOND  10 CYS A 1003    CYS A 1008                          1555   1555  2.02  
SSBOND  11 CYS B    3    CYS B   21                          1555   1555  2.03  
SSBOND  12 CYS B   11    CYS B  425                          1555   1555  2.04  
SSBOND  13 CYS B   14    CYS B   40                          1555   1555  2.03  
SSBOND  14 CYS B   24    CYS B   51                          1555   1555  2.03  
SSBOND  15 CYS B  169    CYS B  176                          1555   1555  2.02  
SSBOND  16 CYS B  224    CYS B  264                          1555   1555  2.03  
SSBOND  17 CYS B  364    CYS B  378                          1555   1555  2.02  
SSBOND  18 CYS B  398    CYS B  423                          1555   1555  2.02  
SSBOND  19 CYS B  427    CYS B  445                          1555   1555  2.03  
SSBOND  20 CYS B  437    CYS B  448                          1555   1555  2.02  
SSBOND  21 CYS B  450    CYS B  459                          1555   1555  2.03  
SSBOND  22 CYS B  461    CYS B  492                          1555   1555  2.03  
SSBOND  23 CYS B  475    CYS B  490                          1555   1555  2.04  
SSBOND  24 CYS B  484    CYS B  495                          1555   1555  2.03  
SSBOND  25 CYS B  497    CYS B  512                          1555   1555  2.03  
SSBOND  26 CYS B  514    CYS B  537                          1555   1555  2.02  
SSBOND  27 CYS B  519    CYS B  535                          1555   1555  2.03  
SSBOND  28 CYS B  527    CYS B  540                          1555   1555  2.03  
SSBOND  29 CYS B  542    CYS B  551                          1555   1555  2.03  
SSBOND  30 CYS B  553    CYS B  576                          1555   1555  2.02  
SSBOND  31 CYS B  560    CYS B  574                          1555   1555  2.03  
SSBOND  32 CYS B  568    CYS B  579                          1555   1555  2.03  
SSBOND  33 CYS B  581    CYS B  590                          1555   1555  2.03  
SSBOND  34 CYS B  593    CYS B  596                          1555   1555  2.04  
SSBOND  35 CYS B  600    CYS B  640                          1555   1555  2.03  
SSBOND  36 CYS B  606    CYS B  625                          1555   1555  2.03  
SSBOND  37 CYS B  609    CYS B  621                          1555   1555  2.02  
SSBOND  38 CYS B  648    CYS B  673                          1555   1555  2.03  
SSBOND  39 CYS C   50    CYS C   57                          1555   1555  2.03  
SSBOND  40 CYS C   89    CYS C  107                          1555   1555  2.03  
SSBOND  41 CYS C   97    CYS C  126                          1555   1555  2.03  
SSBOND  42 CYS C  476    CYS C  487                          1555   1555  2.03  
SSBOND  43 CYS C  620    CYS C  703                          1555   1555  2.03  
SSBOND  44 CYS C  636    CYS C  693                          1555   1555  2.04  
SSBOND  45 CYS C  752    CYS C  758                          1555   1555  2.02  
SSBOND  46 CYS C  829    CYS C  844                          1555   1555  2.03  
SSBOND  47 CYS C 1003    CYS C 1008                          1555   1555  2.03  
SSBOND  48 CYS D    3    CYS D   21                          1555   1555  2.03  
SSBOND  49 CYS D   11    CYS D  425                          1555   1555  2.04  
SSBOND  50 CYS D   14    CYS D   40                          1555   1555  2.03  
SSBOND  51 CYS D   24    CYS D   51                          1555   1555  2.03  
SSBOND  52 CYS D  169    CYS D  176                          1555   1555  2.03  
SSBOND  53 CYS D  224    CYS D  264                          1555   1555  2.03  
SSBOND  54 CYS D  364    CYS D  378                          1555   1555  2.04  
SSBOND  55 CYS D  398    CYS D  423                          1555   1555  2.04  
SSBOND  56 CYS D  427    CYS D  445                          1555   1555  2.03  
SSBOND  57 CYS D  437    CYS D  448                          1555   1555  2.03  
SSBOND  58 CYS D  450    CYS D  459                          1555   1555  2.03  
SSBOND  59 CYS D  461    CYS D  492                          1555   1555  2.02  
SSBOND  60 CYS D  475    CYS D  490                          1555   1555  2.03  
SSBOND  61 CYS D  484    CYS D  495                          1555   1555  2.03  
SSBOND  62 CYS D  497    CYS D  512                          1555   1555  2.03  
SSBOND  63 CYS D  514    CYS D  537                          1555   1555  2.03  
SSBOND  64 CYS D  519    CYS D  535                          1555   1555  2.03  
SSBOND  65 CYS D  527    CYS D  540                          1555   1555  2.03  
SSBOND  66 CYS D  542    CYS D  551                          1555   1555  2.03  
SSBOND  67 CYS D  553    CYS D  576                          1555   1555  2.02  
