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Entry: 4XAM
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HEADER    IMMUNE SYSTEM                           15-DEC-14   4XAM              
TITLE     COMPLEMENT COMPONENT C4B                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT C4 BETA CHAIN;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 20-675;                                       
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: COMPLEMENT C4-A ALPHA CHAIN;                               
COMPND   7 CHAIN: C, E;                                                         
COMPND   8 FRAGMENT: UNP RESIDUES 757-1446;                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: COMPLEMENT C4 GAMMA CHAIN;                                 
COMPND  11 CHAIN: D, F;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 1454-1744                                     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BLOOD;                                                       
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 TISSUE: BLOOD;                                                       
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 TISSUE: BLOOD                                                        
KEYWDS    COMPLEMENT COMPONENT C4, ALPHA-2-MACROGLOBULIN FAMILY, IMMUNE SYSTEM  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MORTENSEN,R.T.KIDMOSE,S.V.PETERSEN,A.SZILAGYI,G.R.ANDERSEN          
REVDAT   3   21-APR-21 4XAM    1       COMPND SOURCE DBREF  SEQADV              
REVDAT   2   27-MAY-15 4XAM    1       JRNL                                     
REVDAT   1   06-MAY-15 4XAM    0                                                
JRNL        AUTH   S.MORTENSEN,R.T.KIDMOSE,S.V.PETERSEN,A.SZILAGYI,Z.PROHASZKA, 
JRNL        AUTH 2 G.R.ANDERSEN                                                 
JRNL        TITL   STRUCTURAL BASIS FOR THE FUNCTION OF COMPLEMENT COMPONENT C4 
JRNL        TITL 2 WITHIN THE CLASSICAL AND LECTIN PATHWAYS OF COMPLEMENT.      
JRNL        REF    J IMMUNOL.                    V. 194  5488 2015              
JRNL        REFN                   ESSN 1550-6606                               
JRNL        PMID   25911760                                                     
JRNL        DOI    10.4049/JIMMUNOL.1500087                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1839)                     
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 34849                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.350                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1168                            
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 49.5454 -  8.3882    0.97     4212   153  0.1726 0.1961        
REMARK   3     2  8.3882 -  6.6631    0.98     4197   148  0.2078 0.2653        
REMARK   3     3  6.6631 -  5.8224    0.99     4227   139  0.2295 0.3172        
REMARK   3     4  5.8224 -  5.2907    0.98     4191   146  0.2148 0.2745        
REMARK   3     5  5.2907 -  4.9118    0.98     4195   148  0.2167 0.2956        
REMARK   3     6  4.9118 -  4.6225    0.99     4237   143  0.2176 0.2713        
REMARK   3     7  4.6225 -  4.3911    0.99     4207   150  0.2499 0.3072        
REMARK   3     8  4.3911 -  4.2001    0.99     4215   141  0.3031 0.3940        
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)     : 0.610            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.020           
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      :  0.010          24802                                  
REMARK   3   ANGLE     :  1.427          33676                                  
REMARK   3   CHIRALITY :  0.051           3778                                  
REMARK   3   PLANARITY :  0.006           4384                                  
REMARK   3   DIHEDRAL  : 18.594           9156                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 20:139                               
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0232  -6.8900 -33.9422              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1743 T22:   1.0177                                     
REMARK   3      T33:   1.3513 T12:   0.1915                                     
REMARK   3      T13:   0.2050 T23:   0.0639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6273 L22:   1.4561                                     
REMARK   3      L33:   3.7588 L12:  -1.6503                                     
REMARK   3      L13:   2.4724 L23:  -0.0535                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0335 S12:   0.4958 S13:  -0.0180                       
REMARK   3      S21:  -0.0188 S22:  -0.1907 S23:  -0.7668                       
REMARK   3      S31:   0.2613 S32:   0.5423 S33:   0.0480                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 140:236                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.5666  23.8766 -48.1226              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1491 T22:   0.8691                                     
REMARK   3      T33:   1.1151 T12:  -0.1318                                     
REMARK   3      T13:   0.2156 T23:   0.1514                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8967 L22:   3.7422                                     
REMARK   3      L33:   2.9776 L12:   1.2151                                     
REMARK   3      L13:  -0.2853 L23:  -1.1026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0064 S12:   0.4162 S13:   0.3648                       
REMARK   3      S21:   0.0297 S22:  -0.0201 S23:  -0.7908                       
REMARK   3      S31:  -0.2897 S32:   0.6761 S33:  -0.1250                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 237:361                              
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3626  19.1269 -84.0577              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6244 T22:   1.0370                                     
REMARK   3      T33:   1.0163 T12:   0.0523                                     
REMARK   3      T13:   0.2527 T23:  -0.0503                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4533 L22:   5.9738                                     
REMARK   3      L33:   5.6703 L12:  -0.3413                                     
REMARK   3      L13:   0.8255 L23:   0.8335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4680 S12:   0.6000 S13:  -0.4794                       
REMARK   3      S21:  -0.3404 S22:  -0.1295 S23:  -0.6365                       
REMARK   3      S31:   0.0967 S32:   0.8402 S33:  -0.2184                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 362:468                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1284 -13.2143 -73.1123              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7897 T22:   1.3366                                     
REMARK   3      T33:   1.1015 T12:   0.6334                                     
REMARK   3      T13:   0.1942 T23:  -0.2052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9762 L22:   3.2310                                     
REMARK   3      L33:   1.1595 L12:   0.1503                                     
REMARK   3      L13:   0.9074 L23:  -1.4243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0052 S12:   0.8675 S13:  -0.3561                       
REMARK   3      S21:  -1.0098 S22:  -0.1849 S23:   0.0227                       
REMARK   3      S31:   0.5040 S32:   0.6553 S33:   0.0647                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 469:568                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0535 -17.0048 -49.9363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0558 T22:   0.8038                                     
REMARK   3      T33:   1.3180 T12:   0.4437                                     
REMARK   3      T13:   0.0061 T23:  -0.1738                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3336 L22:   4.1524                                     
REMARK   3      L33:   3.5669 L12:  -0.2054                                     
REMARK   3      L13:  -0.4804 L23:   1.0892                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2362 S12:   0.7251 S13:  -0.6219                       
REMARK   3      S21:  -0.4706 S22:  -0.4908 S23:  -0.0482                       
REMARK   3      S31:   1.0951 S32:  -0.2254 S33:   0.1629                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 569:605 ) OR (CHAIN C AND RESID     
REMARK   3               757:831 )                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -34.7730  22.6584 -52.8269              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0975 T22:   0.6623                                     
REMARK   3      T33:   1.2811 T12:   0.0797                                     
REMARK   3      T13:   0.2434 T23:   0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2017 L22:   0.6122                                     
REMARK   3      L33:   1.2213 L12:   0.2615                                     
REMARK   3      L13:  -0.0058 L23:  -0.5791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1202 S12:   0.0276 S13:   0.5610                       