SSBOND  68 CYS D  560    CYS D  574                          1555   1555  2.03  
SSBOND  69 CYS D  568    CYS D  579                          1555   1555  2.03  
SSBOND  70 CYS D  581    CYS D  590                          1555   1555  2.03  
SSBOND  71 CYS D  593    CYS D  596                          1555   1555  2.03  
SSBOND  72 CYS D  600    CYS D  640                          1555   1555  2.04  
SSBOND  73 CYS D  606    CYS D  625                          1555   1555  2.03  
SSBOND  74 CYS D  609    CYS D  621                          1555   1555  2.02  
SSBOND  75 CYS D  648    CYS D  673                          1555   1555  2.03  
SSBOND  76 CYS E   50    CYS E   57                          1555   1555  2.03  
SSBOND  77 CYS E   89    CYS E  107                          1555   1555  2.03  
SSBOND  78 CYS E   97    CYS E  126                          1555   1555  2.04  
SSBOND  79 CYS E  476    CYS E  487                          1555   1555  2.04  
SSBOND  80 CYS E  620    CYS E  703                          1555   1555  2.03  
SSBOND  81 CYS E  636    CYS E  693                          1555   1555  2.03  
SSBOND  82 CYS E  752    CYS E  758                          1555   1555  2.03  
SSBOND  83 CYS E  829    CYS E  844                          1555   1555  2.03  
SSBOND  84 CYS E  979    CYS E 1013                          1555   1555  2.04  
SSBOND  85 CYS E 1003    CYS E 1008                          1555   1555  2.02  
SSBOND  86 CYS F    3    CYS F   21                          1555   1555  2.03  
SSBOND  87 CYS F   11    CYS F  425                          1555   1555  2.04  
SSBOND  88 CYS F   14    CYS F   40                          1555   1555  2.03  
SSBOND  89 CYS F   24    CYS F   51                          1555   1555  2.03  
SSBOND  90 CYS F  169    CYS F  176                          1555   1555  2.03  
SSBOND  91 CYS F  224    CYS F  264                          1555   1555  2.02  
SSBOND  92 CYS F  398    CYS F  423                          1555   1555  2.03  
SSBOND  93 CYS F  427    CYS F  445                          1555   1555  2.03  
SSBOND  94 CYS F  437    CYS F  459                          1555   1555  2.03  
SSBOND  95 CYS F  461    CYS F  492                          1555   1555  2.01  
SSBOND  96 CYS F  475    CYS F  490                          1555   1555  2.03  
SSBOND  97 CYS F  484    CYS F  495                          1555   1555  2.03  
SSBOND  98 CYS F  497    CYS F  512                          1555   1555  2.02  
SSBOND  99 CYS F  514    CYS F  537                          1555   1555  2.03  
SSBOND 100 CYS F  519    CYS F  535                          1555   1555  2.02  
SSBOND 101 CYS F  527    CYS F  540                          1555   1555  2.03  
SSBOND 102 CYS F  542    CYS F  551                          1555   1555  2.03  
SSBOND 103 CYS F  568    CYS F  579                          1555   1555  2.03  
SSBOND 104 CYS F  581    CYS F  590                          1555   1555  2.02  
SSBOND 105 CYS F  593    CYS F  596                          1555   1555  2.03  
SSBOND 106 CYS F  600    CYS F  640                          1555   1555  2.03  
SSBOND 107 CYS F  606    CYS F  625                          1555   1555  2.03  
SSBOND 108 CYS F  648    CYS F  673                          1555   1555  2.03  
SSBOND 109 CYS G   50    CYS G   57                          1555   1555  2.03  
SSBOND 110 CYS G   89    CYS G  107                          1555   1555  2.03  
SSBOND 111 CYS G   97    CYS G  126                          1555   1555  2.03  
SSBOND 112 CYS G  476    CYS G  487                          1555   1555  2.04  
SSBOND 113 CYS G  620    CYS G  703                          1555   1555  2.03  
SSBOND 114 CYS G  636    CYS G  693                          1555   1555  2.04  
SSBOND 115 CYS G  752    CYS G  758                          1555   1555  2.03  
SSBOND 116 CYS G  829    CYS G  844                          1555   1555  2.03  
SSBOND 117 CYS G  979    CYS G 1013                          1555   1555  2.03  
SSBOND 118 CYS G 1003    CYS G 1008                          1555   1555  2.02  
SSBOND 119 CYS H    3    CYS H   21                          1555   1555  2.03  
SSBOND 120 CYS H   11    CYS H  425                          1555   1555  2.04  
SSBOND 121 CYS H   14    CYS H   40                          1555   1555  2.03  
SSBOND 122 CYS H   24    CYS H   51                          1555   1555  2.03  
SSBOND 123 CYS H  169    CYS H  176                          1555   1555  2.03  
SSBOND 124 CYS H  224    CYS H  264                          1555   1555  2.02  
SSBOND 125 CYS H  364    CYS H  378                          1555   1555  2.02  
SSBOND 126 CYS H  398    CYS H  423                          1555   1555  2.04  
SSBOND 127 CYS H  427    CYS H  445                          1555   1555  2.03  
SSBOND 128 CYS H  437    CYS H  448                          1555   1555  2.03  
SSBOND 129 CYS H  450    CYS H  459                          1555   1555  2.03  
SSBOND 130 CYS H  461    CYS H  492                          1555   1555  2.03  
SSBOND 131 CYS H  475    CYS H  490                          1555   1555  2.03  
SSBOND 132 CYS H  484    CYS H  495                          1555   1555  2.03  
SSBOND 133 CYS H  497    CYS H  512                          1555   1555  2.03  
SSBOND 134 CYS H  514    CYS H  537                          1555   1555  2.03  
SSBOND 135 CYS H  519    CYS H  535                          1555   1555  2.02  
SSBOND 136 CYS H  527    CYS H  540                          1555   1555  2.03  
SSBOND 137 CYS H  542    CYS H  551                          1555   1555  2.03  
SSBOND 138 CYS H  553    CYS H  576                          1555   1555  2.02  
SSBOND 139 CYS H  560    CYS H  574                          1555   1555  2.02  
SSBOND 140 CYS H  568    CYS H  579                          1555   1555  2.02  
SSBOND 141 CYS H  581    CYS H  590                          1555   1555  2.03  
SSBOND 142 CYS H  593    CYS H  596                          1555   1555  2.03  
SSBOND 143 CYS H  600    CYS H  640                          1555   1555  2.02  
SSBOND 144 CYS H  606    CYS H  625                          1555   1555  2.03  
SSBOND 145 CYS H  609    CYS H  621                          1555   1555  2.02  
SSBOND 146 CYS H  648    CYS H  673                          1555   1555  2.03  
LINK         ND2 ASN A  42                 C1  NAG A3042     1555   1555  1.47  
LINK         ND2 ASN A  70                 C1  NAG A3070     1555   1555  1.43  
LINK         OG  SER A 140                MG    MG A2009     1555   1555  2.14  
LINK         OG  SER A 142                MG    MG A2009     1555   1555  2.08  
LINK         OD1 ASP A 240                MG    MG A2009     1555   1555  2.21  
LINK         ND2 ASN A 373                 C1  NAG A3373     1555   1555  1.45  
LINK         OD1 ASP A 447                CA    CA A2005     1555   1555  2.25  
LINK         OD1 ASP A 449                CA    CA A2005     1555   1555  2.49  
LINK         OD1 ASP A 451                CA    CA A2005     1555   1555  2.26  
LINK         OD2 ASP A 451                CA    CA A2005     1555   1555  3.08  
LINK         O   SER A 453                CA    CA A2005     1555   1555  2.55  
LINK         OD1 ASP A 455                CA    CA A2005     1555   1555  2.30  
LINK         OD2 ASP A 455                CA    CA A2005     1555   1555  2.36  
LINK         OD1 ASP A 511                CA    CA A2006     1555   1555  2.41  
LINK         OD1 ASN A 513                CA    CA A2006     1555   1555  2.43  
LINK         OD1 ASP A 515                CA    CA A2006     1555   1555  2.45  
LINK         O   LEU A 517                CA    CA A2006     1555   1555  2.53  
LINK         OD2 ASP A 519                CA    CA A2006     1555   1555  2.46  
LINK         OD1 ASP A 574                CA    CA A2007     1555   1555  2.38  
LINK         OG1 THR A 576                CA    CA A2007     1555   1555  2.40  
LINK         OD1 ASP A 578                CA    CA A2007     1555   1555  2.37  
LINK         O   LEU A 580                CA    CA A2007     1555   1555  2.55  
LINK         OD1 ASP A 582                CA    CA A2007     1555   1555  2.42  
LINK         OD2 ASP A 582                CA    CA A2007     1555   1555  2.89  
LINK         ND2 ASN A 678                 C1  NAG A3678     1555   1555  1.40  
LINK         ND2 ASN A 716                 C1  NAG A3716     1555   1555  1.45  
LINK         ND2 ASN A 880                 C1  NAG A3880     1555   1555  1.45  
LINK         ND2 ASN A 920                 C1  NAG A3920     1555   1555  1.45  
LINK         ND2 ASN A1031                 C1  NAG A3031     1555   1555  1.43  
LINK         ND2 ASN B  94                 C1  NAG B3094     1555   1555  1.43  
LINK         O   SER B 116                CA    CA B2002     1555   1555  2.40  
LINK         OD2 ASP B 120                CA    CA B2002     1555   1555  2.38  
LINK         ND2 ASN B 232                 C1  NAG B3232     1555   1555  1.41  
LINK         OE2 GLU B 325                CA    CA B2002     1555   1555  3.02  
LINK         ND2 ASN B 620                 C1  NAG B3620     1555   1555  1.41  
LINK         ND2 ASN C  42                 C1  NAG C3042     1555   1555  1.49  
LINK         ND2 ASN C  70                 C1  NAG C3070     1555   1555  1.43  