REMARK   3      S21:  -0.0092 S22:   0.1306 S23:   0.3784                       
REMARK   3      S31:  -0.3034 S32:  -0.1056 S33:  -0.1918                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN C AND RESID 832:934                              
REMARK   3    ORIGIN FOR THE GROUP (A): -37.7062  42.9058 -68.1004              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3231 T22:   0.4456                                     
REMARK   3      T33:   1.0378 T12:   0.1117                                     
REMARK   3      T13:  -0.0389 T23:   0.1008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0731 L22:   5.1168                                     
REMARK   3      L33:   5.2993 L12:   1.7491                                     
REMARK   3      L13:   1.7902 L23:   1.2366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0725 S12:  -0.4864 S13:  -0.1824                       
REMARK   3      S21:  -0.0964 S22:   0.1341 S23:  -0.2381                       
REMARK   3      S31:   0.0757 S32:  -0.2026 S33:  -0.2545                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN C AND (RESID 935:982 OR RESID 1321:1392)         
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3018  44.3013 -51.8058              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9823 T22:   1.3774                                     
REMARK   3      T33:   1.8857 T12:  -0.2216                                     
REMARK   3      T13:  -0.0429 T23:   0.1619                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4026 L22:   2.4309                                     
REMARK   3      L33:   3.7231 L12:  -0.7755                                     
REMARK   3      L13:   0.5369 L23:   0.6034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1618 S12:  -0.4951 S13:   1.2179                       
REMARK   3      S21:   0.4458 S22:   0.0912 S23:  -1.0763                       
REMARK   3      S31:  -0.3052 S32:   0.9914 S33:   0.1227                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN C AND RESID 983:1320                             
REMARK   3    ORIGIN FOR THE GROUP (A):  40.2192   8.4978 -32.2312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7195 T22:   2.2581                                     
REMARK   3      T33:   2.8068 T12:  -0.0356                                     
REMARK   3      T13:   0.0118 T23:   0.4216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2339 L22:   3.0028                                     
REMARK   3      L33:   0.3803 L12:   0.5821                                     
REMARK   3      L13:  -0.0556 L23:   0.6167                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2459 S12:   0.1461 S13:   0.3159                       
REMARK   3      S21:   0.4771 S22:  -0.5175 S23:  -1.8888                       
REMARK   3      S31:  -0.2412 S32:   1.1485 S33:   0.2736                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 1393:1413 ) OR (CHAIN D AND RESID   
REMARK   3               1464:1579 )                                            
REMARK   3    ORIGIN FOR THE GROUP (A): -29.6950  43.6013 -88.2818              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4916 T22:   0.4057                                     
REMARK   3      T33:   0.6854 T12:   0.0025                                     
REMARK   3      T13:  -0.0554 T23:   0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1856 L22:   6.4398                                     
REMARK   3      L33:   6.6334 L12:  -0.4105                                     
REMARK   3      L13:  -2.7706 L23:   0.7020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0991 S12:   0.0881 S13:  -0.0451                       
REMARK   3      S21:  -0.2883 S22:   0.0616 S23:  -0.3102                       
REMARK   3      S31:   0.4029 S32:   0.2731 S33:  -0.1827                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN A AND RESID 606:670                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.9800   1.1165 -53.2229              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8795 T22:   1.3432                                     
REMARK   3      T33:   0.9942 T12:   0.5311                                     
REMARK   3      T13:   0.2274 T23:  -0.2228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2770 L22:   0.1158                                     
REMARK   3      L33:   0.8459 L12:  -0.7335                                     
REMARK   3      L13:   1.9132 L23:  -0.3275                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4074 S12:   0.3215 S13:  -0.0040                       
REMARK   3      S21:  -0.1354 S22:   0.0871 S23:  -0.3782                       
REMARK   3      S31:  -0.2682 S32:   0.4584 S33:   0.8146                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN D AND RESID 1580:1744                            
REMARK   3    ORIGIN FOR THE GROUP (A): -41.1787  76.3721 -60.2732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4187 T22:   1.1330                                     
REMARK   3      T33:   1.0389 T12:   0.2588                                     
REMARK   3      T13:   0.2953 T23:  -0.0560                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4048 L22:   9.2229                                     
REMARK   3      L33:   2.8492 L12:  -2.8812                                     
REMARK   3      L13:   1.3296 L23:   0.9533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0445 S12:  -0.6272 S13:  -0.0063                       
REMARK   3      S21:   0.8635 S22:   0.2362 S23:   0.3691                       
REMARK   3      S31:  -0.1981 S32:  -0.5052 S33:  -0.0823                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN B AND RESID 20:139                               
REMARK   3    ORIGIN FOR THE GROUP (A): -39.8893  11.9677 -22.8264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2688 T22:   0.3385                                     
REMARK   3      T33:   0.8728 T12:   0.1951                                     
REMARK   3      T13:   0.2419 T23:  -0.1225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3059 L22:   5.2772                                     
REMARK   3      L33:   4.9245 L12:  -0.2658                                     
REMARK   3      L13:   1.6221 L23:  -1.1642                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1993 S12:  -0.4166 S13:  -0.1594                       
REMARK   3      S21:   0.3424 S22:   0.0944 S23:   0.3403                       
REMARK   3      S31:   0.0822 S32:  -0.4693 S33:   0.0473                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN B AND RESID 140:236                              
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4056  -7.5904  -0.5505              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5107 T22:   0.9222                                     
REMARK   3      T33:   0.9141 T12:   0.2851                                     
REMARK   3      T13:   0.0235 T23:  -0.0804                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2872 L22:   2.8484                                     
REMARK   3      L33:   5.6695 L12:   0.3063                                     
REMARK   3      L13:   0.3417 L23:  -1.0783                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2325 S12:  -1.1473 S13:   0.3015                       
REMARK   3      S21:  -0.1276 S22:   0.0048 S23:  -0.1485                       
REMARK   3      S31:  -0.5546 S32:   0.2934 S33:   0.1438                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN B AND RESID 237:361                              
REMARK   3    ORIGIN FOR THE GROUP (A): -28.9391 -42.4899   6.0702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9012 T22:   0.9055                                     
REMARK   3      T33:   1.0254 T12:   0.2659                                     
REMARK   3      T13:  -0.0668 T23:   0.2041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9780 L22:   2.7509                                     
REMARK   3      L33:   3.2889 L12:   1.2227                                     
REMARK   3      L13:   1.0736 L23:  -0.0690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6483 S12:  -1.2308 S13:  -0.4792                       
REMARK   3      S21:   0.4371 S22:   0.3643 S23:   0.1274                       
REMARK   3      S31:   0.2070 S32:  -0.3649 S33:   0.2552                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN B AND RESID 362:468                              
REMARK   3    ORIGIN FOR THE GROUP (A): -52.3925 -27.6644 -18.4309              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2519 T22:   0.5469                                     
REMARK   3      T33:   1.0340 T12:  -0.1246                                     
REMARK   3      T13:   0.2227 T23:   0.3396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0025 L22:   2.7117                                     
REMARK   3      L33:   2.3496 L12:   2.0252                                     
REMARK   3      L13:  -0.6098 L23:   0.4723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4857 S12:  -0.1474 S13:   0.0208                       
REMARK   3      S21:   0.4899 S22:  -0.1118 S23:   0.1329                       
REMARK   3      S31:  -0.1016 S32:  -0.0635 S33:   0.1653                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN B AND RESID 469:568                              
REMARK   3    ORIGIN FOR THE GROUP (A): -42.7354 -10.0975 -30.7325              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2167 T22:   0.4482                                     
REMARK   3      T33:   0.9428 T12:   0.0716                                     
REMARK   3      T13:  -0.0327 T23:  -0.0422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9030 L22:   4.2193                                     
REMARK   3      L33:   4.8730 L12:  -1.5760                                     
REMARK   3      L13:   0.9119 L23:  -0.4206                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1850 S12:  -0.0612 S13:  -0.4436                       
REMARK   3      S21:  -0.7028 S22:   0.1023 S23:   0.2890                       
REMARK   3      S31:  -0.0484 S32:   0.1662 S33:  -0.1341                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 569:605 ) OR ( CHAIN E AND RESID    
REMARK   3               757:831)                                               
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2165 -26.7536 -10.0285              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6358 T22:   0.8404                                     
REMARK   3      T33:   0.8503 T12:   0.2384                                     
REMARK   3      T13:   0.1618 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6277 L22:   4.0980                                     
REMARK   3      L33:   3.1247 L12:  -1.2762                                     
REMARK   3      L13:   1.2590 L23:  -2.7887                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5502 S12:  -0.1769 S13:  -0.2736                       
REMARK   3      S21:   0.0371 S22:  -0.0550 S23:   0.0550                       
REMARK   3      S31:   0.4856 S32:   0.6733 S33:  -0.1331                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 832:934                              
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9915 -38.9012  11.7372              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7758 T22:   0.8019                                     
REMARK   3      T33:   1.1744 T12:   0.2749                                     
REMARK   3      T13:  -0.2774 T23:   0.0870                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8568 L22:   6.5824                                     
REMARK   3      L33:   4.4519 L12:  -0.2150                                     
REMARK   3      L13:   0.8117 L23:   2.0408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1792 S12:   0.1246 S13:  -0.2360                       
REMARK   3      S21:  -0.4744 S22:  -0.0412 S23:   0.3427                       
REMARK   3      S31:   0.1320 S32:   0.6048 S33:  -0.2437                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN E AND (RESID 935:982 OR RESID 1321:1392)         
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6537   0.1642  24.1346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6222 T22:   1.7466                                     
REMARK   3      T33:   1.4055 T12:   0.3921                                     
REMARK   3      T13:  -0.1887 T23:  -0.2277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2171 L22:   4.7820                                     
REMARK   3      L33:   4.0596 L12:  -0.2943                                     
REMARK   3      L13:   2.0055 L23:  -1.5233                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7045 S12:  -0.2120 S13:   0.8719                       
REMARK   3      S21:   0.6803 S22:   1.1278 S23:  -0.0980                       
REMARK   3      S31:  -1.1321 S32:  -0.1888 S33:  -0.0911                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 983:1320                             
REMARK   3    ORIGIN FOR THE GROUP (A): -50.5718  34.1759   1.7803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4906 T22:   1.4640                                     
REMARK   3      T33:   1.3073 T12:   0.4898                                     
REMARK   3      T13:   0.1718 T23:  -0.5063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2518 L22:   2.3163                                     
REMARK   3      L33:   2.1428 L12:  -0.8173                                     
REMARK   3      L13:   0.0999 L23:   0.5867                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2294 S12:  -1.2097 S13:   0.6040                       
REMARK   3      S21:   0.0786 S22:  -0.0884 S23:  -0.0336                       
REMARK   3      S31:  -0.4386 S32:  -0.4500 S33:  -0.0982                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 1393:1413 ) OR ( CHAIN F AND        
REMARK   3               RESID 1464:1579)                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6244 -50.2713  23.2714              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7095 T22:   0.8277                                     
REMARK   3      T33:   1.0976 T12:   0.1964                                     
REMARK   3      T13:  -0.0731 T23:   0.2681                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9868 L22:   3.1761                                     
REMARK   3      L33:   7.6440 L12:   1.6700                                     
REMARK   3      L13:  -0.4060 L23:   1.0877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1334 S12:  -1.3294 S13:  -0.7348                       
REMARK   3      S21:  -0.1790 S22:   0.3549 S23:   0.5539                       
REMARK   3      S31:   0.0588 S32:  -0.5995 S33:  -0.2732                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN B AND RESID 606:670                              
REMARK   3    ORIGIN FOR THE GROUP (A): -36.7958  -8.8160 -12.9715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6723 T22:   0.7120                                     
REMARK   3      T33:   1.1867 T12:  -0.0299                                     
REMARK   3      T13:   0.0945 T23:   0.1388                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7854 L22:   7.0023                                     
REMARK   3      L33:   1.3179 L12:  -5.7642                                     
REMARK   3      L13:   1.1088 L23:   0.6309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6863 S12:  -1.3866 S13:   1.0814                       
REMARK   3      S21:   1.6632 S22:   0.4896 S23:  -0.9816                       
REMARK   3      S31:   0.3542 S32:  -0.5847 S33:  -0.6435                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 1580:1744                            
REMARK   3    ORIGIN FOR THE GROUP (A):  28.2202 -33.6013  38.5263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9169 T22:   1.3372                                     
REMARK   3      T33:   1.2325 T12:  -0.0450                                     
REMARK   3      T13:  -0.0576 T23:   0.2962                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7728 L22:   5.4068                                     
REMARK   3      L33:   6.1129 L12:   0.9072                                     
REMARK   3      L13:   1.2707 L23:   0.2529                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5644 S12:   0.3214 S13:   0.2441                       
REMARK   3      S21:  -0.9874 S22:   0.0726 S23:  -0.4536                       
REMARK   3      S31:  -0.5755 S32:   1.3348 S33:   0.2530                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 12                                          
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESID 20:139                    
REMARK   3     SELECTION          : CHAIN B AND RESID 20:139                    
REMARK   3     ATOM PAIRS NUMBER  : 927                                         
REMARK   3     RMSD               : 0.045                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESID 140:236                   
REMARK   3     SELECTION          : CHAIN B AND RESID 140:236                   
REMARK   3     ATOM PAIRS NUMBER  : 796                                         
REMARK   3     RMSD               : 0.045                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESID 237:361                   
REMARK   3     SELECTION          : CHAIN B AND RESID 237:361                   
REMARK   3     ATOM PAIRS NUMBER  : 983                                         
REMARK   3     RMSD               : 0.043                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESID 362:468                   
REMARK   3     SELECTION          : CHAIN B AND RESID 362:468                   
REMARK   3     ATOM PAIRS NUMBER  : 767                                         
REMARK   3     RMSD               : 0.103                                       
REMARK   3   NCS GROUP : 5                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESID 469:568                   
REMARK   3     SELECTION          : CHAIN B AND RESID 469:568                   
REMARK   3     ATOM PAIRS NUMBER  : 791                                         