LINK         ND2 ASN C 373                 C1  NAG C3373     1555   1555  1.43  
LINK         OD1 ASP C 447                CA    CA C2005     1555   1555  3.10  
LINK         OD1 ASP C 449                CA    CA C2005     1555   1555  2.41  
LINK         OD2 ASP C 449                CA    CA C2005     1555   1555  2.95  
LINK         OD1 ASP C 451                CA    CA C2005     1555   1555  2.48  
LINK         OD2 ASP C 451                CA    CA C2005     1555   1555  2.56  
LINK         OD1 ASP C 455                CA    CA C2005     1555   1555  2.48  
LINK         OD2 ASP C 455                CA    CA C2005     1555   1555  2.59  
LINK         OD1 ASP C 511                CA    CA C2006     1555   1555  2.36  
LINK         OD1 ASN C 513                CA    CA C2006     1555   1555  2.40  
LINK         OD1 ASP C 515                CA    CA C2006     1555   1555  2.40  
LINK         O   LEU C 517                CA    CA C2006     1555   1555  2.33  
LINK         OD2 ASP C 519                CA    CA C2006     1555   1555  2.44  
LINK         OD1 ASP C 574                CA    CA C2007     1555   1555  2.41  
LINK         OG1 THR C 576                CA    CA C2007     1555   1555  2.33  
LINK         OD1 ASP C 578                CA    CA C2007     1555   1555  2.37  
LINK         O   LEU C 580                CA    CA C2007     1555   1555  2.09  
LINK         OD1 ASP C 582                CA    CA C2007     1555   1555  2.44  
LINK         OD2 ASP C 582                CA    CA C2007     1555   1555  2.84  
LINK         ND2 ASN C 678                 C1  NAG C3678     1555   1555  1.41  
LINK         ND2 ASN C 716                 C1  NAG C3716     1555   1555  1.46  
LINK         ND2 ASN C 880                 C1  NAG C3880     1555   1555  1.46  
LINK         ND2 ASN C 920                 C1  NAG C3920     1555   1555  1.44  
LINK         ND2 ASN C1031                 C1  NAG C3031     1555   1555  1.45  
LINK         O   SER D 116                CA    CA D2002     1555   1555  2.43  
LINK         ND2 ASN D 232                 C1  NAG D3232     1555   1555  1.46  
LINK         OE2 GLU D 325                CA    CA D2002     1555   1555  2.41  
LINK         ND2 ASN D 620                 C1  NAG D3620     1555   1555  1.44  
LINK         ND2 ASN E  42                 C1  NAG E3042     1555   1555  1.43  
LINK         ND2 ASN E  70                 C1  NAG E3070     1555   1555  1.44  
LINK         ND2 ASN E 373                 C1  NAG E3373     1555   1555  1.44  
LINK         OD1 ASP E 447                CA    CA E2005     1555   1555  2.93  
LINK         OD1 ASP E 451                CA    CA E2005     1555   1555  2.33  
LINK         OD2 ASP E 451                CA    CA E2005     1555   1555  2.67  
LINK         O   SER E 453                CA    CA E2005     1555   1555  2.48  
LINK         OD1 ASP E 455                CA    CA E2005     1555   1555  2.49  
LINK         OD2 ASP E 455                CA    CA E2005     1555   1555  2.54  
LINK         OD1 ASP E 511                CA    CA E2006     1555   1555  2.39  
LINK         OD1 ASN E 513                CA    CA E2006     1555   1555  2.38  
LINK         OD1 ASP E 515                CA    CA E2006     1555   1555  2.43  
LINK         O   LEU E 517                CA    CA E2006     1555   1555  2.41  
LINK         OD1 ASP E 519                CA    CA E2006     1555   1555  3.16  
LINK         OD2 ASP E 519                CA    CA E2006     1555   1555  2.48  
LINK         OD1 ASP E 574                CA    CA E2007     1555   1555  2.36  
LINK         OG1 THR E 576                CA    CA E2007     1555   1555  2.38  
LINK         OD1 ASP E 578                CA    CA E2007     1555   1555  2.46  
LINK         O   LEU E 580                CA    CA E2007     1555   1555  2.42  
LINK         OD1 ASP E 582                CA    CA E2007     1555   1555  2.40  
LINK         OD2 ASP E 582                CA    CA E2007     1555   1555  2.44  
LINK         ND2 ASN E 678                 C1  NAG E3678     1555   1555  1.39  
LINK         ND2 ASN E 716                 C1  NAG E3716     1555   1555  1.44  
LINK         ND2 ASN E 880                 C1  NAG E3880     1555   1555  1.44  
LINK         ND2 ASN E 920                 C1  NAG E3920     1555   1555  1.42  
LINK         ND2 ASN E1031                 C1  NAG E3031     1555   1555  1.43  
LINK         ND2 ASN F  94                 C1  NAG F3094     1555   1555  1.45  
LINK         O   SER F 116                CA    CA F2002     1555   1555  2.48  
LINK         OD2 ASP F 120                CA    CA F2002     1555   1555  2.42  
LINK         ND2 ASN F 190                 C1  NAG F3190     1555   1555  1.41  
LINK         OE1 GLU F 325                CA    CA F2002     1555   1555  2.45  
LINK         ND2 ASN F 620                 C1  NAG F3620     1555   1555  1.43  
LINK         ND2 ASN G  42                 C1  NAG G3042     1555   1555  1.48  
LINK         ND2 ASN G  70                 C1  NAG G3070     1555   1555  1.44  
LINK         ND2 ASN G 373                 C1  NAG G3373     1555   1555  1.44  
LINK         OD1 ASP G 447                CA    CA G2005     1555   1555  2.30  
LINK         OD1 ASP G 449                CA    CA G2005     1555   1555  2.46  
LINK         OD1 ASP G 451                CA    CA G2005     1555   1555  2.38  
LINK         O   SER G 453                CA    CA G2005     1555   1555  2.51  
LINK         OD1 ASP G 455                CA    CA G2005     1555   1555  2.39  
LINK         OD2 ASP G 455                CA    CA G2005     1555   1555  2.47  
LINK         OD1 ASP G 511                CA    CA G2006     1555   1555  2.35  
LINK         OD1 ASN G 513                CA    CA G2006     1555   1555  2.42  
LINK         OD1 ASP G 515                CA    CA G2006     1555   1555  2.36  
LINK         O   LEU G 517                CA    CA G2006     1555   1555  2.47  
LINK         OD1 ASP G 519                CA    CA G2006     1555   1555  3.16  
LINK         OD2 ASP G 519                CA    CA G2006     1555   1555  2.48  
LINK         OG1 THR G 576                CA    CA G2007     1555   1555  2.51  
LINK         OD1 ASP G 578                CA    CA G2007     1555   1555  2.28  
LINK         O   LEU G 580                CA    CA G2007     1555   1555  2.56  
LINK         OD1 ASP G 582                CA    CA G2007     1555   1555  2.32  
LINK         ND2 ASN G 678                 C1  NAG G3678     1555   1555  1.40  
LINK         ND2 ASN G 716                 C1  NAG G3716     1555   1555  1.47  
LINK         ND2 ASN G 880                 C1  NAG G3880     1555   1555  1.44  
LINK         ND2 ASN G 920                 C1  NAG G3920     1555   1555  1.44  
LINK         ND2 ASN G1031                 C1  NAG G3031     1555   1555  1.43  
LINK         ND2 ASN H  94                 C1  NAG H3094     1555   1555  1.42  
LINK         O   SER H 116                CA    CA H2002     1555   1555  2.39  
LINK         OD2 ASP H 120                CA    CA H2002     1555   1555  2.32  
LINK         ND2 ASN H 190                 C1  NAG H3190     1555   1555  1.40  
LINK         ND2 ASN H 232                 C1  NAG H3232     1555   1555  1.48  
LINK         O   GLU H 325                CA    CA H2002     1555   1555  3.10  
LINK         OE2 GLU H 325                CA    CA H2002     1555   1555  2.34  
LINK         ND2 ASN H 620                 C1  NAG H3620     1555   1555  1.47  
LINK        CA    CA A2007                 O   HOH A4020     1555   1555  3.14  
LINK        MG    MG A2009                 O   HOH A4008     1555   1555  2.13  
LINK        MG    MG A2009                 O   HOH A4012     1555   1555  2.04  
LINK        MG    MG A2009                 O   HOH A4011     1555   1555  2.33  
LINK         O4  NAG A3070                 C1  NAG A3071     1555   1555  1.42  
LINK         O4  NAG A3071                 C1  BMA A3072     1555   1555  1.44  
LINK         O6  BMA A3072                 C1  MAN A3073     1555   1555  1.44  
LINK         O6  MAN A3073                 C1  MAN A3074     1555   1555  1.44  
LINK         O4  NAG A3373                 C1  NAG A3374     1555   1555  1.45  
LINK         O4  NAG A3374                 C1  BMA A3375     1555   1555  1.43  
LINK         O3  BMA A3375                 C1  MAN A3380     1555   1555  1.45  
LINK         O6  BMA A3375                 C1  MAN A3376     1555   1555  1.47  
LINK         O3  MAN A3376                 C1  MAN A3379     1555   1555  1.45  
LINK         O6  MAN A3376                 C1  MAN A3377     1555   1555  1.42  
LINK         O2  MAN A3377                 C1  MAN A3378     1555   1555  1.44  
LINK         O2  MAN A3380                 C1  MAN A3381     1555   1555  1.45  
LINK         O6  MAN A3381                 C1  MAN A3382     1555   1555  1.45  
LINK         O4  NAG A3716                 C1  NAG A3717     1555   1555  1.44  
LINK         O4  NAG A3717                 C1  BMA A3718     1555   1555  1.45  
LINK         O6  BMA A3718                 C1  MAN A3719     1555   1555  1.45  
LINK         O4  NAG A3880                 C1  NAG A3881     1555   1555  1.43  
LINK         O4  NAG A3881                 C1  BMA A3882     1555   1555  1.44  
LINK         O4  NAG B3094                 C1  NAG B3095     1555   1555  1.45  