REMARK   3     RMSD               : 0.050                                       
REMARK   3   NCS GROUP : 6                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESID 569:605 OR RESID         
REMARK   3                          757:831)                                    
REMARK   3     SELECTION          : CHAIN B AND (RESID 569:605 OR RESID         
REMARK   3                          757:831)                                    
REMARK   3     ATOM PAIRS NUMBER  : 899                                         
REMARK   3     RMSD               : 0.044                                       
REMARK   3   NCS GROUP : 7                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESID 832:934                   
REMARK   3     SELECTION          : CHAIN B AND RESID 832:934                   
REMARK   3     ATOM PAIRS NUMBER  : 775                                         
REMARK   3     RMSD               : 0.041                                       
REMARK   3   NCS GROUP : 8                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESID 935:982 OR RESID         
REMARK   3                          1321:1392)                                  
REMARK   3     SELECTION          : CHAIN B AND (RESID 935:982 OR RESID         
REMARK   3                          1321:1392)                                  
REMARK   3     ATOM PAIRS NUMBER  : 940                                         
REMARK   3     RMSD               : 0.032                                       
REMARK   3   NCS GROUP : 9                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESID 983:1320                  
REMARK   3     SELECTION          : CHAIN B AND RESID 983:1320                  
REMARK   3     ATOM PAIRS NUMBER  : 2371                                        
REMARK   3     RMSD               : 0.068                                       
REMARK   3   NCS GROUP : 10                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESID 1393:1579                 
REMARK   3     SELECTION          : CHAIN B AND RESID 1393:1579                 
REMARK   3     ATOM PAIRS NUMBER  : 1075                                        
REMARK   3     RMSD               : 0.045                                       
REMARK   3   NCS GROUP : 11                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESID 606:679                   
REMARK   3     SELECTION          : CHAIN B AND RESID 606:679                   
REMARK   3     ATOM PAIRS NUMBER  : 474                                         
REMARK   3     RMSD               : 0.045                                       
REMARK   3   NCS GROUP : 12                                                     
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND RESID 1580:1750                 
REMARK   3     SELECTION          : CHAIN B AND RESID 1580:1750                 
REMARK   3     ATOM PAIRS NUMBER  : 1331                                        
REMARK   3     RMSD               : 0.036                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4XAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205242.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9840                             
REMARK 200  MONOCHROMATOR                  : SILICON (1 1 1) CHANNEL-CUT        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION NOVEMBER 11, 2013      
REMARK 200  DATA SCALING SOFTWARE          : XSCALE JANUARY 10, 2014            
REMARK 200                                   BUILT=20140307VERSION              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34865                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.542                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 7.040                              
REMARK 200  R MERGE                    (I) : 0.26400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.15                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.560                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4FXK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THIN PLATES                                                  
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE CRYSTALS APPEARED AFTER MIXING C4B   
REMARK 280  AT 4 MG/ML IN 20 MM HEPES PH 7.5, 100 MM SODIUM CHLORIDE WITH       
REMARK 280  100 MM HEPES PH 7.0, 400 MM MAGNESIUM CHLORIDE, 7.5% PEG8000 AND    
REMARK 280  A MICROSEEDING STOCK AT THE VOLUME RATION 1:1:0.5. THE CRYSTALS     
REMARK 280  APPEARED IN 1-2 WEEKS AND REACHED THE FINAL SIZE IN 1 MONTH,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       80.54000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16350 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 67460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16240 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 67440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     LYS A   671                                                      
REMARK 465     GLU A   672                                                      
REMARK 465     LYS A   673                                                      
REMARK 465     THR A   674                                                      
REMARK 465     THR A   675                                                      
REMARK 465     GLY C  1231                                                      
REMARK 465     SER C  1232                                                      
REMARK 465     VAL C  1233                                                      
REMARK 465     THR C  1234                                                      
REMARK 465     GLY C  1235                                                      
REMARK 465     SER C  1236                                                      
REMARK 465     GLN C  1237                                                      
REMARK 465     SER C  1238                                                      
REMARK 465     ASN C  1239                                                      
REMARK 465     ALA C  1240                                                      
REMARK 465     VAL C  1241                                                      
REMARK 465     SER C  1242                                                      
REMARK 465     PRO C  1243                                                      
REMARK 465     THR C  1244                                                      
REMARK 465     PRO C  1245                                                      
REMARK 465     ALA C  1246                                                      
REMARK 465     PRO C  1247                                                      
REMARK 465     ARG C  1248                                                      
REMARK 465     ASN C  1249                                                      
REMARK 465     PRO C  1250                                                      
REMARK 465     SER C  1251                                                      
REMARK 465     ASP C  1252                                                      
REMARK 465     PRO C  1253                                                      
REMARK 465     MET C  1254                                                      
REMARK 465     PRO C  1255                                                      
REMARK 465     ASN C  1414                                                      
REMARK 465     GLU C  1415                                                      
REMARK 465     ASP C  1416                                                      
REMARK 465     TYR C  1417                                                      
REMARK 465     GLU C  1418                                                      
REMARK 465     ASP C  1419                                                      
REMARK 465     TYR C  1420                                                      
REMARK 465     GLU C  1421                                                      
REMARK 465     TYR C  1422                                                      
REMARK 465     ASP C  1423                                                      
REMARK 465     GLU C  1424                                                      
REMARK 465     LEU C  1425                                                      
REMARK 465     PRO C  1426                                                      
REMARK 465     ALA C  1427                                                      
REMARK 465     LYS C  1428                                                      
REMARK 465     ASP C  1429                                                      
REMARK 465     ASP C  1430                                                      
REMARK 465     PRO C  1431                                                      
REMARK 465     ASP C  1432                                                      
REMARK 465     ALA C  1433                                                      
REMARK 465     PRO C  1434                                                      
REMARK 465     LEU C  1435                                                      
REMARK 465     GLN C  1436                                                      
REMARK 465     PRO C  1437                                                      