LINK        CA    CA C2005                 O   HOH C4003     1555   1555  2.43  
LINK        CA    CA C2007                 O   HOH C4007     1555   1555  2.45  
LINK         O4  NAG C3070                 C1  NAG C3071     1555   1555  1.44  
LINK         O4  NAG C3071                 C1  BMA C3072     1555   1555  1.43  
LINK         O3  BMA C3072                 C1  MAN C3073     1555   1555  1.44  
LINK         O4  NAG C3373                 C1  NAG C3374     1555   1555  1.44  
LINK         O4  NAG C3374                 C1  BMA C3375     1555   1555  1.46  
LINK         O3  BMA C3375                 C1  MAN C3378     1555   1555  1.42  
LINK         O6  BMA C3375                 C1  MAN C3376     1555   1555  1.44  
LINK         O6  MAN C3376                 C1  MAN C3377     1555   1555  1.45  
LINK         O2  MAN C3377                 C1  MAN C3380     1555   1555  1.44  
LINK         O4  NAG C3716                 C1  NAG C3717     1555   1555  1.43  
LINK         O4  NAG C3717                 C1  BMA C3718     1555   1555  1.44  
LINK         O6  BMA C3718                 C1  MAN C3719     1555   1555  1.45  
LINK         O3  MAN C3719                 C1  MAN C3720     1555   1555  1.45  
LINK         O4  NAG C3880                 C1  NAG C3881     1555   1555  1.45  
LINK         O4  NAG C3881                 C1  BMA C3882     1555   1555  1.45  
LINK         O3  BMA C3882                 C1  MAN C3884     1555   1555  1.45  
LINK         O6  BMA C3882                 C1  MAN C3883     1555   1555  1.45  
LINK        CA    CA E2005                 O   HOH E4001     1555   1555  2.14  
LINK         O4  NAG E3070                 C1  NAG E3071     1555   1555  1.45  
LINK         O4  NAG E3071                 C1  BMA E3072     1555   1555  1.45  
LINK         O3  BMA E3072                 C1  MAN E3073     1555   1555  1.44  
LINK         O6  BMA E3072                 C1  MAN E3074     1555   1555  1.41  
LINK         O6  MAN E3074                 C1  MAN E3075     1555   1555  1.43  
LINK         O4  NAG E3373                 C1  NAG E3374     1555   1555  1.44  
LINK         O4  NAG E3374                 C1  BMA E3375     1555   1555  1.44  
LINK         O3  BMA E3375                 C1  MAN E3380     1555   1555  1.45  
LINK         O4  NAG E3716                 C1  NAG E3717     1555   1555  1.44  
LINK         O4  NAG E3717                 C1  BMA E3718     1555   1555  1.45  
LINK         O6  BMA E3718                 C1  MAN E3719     1555   1555  1.44  
LINK         O4  NAG E3880                 C1  NAG E3881     1555   1555  1.42  
LINK         O4  NAG E3881                 C1  BMA E3882     1555   1555  1.44  
LINK         O3  BMA E3882                 C1  MAN E3883     1555   1555  1.45  
LINK         O6  BMA E3882                 C1  MAN E3884     1555   1555  1.44  
LINK         O4  NAG G3070                 C1  NAG G3071     1555   1555  1.45  
LINK         O4  NAG G3071                 C1  BMA G3072     1555   1555  1.44  
LINK         O3  BMA G3072                 C1  MAN G3073     1555   1555  1.46  
LINK         O6  BMA G3072                 C1  MAN G3074     1555   1555  1.47  
LINK         O4  NAG G3373                 C1  NAG G3374     1555   1555  1.43  
LINK         O4  NAG G3374                 C1  BMA G3375     1555   1555  1.45  
LINK         O3  BMA G3375                 C1  MAN G3376     1555   1555  1.47  
LINK         O6  BMA G3375                 C1  MAN G3379     1555   1555  1.42  
LINK         O2  MAN G3376                 C1  MAN G3377     1555   1555  1.44  
LINK         O6  MAN G3379                 C1  MAN G3380     1555   1555  1.47  
LINK         O4  NAG G3716                 C1  NAG G3717     1555   1555  1.44  
LINK         O4  NAG G3717                 C1  BMA G3718     1555   1555  1.46  
LINK         O6  BMA G3718                 C1  MAN G3719     1555   1555  1.44  
LINK         O4  NAG G3880                 C1  NAG G3881     1555   1555  1.46  
LINK         O4  NAG G3881                 C1  BMA G3882     1555   1555  1.43  
LINK         O3  BMA G3882                 C1  MAN G3883     1555   1555  1.45  
LINK         O2  MAN G3883                 C1  MAN G3884     1555   1555  1.47  
CISPEP   1 LEU A  119    PRO A  120          0        -8.12                     
CISPEP   2 ARG A  164    PRO A  165          0         2.35                     
CISPEP   3 LYS A  288    PRO A  289          0         1.88                     
CISPEP   4 ILE A  609    PRO A  610          0         3.72                     
CISPEP   5 SER B   77    PRO B   78          0        -3.44                     
CISPEP   6 LEU B  155    PRO B  156          0         6.08                     