REMARK 465     VAL C  1438                                                      
REMARK 465     THR C  1439                                                      
REMARK 465     PRO C  1440                                                      
REMARK 465     LEU C  1441                                                      
REMARK 465     GLN C  1442                                                      
REMARK 465     LEU C  1443                                                      
REMARK 465     PHE C  1444                                                      
REMARK 465     GLU C  1445                                                      
REMARK 465     GLY C  1446                                                      
REMARK 465     GLU D  1454                                                      
REMARK 465     ALA D  1455                                                      
REMARK 465     PRO D  1456                                                      
REMARK 465     LYS D  1457                                                      
REMARK 465     VAL D  1458                                                      
REMARK 465     VAL D  1459                                                      
REMARK 465     GLU D  1460                                                      
REMARK 465     GLU D  1461                                                      
REMARK 465     GLN D  1462                                                      
REMARK 465     GLU D  1463                                                      
REMARK 465     LYS B   671                                                      
REMARK 465     GLU B   672                                                      
REMARK 465     LYS B   673                                                      
REMARK 465     THR B   674                                                      
REMARK 465     THR B   675                                                      
REMARK 465     GLY E  1231                                                      
REMARK 465     SER E  1232                                                      
REMARK 465     VAL E  1233                                                      
REMARK 465     THR E  1234                                                      
REMARK 465     GLY E  1235                                                      
REMARK 465     SER E  1236                                                      
REMARK 465     GLN E  1237                                                      
REMARK 465     SER E  1238                                                      
REMARK 465     ASN E  1239                                                      
REMARK 465     ALA E  1240                                                      
REMARK 465     VAL E  1241                                                      
REMARK 465     SER E  1242                                                      
REMARK 465     PRO E  1243                                                      
REMARK 465     THR E  1244                                                      
REMARK 465     PRO E  1245                                                      
REMARK 465     ALA E  1246                                                      
REMARK 465     PRO E  1247                                                      
REMARK 465     ARG E  1248                                                      
REMARK 465     ASN E  1249                                                      
REMARK 465     PRO E  1250                                                      
REMARK 465     SER E  1251                                                      
REMARK 465     ASP E  1252                                                      
REMARK 465     PRO E  1253                                                      
REMARK 465     MET E  1254                                                      
REMARK 465     PRO E  1255                                                      
REMARK 465     ASN E  1414                                                      
REMARK 465     GLU E  1415                                                      
REMARK 465     ASP E  1416                                                      
REMARK 465     TYR E  1417                                                      
REMARK 465     GLU E  1418                                                      
REMARK 465     ASP E  1419                                                      
REMARK 465     TYR E  1420                                                      
REMARK 465     GLU E  1421                                                      
REMARK 465     TYR E  1422                                                      
REMARK 465     ASP E  1423                                                      
REMARK 465     GLU E  1424                                                      
REMARK 465     LEU E  1425                                                      
REMARK 465     PRO E  1426                                                      
REMARK 465     ALA E  1427                                                      
REMARK 465     LYS E  1428                                                      
REMARK 465     ASP E  1429                                                      
REMARK 465     ASP E  1430                                                      
REMARK 465     PRO E  1431                                                      
REMARK 465     ASP E  1432                                                      
REMARK 465     ALA E  1433                                                      
REMARK 465     PRO E  1434                                                      
REMARK 465     LEU E  1435                                                      
REMARK 465     GLN E  1436                                                      
REMARK 465     PRO E  1437                                                      
REMARK 465     VAL E  1438                                                      
REMARK 465     THR E  1439                                                      
REMARK 465     PRO E  1440                                                      
REMARK 465     LEU E  1441                                                      
REMARK 465     GLN E  1442                                                      
REMARK 465     LEU E  1443                                                      
REMARK 465     PHE E  1444                                                      
REMARK 465     GLU E  1445                                                      
REMARK 465     GLY E  1446                                                      
REMARK 465     GLU F  1454                                                      
REMARK 465     ALA F  1455                                                      
REMARK 465     PRO F  1456                                                      
REMARK 465     LYS F  1457                                                      
REMARK 465     VAL F  1458                                                      
REMARK 465     VAL F  1459                                                      
REMARK 465     GLU F  1460                                                      
REMARK 465     GLU F  1461                                                      
REMARK 465     GLN F  1462                                                      
REMARK 465     GLU F  1463                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER E  1301     OG1  THR E  1305              2.05            
REMARK 500   O    SER C  1301     OG1  THR C  1305              2.05            
REMARK 500   O    ARG E  1008     OG1  THR E  1014              2.10            
REMARK 500   OG1  THR D  1692     O    GLN D  1700              2.10            
REMARK 500   O    ARG C  1008     OG1  THR C  1014              2.12            
REMARK 500   OG1  THR F  1692     O    GLN F  1700              2.13            
REMARK 500   O    TYR E  1027     OG1  THR E  1031              2.14            
REMARK 500   O    ILE C  1317     OG1  THR C  1321              2.14            
REMARK 500   NH2  ARG B   138     OD2  ASP B   221              2.15            
REMARK 500   N    SER B   136     OE1  GLU B   224              2.16            
REMARK 500   OD1  ASP B    81     OH   TYR B   506              2.16            
REMARK 500   O    TYR C  1027     OG1  THR C  1031              2.17            
REMARK 500   O    PRO B   205     OG   SER B   208              2.18            
REMARK 500   O    LEU C  1083     OG   SER C  1087              2.19            
REMARK 500   O    LEU E  1083     OG   SER E  1087              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   OD1  ASN C  1135     N    LYS B    20     1655     2.07            
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    GLN C1092   CD    GLN C1092   NE2    -0.152                       
REMARK 500    GLN E1092   CD    GLN E1092   NE2    -0.156                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  47   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    PRO A  61   C   -  N   -  CA  ANGL. DEV. = -11.3 DEGREES          
REMARK 500    LEU A 338   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    PRO D1530   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    LEU B  24   CB  -  CG  -  CD1 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    PRO B  47   C   -  N   -  CA  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    PRO B  61   C   -  N   -  CA  ANGL. DEV. = -12.5 DEGREES          
REMARK 500    LEU B 338   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    PRO F1530   C   -  N   -  CA  ANGL. DEV. =   9.6 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  27      146.97   -176.56                                   
REMARK 500    PRO A  36     -179.49    -64.70                                   
REMARK 500    ARG A  63      -82.77    -56.18                                   
REMARK 500    ASN A  65       -1.45     89.46                                   
REMARK 500    ARG A 104     -124.60     50.76                                   
REMARK 500    SER A 120      -78.12   -122.19                                   
REMARK 500    PRO A 152       96.26    -69.81                                   
REMARK 500    SER A 196       -4.71     73.42                                   
REMARK 500    ASP A 290     -168.65    -76.05                                   
REMARK 500    LEU A 299       -6.24     81.75                                   
REMARK 500    PHE A 319      -70.65    -56.16                                   
REMARK 500    LEU A 336      161.72    176.68                                   
REMARK 500    ARG A 337      167.62    177.07                                   
REMARK 500    MET A 352      164.24    171.61                                   
REMARK 500    SER A 364      -68.49    -91.74                                   
REMARK 500    HIS A 377       -5.28     72.22                                   
REMARK 500    LEU A 378     -159.70     56.37                                   
REMARK 500    VAL A 379       79.67   -154.67                                   
REMARK 500    ARG A 391     -111.90     52.25                                   
REMARK 500    ALA A 398       75.48     61.73                                   
REMARK 500    LEU A 526       73.58     57.78                                   
REMARK 500    ALA A 564     -169.57   -164.91                                   
REMARK 500    LYS A 579     -147.55     55.68                                   
REMARK 500    GLN A 580       64.80     38.73                                   
REMARK 500    ARG A 582      -79.65    -86.88                                   
REMARK 500    ARG A 666     -136.79     42.13                                   
REMARK 500    GLU C 764      -72.27    -85.65                                   
REMARK 500    LEU C 766      -70.25   -132.27                                   
REMARK 500    GLU C 769      -19.59     75.51                                   
REMARK 500    ARG C 791      -30.46     59.34                                   
REMARK 500    THR C 804     -168.33   -165.27                                   
REMARK 500    THR C 816      -75.01    -80.01                                   
REMARK 500    GLU C 832      -23.50     74.97                                   
REMARK 500    ARG C 852       65.75   -118.32                                   
REMARK 500    ALA C 878     -126.20     50.49                                   
REMARK 500    PRO C 890     -179.35    -63.97                                   
REMARK 500    THR C 904     -169.62   -125.76                                   
REMARK 500    ALA C 905     -146.42     53.06                                   
REMARK 500    ALA C 907     -122.09     52.37                                   
REMARK 500    PHE C 921       73.18   -116.44                                   
REMARK 500    ARG C 956      -67.86   -130.68                                   
REMARK 500    ILE C 969       65.85   -117.37                                   
REMARK 500    ASN C 975       73.30     59.34                                   
REMARK 500    ALA C 994     -178.59    -69.71                                   
REMARK 500    LEU C 995      -85.06   -112.97                                   
REMARK 500    SER C 996       77.59   -152.48                                   
REMARK 500    LEU C1004      -67.33   -135.29                                   
REMARK 500    ARG C1005     -145.98     50.46                                   
REMARK 500    ALA C1062      -72.95    -53.76                                   
REMARK 500    GLU C1091      -71.60    -77.09                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     163 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 PRO A   47     ARG A   48                 -146.59                    
REMARK 500 GLU A  351     MET A  352                  142.96                    
REMARK 500 LEU A  596     ALA A  597                 -147.74                    
REMARK 500 ILE C  969     PRO C  970                  148.85                    
REMARK 500 ALA C 1062     ASP C 1063                  148.79                    
REMARK 500 THR C 1322     GLU C 1323                  142.61                    
REMARK 500 GLU C 1357     LEU C 1358                  134.25                    
REMARK 500 GLN C 1359     PHE C 1360                  149.27                    
REMARK 500 ASP C 1388     MET C 1389                  148.31                    
REMARK 500 TYR C 1409     THR C 1410                  148.40                    
REMARK 500 THR C 1410     MET C 1411                 -143.66                    
REMARK 500 LEU D 1578     LEU D 1579                  -40.03                    
REMARK 500 PRO D 1596     ARG D 1597                  149.20                    
REMARK 500 PRO B   47     ARG B   48                 -144.98                    
REMARK 500 GLU B  351     MET B  352                  142.27                    
REMARK 500 LEU B  596     ALA B  597                 -146.88                    
REMARK 500 ILE E  969     PRO E  970                  148.45                    
REMARK 500 ALA E 1062     ASP E 1063                  149.12                    
REMARK 500 THR E 1322     GLU E 1323                  143.25                    
REMARK 500 GLU E 1357     LEU E 1358                  133.78                    
REMARK 500 GLN E 1359     PHE E 1360                  149.54                    
REMARK 500 ASP E 1388     MET E 1389                  149.08                    
REMARK 500 TYR E 1409     THR E 1410                  148.23                    
REMARK 500 THR E 1410     MET E 1411                 -142.88                    
REMARK 500 LEU F 1578     LEU F 1579                  -40.97                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4XAM A   20   675  UNP    P0C0L4   CO4A_HUMAN      20    675             
DBREF  4XAM C  757  1446  UNP    P0C0L4   CO4A_HUMAN     757   1446             
DBREF  4XAM D 1454  1744  UNP    P0C0L4   CO4A_HUMAN    1454   1744             
DBREF  4XAM B   20   675  UNP    P0C0L4   CO4A_HUMAN      20    675             
DBREF  4XAM E  757  1446  UNP    P0C0L4   CO4A_HUMAN     757   1446             
DBREF  4XAM F 1454  1744  UNP    P0C0L4   CO4A_HUMAN    1454   1744             
SEQADV 4XAM SER C 1201  UNP  P0C0L4    THR  1201 VARIANT                        
SEQADV 4XAM SER E 1201  UNP  P0C0L4    THR  1201 VARIANT                        
SEQRES   1 A  656  LYS PRO ARG LEU LEU LEU PHE SER PRO SER VAL VAL HIS          
SEQRES   2 A  656  LEU GLY VAL PRO LEU SER VAL GLY VAL GLN LEU GLN ASP          
SEQRES   3 A  656  VAL PRO ARG GLY GLN VAL VAL LYS GLY SER VAL PHE LEU          
SEQRES   4 A  656  ARG ASN PRO SER ARG ASN ASN VAL PRO CYS SER PRO LYS          
SEQRES   5 A  656  VAL ASP PHE THR LEU SER SER GLU ARG ASP PHE ALA LEU          
SEQRES   6 A  656  LEU SER LEU GLN VAL PRO LEU LYS ASP ALA LYS SER CYS          
SEQRES   7 A  656  GLY LEU HIS GLN LEU LEU ARG GLY PRO GLU VAL GLN LEU          
SEQRES   8 A  656  VAL ALA HIS SER PRO TRP LEU LYS ASP SER LEU SER ARG          
SEQRES   9 A  656  THR THR ASN ILE GLN GLY ILE ASN LEU LEU PHE SER SER          
SEQRES  10 A  656  ARG ARG GLY HIS LEU PHE LEU GLN THR ASP GLN PRO ILE          
SEQRES  11 A  656  TYR ASN PRO GLY GLN ARG VAL ARG TYR ARG VAL PHE ALA          
SEQRES  12 A  656  LEU ASP GLN LYS MET ARG PRO SER THR ASP THR ILE THR          
SEQRES  13 A  656  VAL MET VAL GLU ASN SER HIS GLY LEU ARG VAL ARG LYS          
SEQRES  14 A  656  LYS GLU VAL TYR MET PRO SER SER ILE PHE GLN ASP ASP          
SEQRES  15 A  656  PHE VAL ILE PRO ASP ILE SER GLU PRO GLY THR TRP LYS          
SEQRES  16 A  656  ILE SER ALA ARG PHE SER ASP GLY LEU GLU SER ASN SER          
SEQRES  17 A  656  SER THR GLN PHE GLU VAL LYS LYS TYR VAL LEU PRO ASN          
SEQRES  18 A  656  PHE GLU VAL LYS ILE THR PRO GLY LYS PRO TYR ILE LEU          
SEQRES  19 A  656  THR VAL PRO GLY HIS LEU ASP GLU MET GLN LEU ASP ILE          
SEQRES  20 A  656  GLN ALA ARG TYR ILE TYR GLY LYS PRO VAL GLN GLY VAL          
SEQRES  21 A  656  ALA TYR VAL ARG PHE GLY LEU LEU ASP GLU ASP GLY LYS          
SEQRES  22 A  656  LYS THR PHE PHE ARG GLY LEU GLU SER GLN THR LYS LEU          
SEQRES  23 A  656  VAL ASN GLY GLN SER HIS ILE SER LEU SER LYS ALA GLU          
SEQRES  24 A  656  PHE GLN ASP ALA LEU GLU LYS LEU ASN MET GLY ILE THR          
SEQRES  25 A  656  ASP LEU GLN GLY LEU ARG LEU TYR VAL ALA ALA ALA ILE          