CISPEP   7 LEU B  587    PRO B  588          0       -10.93                     
CISPEP   8 LEU C  119    PRO C  120          0        -3.58                     
CISPEP   9 ILE C  609    PRO C  610          0         4.49                     
CISPEP  10 SER D   77    PRO D   78          0        -1.61                     
CISPEP  11 LEU D  155    PRO D  156          0        -1.32                     
CISPEP  12 LEU D  587    PRO D  588          0        -0.47                     
CISPEP  13 LEU E  119    PRO E  120          0        -4.99                     
CISPEP  14 ILE E  609    PRO E  610          0        -2.23                     
CISPEP  15 SER F   77    PRO F   78          0        -0.74                     
CISPEP  16 LEU F  155    PRO F  156          0        -5.54                     
CISPEP  17 LEU F  587    PRO F  588          0        -6.55                     
CISPEP  18 LEU G  119    PRO G  120          0        -9.52                     
CISPEP  19 ILE G  609    PRO G  610          0         0.82                     
CISPEP  20 SER H   77    PRO H   78          0        -0.47                     
CISPEP  21 LEU H  155    PRO H  156          0         0.22                     
CISPEP  22 LEU H  587    PRO H  588          0         4.59                     
SITE     1 AC1  5 ASP A 447  ASP A 449  ASP A 451  SER A 453                    
SITE     2 AC1  5 ASP A 455                                                     
SITE     1 AC2  6 ASP A 511  VAL A 512  ASN A 513  ASP A 515                    
SITE     2 AC2  6 LEU A 517  ASP A 519                                          
SITE     1 AC3  5 ASP A 574  THR A 576  ASP A 578  LEU A 580                    
SITE     2 AC3  5 ASP A 582                                                     
SITE     1 AC4  6 SER A 140  SER A 142  ASP A 240  HOH A4008                    
SITE     2 AC4  6 HOH A4011  HOH A4012                                          
SITE     1 AC5  5 SER B 116  MET B 117  ASP B 120  ASP B 242                    
SITE     2 AC5  5 GLU B 325                                                     
SITE     1 AC6  6 ASP C 447  ASP C 449  ASP C 451  SER C 453                    
SITE     2 AC6  6 ASP C 455  HOH C4003                                          
SITE     1 AC7  5 ASP C 511  ASN C 513  ASP C 515  LEU C 517                    
SITE     2 AC7  5 ASP C 519                                                     
SITE     1 AC8  6 ASP C 574  THR C 576  ASP C 578  LEU C 580                    
SITE     2 AC8  6 ASP C 582  HOH C4007                                          
SITE     1 AC9  3 SER D 116  ASP D 120  GLU D 325                               
SITE     1 AD1  6 ASP E 447  ASP E 449  ASP E 451  SER E 453                    
SITE     2 AD1  6 ASP E 455  HOH E4001                                          
SITE     1 AD2  6 ASP E 511  VAL E 512  ASN E 513  ASP E 515                    
SITE     2 AD2  6 LEU E 517  ASP E 519                                          
SITE     1 AD3  5 ASP E 574  THR E 576  ASP E 578  LEU E 580                    
SITE     2 AD3  5 ASP E 582                                                     
SITE     1 AD4  4 SER F 116  ASP F 120  ASP F 242  GLU F 325                    
SITE     1 AD5  5 ASP G 447  ASP G 449  ASP G 451  SER G 453                    
SITE     2 AD5  5 ASP G 455                                                     
SITE     1 AD6  5 ASP G 511  ASN G 513  ASP G 515  LEU G 517                    
SITE     2 AD6  5 ASP G 519                                                     
SITE     1 AD7  6 ASP G 574  THR G 576  ASP G 578  LEU G 580                    
SITE     2 AD7  6 VAL G 581  ASP G 582                                          
SITE     1 AD8  4 SER H 116  ASP H 120  ASP H 242  GLU H 325                    
SITE     1 AD9  2 ASN A  42  NAG A3071                                          
SITE     1 AE1  4 ASN A  42  ASN A  70  NAG A3042  ARG G  12                    
SITE     1 AE2 13 GLN A 129  ASP A 230  ALA A 260  GLY A 261                    
SITE     2 AE2 13 GLY A 319  GLU A 329  PHE A 354  SER A 357                    
SITE     3 AE2 13 ASN A 373  MET A 374  SER A 375  GLN A 376                    
SITE     4 AE2 13 HOH A4007                                                     
SITE     1 AE3  1 ASN A 678                                                     
SITE     1 AE4  4 THR A 657  ASP A 659  ASN A 716  TYR A 741                    
SITE     1 AE5  2 ASN A 880  ASN A 886                                          
SITE     1 AE6  3 ASN A 920  SER A 922  ARG B 643                               
SITE     1 AE7  6 SER A 929  HIS A 930  VAL A 931  ASN A1031                    