SEQRES  26 A  656  ILE GLU SER PRO GLY GLY GLU MET GLU GLU ALA GLU LEU          
SEQRES  27 A  656  THR SER TRP TYR PHE VAL SER SER PRO PHE SER LEU ASP          
SEQRES  28 A  656  LEU SER LYS THR LYS ARG HIS LEU VAL PRO GLY ALA PRO          
SEQRES  29 A  656  PHE LEU LEU GLN ALA LEU VAL ARG GLU MET SER GLY SER          
SEQRES  30 A  656  PRO ALA SER GLY ILE PRO VAL LYS VAL SER ALA THR VAL          
SEQRES  31 A  656  SER SER PRO GLY SER VAL PRO GLU VAL GLN ASP ILE GLN          
SEQRES  32 A  656  GLN ASN THR ASP GLY SER GLY GLN VAL SER ILE PRO ILE          
SEQRES  33 A  656  ILE ILE PRO GLN THR ILE SER GLU LEU GLN LEU SER VAL          
SEQRES  34 A  656  SER ALA GLY SER PRO HIS PRO ALA ILE ALA ARG LEU THR          
SEQRES  35 A  656  VAL ALA ALA PRO PRO SER GLY GLY PRO GLY PHE LEU SER          
SEQRES  36 A  656  ILE GLU ARG PRO ASP SER ARG PRO PRO ARG VAL GLY ASP          
SEQRES  37 A  656  THR LEU ASN LEU ASN LEU ARG ALA VAL GLY SER GLY ALA          
SEQRES  38 A  656  THR PHE SER HIS TYR TYR TYR MET ILE LEU SER ARG GLY          
SEQRES  39 A  656  GLN ILE VAL PHE MET ASN ARG GLU PRO LYS ARG THR LEU          
SEQRES  40 A  656  THR SER VAL SER VAL PHE VAL ASP HIS HIS LEU ALA PRO          
SEQRES  41 A  656  SER PHE TYR PHE VAL ALA PHE TYR TYR HIS GLY ASP HIS          
SEQRES  42 A  656  PRO VAL ALA ASN SER LEU ARG VAL ASP VAL GLN ALA GLY          
SEQRES  43 A  656  ALA CYS GLU GLY LYS LEU GLU LEU SER VAL ASP GLY ALA          
SEQRES  44 A  656  LYS GLN TYR ARG ASN GLY GLU SER VAL LYS LEU HIS LEU          
SEQRES  45 A  656  GLU THR ASP SER LEU ALA LEU VAL ALA LEU GLY ALA LEU          
SEQRES  46 A  656  ASP THR ALA LEU TYR ALA ALA GLY SER LYS SER HIS LYS          
SEQRES  47 A  656  PRO LEU ASN MET GLY LYS VAL PHE GLU ALA MET ASN SER          
SEQRES  48 A  656  TYR ASP LEU GLY CYS GLY PRO GLY GLY GLY ASP SER ALA          
SEQRES  49 A  656  LEU GLN VAL PHE GLN ALA ALA GLY LEU ALA PHE SER ASP          
SEQRES  50 A  656  GLY ASP GLN TRP THR LEU SER ARG LYS ARG LEU SER CYS          
SEQRES  51 A  656  PRO LYS GLU LYS THR THR                                      
SEQRES   1 C  690  ALA LEU GLU ILE LEU GLN GLU GLU ASP LEU ILE ASP GLU          
SEQRES   2 C  690  ASP ASP ILE PRO VAL ARG SER PHE PHE PRO GLU ASN TRP          
SEQRES   3 C  690  LEU TRP ARG VAL GLU THR VAL ASP ARG PHE GLN ILE LEU          
SEQRES   4 C  690  THR LEU TRP LEU PRO ASP SER LEU THR THR TRP GLU ILE          
SEQRES   5 C  690  HIS GLY LEU SER LEU SER LYS THR LYS GLY LEU CYS VAL          
SEQRES   6 C  690  ALA THR PRO VAL GLN LEU ARG VAL PHE ARG GLU PHE HIS          
SEQRES   7 C  690  LEU HIS LEU ARG LEU PRO MET SER VAL ARG ARG PHE GLU          
SEQRES   8 C  690  GLN LEU GLU LEU ARG PRO VAL LEU TYR ASN TYR LEU ASP          
SEQRES   9 C  690  LYS ASN LEU THR VAL SER VAL HIS VAL SER PRO VAL GLU          
SEQRES  10 C  690  GLY LEU CYS LEU ALA GLY GLY GLY GLY LEU ALA GLN GLN          
SEQRES  11 C  690  VAL LEU VAL PRO ALA GLY SER ALA ARG PRO VAL ALA PHE          
SEQRES  12 C  690  SER VAL VAL PRO THR ALA ALA ALA ALA VAL SER LEU LYS          
SEQRES  13 C  690  VAL VAL ALA ARG GLY SER PHE GLU PHE PRO VAL GLY ASP          
SEQRES  14 C  690  ALA VAL SER LYS VAL LEU GLN ILE GLU LYS GLU GLY ALA          
SEQRES  15 C  690  ILE HIS ARG GLU GLU LEU VAL TYR GLU LEU ASN PRO LEU          
SEQRES  16 C  690  ASP HIS ARG GLY ARG THR LEU GLU ILE PRO GLY ASN SER          
SEQRES  17 C  690  ASP PRO ASN MET ILE PRO ASP GLY ASP PHE ASN SER TYR          
SEQRES  18 C  690  VAL ARG VAL THR ALA SER ASP PRO LEU ASP THR LEU GLY          
SEQRES  19 C  690  SER GLU GLY ALA LEU SER PRO GLY GLY VAL ALA SER LEU          
SEQRES  20 C  690  LEU ARG LEU PRO ARG GLY CYS GLY GLU GLN THR MET ILE          
SEQRES  21 C  690  TYR LEU ALA PRO THR LEU ALA ALA SER ARG TYR LEU ASP          
SEQRES  22 C  690  LYS THR GLU GLN TRP SER THR LEU PRO PRO GLU THR LYS          
SEQRES  23 C  690  ASP HIS ALA VAL ASP LEU ILE GLN LYS GLY TYR MET ARG          
SEQRES  24 C  690  ILE GLN GLN PHE ARG LYS ALA ASP GLY SER TYR ALA ALA          
SEQRES  25 C  690  TRP LEU SER ARG ASP SER SER THR TRP LEU THR ALA PHE          
SEQRES  26 C  690  VAL LEU LYS VAL LEU SER LEU ALA GLN GLU GLN VAL GLY          
SEQRES  27 C  690  GLY SER PRO GLU LYS LEU GLN GLU THR SER ASN TRP LEU          
SEQRES  28 C  690  LEU SER GLN GLN GLN ALA ASP GLY SER PHE GLN ASP PRO          
SEQRES  29 C  690  CYS PRO VAL LEU ASP ARG SER MET GLN GLY GLY LEU VAL          
SEQRES  30 C  690  GLY ASN ASP GLU THR VAL ALA LEU THR ALA PHE VAL THR          
SEQRES  31 C  690  ILE ALA LEU HIS HIS GLY LEU ALA VAL PHE GLN ASP GLU          
SEQRES  32 C  690  GLY ALA GLU PRO LEU LYS GLN ARG VAL GLU ALA SER ILE          
SEQRES  33 C  690  SER LYS ALA ASN SER PHE LEU GLY GLU LYS ALA SER ALA          
SEQRES  34 C  690  GLY LEU LEU GLY ALA HIS ALA ALA ALA ILE THR ALA TYR          
SEQRES  35 C  690  ALA LEU SER LEU THR LYS ALA PRO VAL ASP LEU LEU GLY          
SEQRES  36 C  690  VAL ALA HIS ASN ASN LEU MET ALA MET ALA GLN GLU THR          
SEQRES  37 C  690  GLY ASP ASN LEU TYR TRP GLY SER VAL THR GLY SER GLN          
SEQRES  38 C  690  SER ASN ALA VAL SER PRO THR PRO ALA PRO ARG ASN PRO          
SEQRES  39 C  690  SER ASP PRO MET PRO GLN ALA PRO ALA LEU TRP ILE GLU          
SEQRES  40 C  690  THR THR ALA TYR ALA LEU LEU HIS LEU LEU LEU HIS GLU          
SEQRES  41 C  690  GLY LYS ALA GLU MET ALA ASP GLN ALA SER ALA TRP LEU          
SEQRES  42 C  690  THR ARG GLN GLY SER PHE GLN GLY GLY PHE ARG SER THR          
SEQRES  43 C  690  GLN ASP THR VAL ILE ALA LEU ASP ALA LEU SER ALA TYR          
SEQRES  44 C  690  TRP ILE ALA SER HIS THR THR GLU GLU ARG GLY LEU ASN          
SEQRES  45 C  690  VAL THR LEU SER SER THR GLY ARG ASN GLY PHE LYS SER          
SEQRES  46 C  690  HIS ALA LEU GLN LEU ASN ASN ARG GLN ILE ARG GLY LEU          
SEQRES  47 C  690  GLU GLU GLU LEU GLN PHE SER LEU GLY SER LYS ILE ASN          
SEQRES  48 C  690  VAL LYS VAL GLY GLY ASN SER LYS GLY THR LEU LYS VAL          
SEQRES  49 C  690  LEU ARG THR TYR ASN VAL LEU ASP MET LYS ASN THR THR          
SEQRES  50 C  690  CYS GLN ASP LEU GLN ILE GLU VAL THR VAL LYS GLY HIS          
SEQRES  51 C  690  VAL GLU TYR THR MET GLU ALA ASN GLU ASP TYR GLU ASP          
SEQRES  52 C  690  TYR GLU TYR ASP GLU LEU PRO ALA LYS ASP ASP PRO ASP          
SEQRES  53 C  690  ALA PRO LEU GLN PRO VAL THR PRO LEU GLN LEU PHE GLU          
SEQRES  54 C  690  GLY                                                          
SEQRES   1 D  291  GLU ALA PRO LYS VAL VAL GLU GLU GLN GLU SER ARG VAL          
SEQRES   2 D  291  HIS TYR THR VAL CYS ILE TRP ARG ASN GLY LYS VAL GLY          
SEQRES   3 D  291  LEU SER GLY MET ALA ILE ALA ASP VAL THR LEU LEU SER          
SEQRES   4 D  291  GLY PHE HIS ALA LEU ARG ALA ASP LEU GLU LYS LEU THR          
SEQRES   5 D  291  SER LEU SER ASP ARG TYR VAL SER HIS PHE GLU THR GLU          
SEQRES   6 D  291  GLY PRO HIS VAL LEU LEU TYR PHE ASP SER VAL PRO THR          
SEQRES   7 D  291  SER ARG GLU CYS VAL GLY PHE GLU ALA VAL GLN GLU VAL          
SEQRES   8 D  291  PRO VAL GLY LEU VAL GLN PRO ALA SER ALA THR LEU TYR          
SEQRES   9 D  291  ASP TYR TYR ASN PRO GLU ARG ARG CYS SER VAL PHE TYR          
SEQRES  10 D  291  GLY ALA PRO SER LYS SER ARG LEU LEU ALA THR LEU CYS          
SEQRES  11 D  291  SER ALA GLU VAL CYS GLN CYS ALA GLU GLY LYS CYS PRO          
SEQRES  12 D  291  ARG GLN ARG ARG ALA LEU GLU ARG GLY LEU GLN ASP GLU          
SEQRES  13 D  291  ASP GLY TYR ARG MET LYS PHE ALA CYS TYR TYR PRO ARG          
SEQRES  14 D  291  VAL GLU TYR GLY PHE GLN VAL LYS VAL LEU ARG GLU ASP          
SEQRES  15 D  291  SER ARG ALA ALA PHE ARG LEU PHE GLU THR LYS ILE THR          
SEQRES  16 D  291  GLN VAL LEU HIS PHE THR LYS ASP VAL LYS ALA ALA ALA          
SEQRES  17 D  291  ASN GLN MET ARG ASN PHE LEU VAL ARG ALA SER CYS ARG          
SEQRES  18 D  291  LEU ARG LEU GLU PRO GLY LYS GLU TYR LEU ILE MET GLY          
SEQRES  19 D  291  LEU ASP GLY ALA THR TYR ASP LEU GLU GLY HIS PRO GLN          
SEQRES  20 D  291  TYR LEU LEU ASP SER ASN SER TRP ILE GLU GLU MET PRO          
SEQRES  21 D  291  SER GLU ARG LEU CYS ARG SER THR ARG GLN ARG ALA ALA          
SEQRES  22 D  291  CYS ALA GLN LEU ASN ASP PHE LEU GLN GLU TYR GLY THR          
SEQRES  23 D  291  GLN GLY CYS GLN VAL                                          
SEQRES   1 B  656  LYS PRO ARG LEU LEU LEU PHE SER PRO SER VAL VAL HIS          
SEQRES   2 B  656  LEU GLY VAL PRO LEU SER VAL GLY VAL GLN LEU GLN ASP          
SEQRES   3 B  656  VAL PRO ARG GLY GLN VAL VAL LYS GLY SER VAL PHE LEU          
SEQRES   4 B  656  ARG ASN PRO SER ARG ASN ASN VAL PRO CYS SER PRO LYS          
SEQRES   5 B  656  VAL ASP PHE THR LEU SER SER GLU ARG ASP PHE ALA LEU          
SEQRES   6 B  656  LEU SER LEU GLN VAL PRO LEU LYS ASP ALA LYS SER CYS          
SEQRES   7 B  656  GLY LEU HIS GLN LEU LEU ARG GLY PRO GLU VAL GLN LEU          
SEQRES   8 B  656  VAL ALA HIS SER PRO TRP LEU LYS ASP SER LEU SER ARG          
SEQRES   9 B  656  THR THR ASN ILE GLN GLY ILE ASN LEU LEU PHE SER SER          
SEQRES  10 B  656  ARG ARG GLY HIS LEU PHE LEU GLN THR ASP GLN PRO ILE          
SEQRES  11 B  656  TYR ASN PRO GLY GLN ARG VAL ARG TYR ARG VAL PHE ALA          