SITE     2 AE7  6 PRO G 112  LEU G 115                                          
SITE     1 AE8  3 ALA B  92  ASN B  94  GLN B 390                               
SITE     1 AE9  2 ASN B 232  ARG B 235                                          
SITE     1 AF1  2 PRO B 616  ASN B 620                                          
SITE     1 AF2  1 ASN C  42                                                     
SITE     1 AF3  5 ILE C  38  ALA C  40  ASN C  42  GLN C  43                    
SITE     2 AF3  5 ASN C  70                                                     
SITE     1 AF4  7 GLU C 329  PHE C 354  SER C 357  ASN C 373                    
SITE     2 AF4  7 MET C 374  SER C 375  GLN C 376                               
SITE     1 AF5  2 ARG A 146  ASN C 678                                          
SITE     1 AF6 10 THR C 657  ASP C 659  ASN C 716  THR C 718                    
SITE     2 AF6 10 ARG C 740  TYR C 741  ASP D 501  LYS F  26                    
SITE     3 AF6 10 LEU F  27  ASN F  28                                          
SITE     1 AF7  4 SER C 836  ASN C 880  ARG C 889  LYS C 892                    
SITE     1 AF8  6 TYR C 918  ASN C 920  PHE C 921  SER C 922                    
SITE     2 AF8  6 TRP D 649  VAL D 674                                          
SITE     1 AF9  5 SER C 929  HIS C 930  VAL C 931  ASN C1031                    
SITE     2 AF9  5 LEU E 115                                                     
SITE     1 AG1  3 TYR D 103  PRO D 104  ASN D 232                               
SITE     1 AG2  3 PHE D 617  ASN D 620  ALA D 624                               
SITE     1 AG3  2 ASN E  42  GLU E  96                                          
SITE     1 AG4  5 ILE E  38  ASN E  42  GLN E  43  ASN E  70                    
SITE     2 AG4  5 LYS F 272                                                     
SITE     1 AG5  8 GLU E 329  PHE E 354  SER E 357  PHE E 371                    
SITE     2 AG5  8 ASN E 373  MET E 374  SER E 375  GLN E 376                    
SITE     1 AG6  1 ASN E 678                                                     
SITE     1 AG7  8 GLU D  64  GLN D  66  THR E 657  ASP E 659                    
SITE     2 AG7  8 ASN E 716  PHE E 717  TYR E 741  ASP F 501                    
SITE     1 AG8  3 SER A 836  ASN E 880  THR E 887                               
SITE     1 AG9  5 TYR E 918  ASN E 920  SER E 922  GLU E 925                    
SITE     2 AG9  5 VAL F 674                                                     
SITE     1 AH1  4 SER E 929  HIS E 930  VAL E 931  ASN E1031                    
SITE     1 AH2  1 ASN F  94                                                     
SITE     1 AH3  1 ASN F 190                                                     
SITE     1 AH4  3 PRO F 616  GLY F 618  ASN F 620                               
SITE     1 AH5  2 ASN G  42  NAG G3070                                          
SITE     1 AH6  4 ILE G  38  ASN G  42  ASN G  70  NAG G3042                    
SITE     1 AH7  9 GLU G 329  PHE G 354  SER G 357  PHE G 371                    
SITE     2 AH7  9 ASN G 373  MET G 374  SER G 375  GLN G 376                    
SITE     3 AH7  9 ASN G 378                                                     
SITE     1 AH8  1 ASN G 678                                                     
SITE     1 AH9  6 THR G 657  ASP G 659  ASN G 716  PHE G 717                    
SITE     2 AH9  6 THR G 718  TYR G 741                                          
SITE     1 AI1  3 SER C 836  ASN G 880  LYS G 892                               
SITE     1 AI2  5 TYR G 918  ASN G 920  PHE G 921  ARG H 643                    
SITE     2 AI2  5 VAL H 674                                                     
SITE     1 AI3  7 PRO A 112  GLN A 114  LEU A 115  SER G 929                    
SITE     2 AI3  7 HIS G 930  VAL G 931  ASN G1031                               
SITE     1 AI4  2 ASN H  94  GLN H 390                                          
SITE     1 AI5  1 ASN H 190                                                     
SITE     1 AI6  1 ASN H 232                                                     
SITE     1 AI7  5 ILE A 254  PRO A 255  ASP A 258  PRO H 616                    
SITE     2 AI7  5 ASN H 620                                                     
CRYST1  132.030  163.480  536.650  90.00  90.00  90.00 P 21 21 21   16          
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      0.007574  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006117  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.001863        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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