SEQRES  12 B  656  LEU ASP GLN LYS MET ARG PRO SER THR ASP THR ILE THR          
SEQRES  13 B  656  VAL MET VAL GLU ASN SER HIS GLY LEU ARG VAL ARG LYS          
SEQRES  14 B  656  LYS GLU VAL TYR MET PRO SER SER ILE PHE GLN ASP ASP          
SEQRES  15 B  656  PHE VAL ILE PRO ASP ILE SER GLU PRO GLY THR TRP LYS          
SEQRES  16 B  656  ILE SER ALA ARG PHE SER ASP GLY LEU GLU SER ASN SER          
SEQRES  17 B  656  SER THR GLN PHE GLU VAL LYS LYS TYR VAL LEU PRO ASN          
SEQRES  18 B  656  PHE GLU VAL LYS ILE THR PRO GLY LYS PRO TYR ILE LEU          
SEQRES  19 B  656  THR VAL PRO GLY HIS LEU ASP GLU MET GLN LEU ASP ILE          
SEQRES  20 B  656  GLN ALA ARG TYR ILE TYR GLY LYS PRO VAL GLN GLY VAL          
SEQRES  21 B  656  ALA TYR VAL ARG PHE GLY LEU LEU ASP GLU ASP GLY LYS          
SEQRES  22 B  656  LYS THR PHE PHE ARG GLY LEU GLU SER GLN THR LYS LEU          
SEQRES  23 B  656  VAL ASN GLY GLN SER HIS ILE SER LEU SER LYS ALA GLU          
SEQRES  24 B  656  PHE GLN ASP ALA LEU GLU LYS LEU ASN MET GLY ILE THR          
SEQRES  25 B  656  ASP LEU GLN GLY LEU ARG LEU TYR VAL ALA ALA ALA ILE          
SEQRES  26 B  656  ILE GLU SER PRO GLY GLY GLU MET GLU GLU ALA GLU LEU          
SEQRES  27 B  656  THR SER TRP TYR PHE VAL SER SER PRO PHE SER LEU ASP          
SEQRES  28 B  656  LEU SER LYS THR LYS ARG HIS LEU VAL PRO GLY ALA PRO          
SEQRES  29 B  656  PHE LEU LEU GLN ALA LEU VAL ARG GLU MET SER GLY SER          
SEQRES  30 B  656  PRO ALA SER GLY ILE PRO VAL LYS VAL SER ALA THR VAL          
SEQRES  31 B  656  SER SER PRO GLY SER VAL PRO GLU VAL GLN ASP ILE GLN          
SEQRES  32 B  656  GLN ASN THR ASP GLY SER GLY GLN VAL SER ILE PRO ILE          
SEQRES  33 B  656  ILE ILE PRO GLN THR ILE SER GLU LEU GLN LEU SER VAL          
SEQRES  34 B  656  SER ALA GLY SER PRO HIS PRO ALA ILE ALA ARG LEU THR          
SEQRES  35 B  656  VAL ALA ALA PRO PRO SER GLY GLY PRO GLY PHE LEU SER          
SEQRES  36 B  656  ILE GLU ARG PRO ASP SER ARG PRO PRO ARG VAL GLY ASP          
SEQRES  37 B  656  THR LEU ASN LEU ASN LEU ARG ALA VAL GLY SER GLY ALA          
SEQRES  38 B  656  THR PHE SER HIS TYR TYR TYR MET ILE LEU SER ARG GLY          
SEQRES  39 B  656  GLN ILE VAL PHE MET ASN ARG GLU PRO LYS ARG THR LEU          
SEQRES  40 B  656  THR SER VAL SER VAL PHE VAL ASP HIS HIS LEU ALA PRO          
SEQRES  41 B  656  SER PHE TYR PHE VAL ALA PHE TYR TYR HIS GLY ASP HIS          
SEQRES  42 B  656  PRO VAL ALA ASN SER LEU ARG VAL ASP VAL GLN ALA GLY          
SEQRES  43 B  656  ALA CYS GLU GLY LYS LEU GLU LEU SER VAL ASP GLY ALA          
SEQRES  44 B  656  LYS GLN TYR ARG ASN GLY GLU SER VAL LYS LEU HIS LEU          
SEQRES  45 B  656  GLU THR ASP SER LEU ALA LEU VAL ALA LEU GLY ALA LEU          
SEQRES  46 B  656  ASP THR ALA LEU TYR ALA ALA GLY SER LYS SER HIS LYS          
SEQRES  47 B  656  PRO LEU ASN MET GLY LYS VAL PHE GLU ALA MET ASN SER          
SEQRES  48 B  656  TYR ASP LEU GLY CYS GLY PRO GLY GLY GLY ASP SER ALA          
SEQRES  49 B  656  LEU GLN VAL PHE GLN ALA ALA GLY LEU ALA PHE SER ASP          
SEQRES  50 B  656  GLY ASP GLN TRP THR LEU SER ARG LYS ARG LEU SER CYS          
SEQRES  51 B  656  PRO LYS GLU LYS THR THR                                      
SEQRES   1 E  690  ALA LEU GLU ILE LEU GLN GLU GLU ASP LEU ILE ASP GLU          
SEQRES   2 E  690  ASP ASP ILE PRO VAL ARG SER PHE PHE PRO GLU ASN TRP          
SEQRES   3 E  690  LEU TRP ARG VAL GLU THR VAL ASP ARG PHE GLN ILE LEU          
SEQRES   4 E  690  THR LEU TRP LEU PRO ASP SER LEU THR THR TRP GLU ILE          
SEQRES   5 E  690  HIS GLY LEU SER LEU SER LYS THR LYS GLY LEU CYS VAL          
SEQRES   6 E  690  ALA THR PRO VAL GLN LEU ARG VAL PHE ARG GLU PHE HIS          
SEQRES   7 E  690  LEU HIS LEU ARG LEU PRO MET SER VAL ARG ARG PHE GLU          
SEQRES   8 E  690  GLN LEU GLU LEU ARG PRO VAL LEU TYR ASN TYR LEU ASP          
SEQRES   9 E  690  LYS ASN LEU THR VAL SER VAL HIS VAL SER PRO VAL GLU          
SEQRES  10 E  690  GLY LEU CYS LEU ALA GLY GLY GLY GLY LEU ALA GLN GLN          
SEQRES  11 E  690  VAL LEU VAL PRO ALA GLY SER ALA ARG PRO VAL ALA PHE          
SEQRES  12 E  690  SER VAL VAL PRO THR ALA ALA ALA ALA VAL SER LEU LYS          
SEQRES  13 E  690  VAL VAL ALA ARG GLY SER PHE GLU PHE PRO VAL GLY ASP          
SEQRES  14 E  690  ALA VAL SER LYS VAL LEU GLN ILE GLU LYS GLU GLY ALA          
SEQRES  15 E  690  ILE HIS ARG GLU GLU LEU VAL TYR GLU LEU ASN PRO LEU          
SEQRES  16 E  690  ASP HIS ARG GLY ARG THR LEU GLU ILE PRO GLY ASN SER          
SEQRES  17 E  690  ASP PRO ASN MET ILE PRO ASP GLY ASP PHE ASN SER TYR          
SEQRES  18 E  690  VAL ARG VAL THR ALA SER ASP PRO LEU ASP THR LEU GLY          
SEQRES  19 E  690  SER GLU GLY ALA LEU SER PRO GLY GLY VAL ALA SER LEU          
SEQRES  20 E  690  LEU ARG LEU PRO ARG GLY CYS GLY GLU GLN THR MET ILE          
SEQRES  21 E  690  TYR LEU ALA PRO THR LEU ALA ALA SER ARG TYR LEU ASP          
SEQRES  22 E  690  LYS THR GLU GLN TRP SER THR LEU PRO PRO GLU THR LYS          
SEQRES  23 E  690  ASP HIS ALA VAL ASP LEU ILE GLN LYS GLY TYR MET ARG          
SEQRES  24 E  690  ILE GLN GLN PHE ARG LYS ALA ASP GLY SER TYR ALA ALA          
SEQRES  25 E  690  TRP LEU SER ARG ASP SER SER THR TRP LEU THR ALA PHE          
SEQRES  26 E  690  VAL LEU LYS VAL LEU SER LEU ALA GLN GLU GLN VAL GLY          
SEQRES  27 E  690  GLY SER PRO GLU LYS LEU GLN GLU THR SER ASN TRP LEU          
SEQRES  28 E  690  LEU SER GLN GLN GLN ALA ASP GLY SER PHE GLN ASP PRO          
SEQRES  29 E  690  CYS PRO VAL LEU ASP ARG SER MET GLN GLY GLY LEU VAL          
SEQRES  30 E  690  GLY ASN ASP GLU THR VAL ALA LEU THR ALA PHE VAL THR          
SEQRES  31 E  690  ILE ALA LEU HIS HIS GLY LEU ALA VAL PHE GLN ASP GLU          
SEQRES  32 E  690  GLY ALA GLU PRO LEU LYS GLN ARG VAL GLU ALA SER ILE          
SEQRES  33 E  690  SER LYS ALA ASN SER PHE LEU GLY GLU LYS ALA SER ALA          
SEQRES  34 E  690  GLY LEU LEU GLY ALA HIS ALA ALA ALA ILE THR ALA TYR          
SEQRES  35 E  690  ALA LEU SER LEU THR LYS ALA PRO VAL ASP LEU LEU GLY          
SEQRES  36 E  690  VAL ALA HIS ASN ASN LEU MET ALA MET ALA GLN GLU THR          
SEQRES  37 E  690  GLY ASP ASN LEU TYR TRP GLY SER VAL THR GLY SER GLN          
SEQRES  38 E  690  SER ASN ALA VAL SER PRO THR PRO ALA PRO ARG ASN PRO          
SEQRES  39 E  690  SER ASP PRO MET PRO GLN ALA PRO ALA LEU TRP ILE GLU          
SEQRES  40 E  690  THR THR ALA TYR ALA LEU LEU HIS LEU LEU LEU HIS GLU          
SEQRES  41 E  690  GLY LYS ALA GLU MET ALA ASP GLN ALA SER ALA TRP LEU          
SEQRES  42 E  690  THR ARG GLN GLY SER PHE GLN GLY GLY PHE ARG SER THR          
SEQRES  43 E  690  GLN ASP THR VAL ILE ALA LEU ASP ALA LEU SER ALA TYR          
SEQRES  44 E  690  TRP ILE ALA SER HIS THR THR GLU GLU ARG GLY LEU ASN          
SEQRES  45 E  690  VAL THR LEU SER SER THR GLY ARG ASN GLY PHE LYS SER          
SEQRES  46 E  690  HIS ALA LEU GLN LEU ASN ASN ARG GLN ILE ARG GLY LEU          
SEQRES  47 E  690  GLU GLU GLU LEU GLN PHE SER LEU GLY SER LYS ILE ASN          
SEQRES  48 E  690  VAL LYS VAL GLY GLY ASN SER LYS GLY THR LEU LYS VAL          
SEQRES  49 E  690  LEU ARG THR TYR ASN VAL LEU ASP MET LYS ASN THR THR          
SEQRES  50 E  690  CYS GLN ASP LEU GLN ILE GLU VAL THR VAL LYS GLY HIS          
SEQRES  51 E  690  VAL GLU TYR THR MET GLU ALA ASN GLU ASP TYR GLU ASP          
SEQRES  52 E  690  TYR GLU TYR ASP GLU LEU PRO ALA LYS ASP ASP PRO ASP          
SEQRES  53 E  690  ALA PRO LEU GLN PRO VAL THR PRO LEU GLN LEU PHE GLU          
SEQRES  54 E  690  GLY                                                          
SEQRES   1 F  291  GLU ALA PRO LYS VAL VAL GLU GLU GLN GLU SER ARG VAL          
SEQRES   2 F  291  HIS TYR THR VAL CYS ILE TRP ARG ASN GLY LYS VAL GLY          
SEQRES   3 F  291  LEU SER GLY MET ALA ILE ALA ASP VAL THR LEU LEU SER          
SEQRES   4 F  291  GLY PHE HIS ALA LEU ARG ALA ASP LEU GLU LYS LEU THR          
SEQRES   5 F  291  SER LEU SER ASP ARG TYR VAL SER HIS PHE GLU THR GLU          
SEQRES   6 F  291  GLY PRO HIS VAL LEU LEU TYR PHE ASP SER VAL PRO THR          
SEQRES   7 F  291  SER ARG GLU CYS VAL GLY PHE GLU ALA VAL GLN GLU VAL          
SEQRES   8 F  291  PRO VAL GLY LEU VAL GLN PRO ALA SER ALA THR LEU TYR          
SEQRES   9 F  291  ASP TYR TYR ASN PRO GLU ARG ARG CYS SER VAL PHE TYR          
SEQRES  10 F  291  GLY ALA PRO SER LYS SER ARG LEU LEU ALA THR LEU CYS          
SEQRES  11 F  291  SER ALA GLU VAL CYS GLN CYS ALA GLU GLY LYS CYS PRO          
SEQRES  12 F  291  ARG GLN ARG ARG ALA LEU GLU ARG GLY LEU GLN ASP GLU          
SEQRES  13 F  291  ASP GLY TYR ARG MET LYS PHE ALA CYS TYR TYR PRO ARG          
SEQRES  14 F  291  VAL GLU TYR GLY PHE GLN VAL LYS VAL LEU ARG GLU ASP          
SEQRES  15 F  291  SER ARG ALA ALA PHE ARG LEU PHE GLU THR LYS ILE THR          
SEQRES  16 F  291  GLN VAL LEU HIS PHE THR LYS ASP VAL LYS ALA ALA ALA          
SEQRES  17 F  291  ASN GLN MET ARG ASN PHE LEU VAL ARG ALA SER CYS ARG          
SEQRES  18 F  291  LEU ARG LEU GLU PRO GLY LYS GLU TYR LEU ILE MET GLY          
SEQRES  19 F  291  LEU ASP GLY ALA THR TYR ASP LEU GLU GLY HIS PRO GLN          
SEQRES  20 F  291  TYR LEU LEU ASP SER ASN SER TRP ILE GLU GLU MET PRO          
SEQRES  21 F  291  SER GLU ARG LEU CYS ARG SER THR ARG GLN ARG ALA ALA          
SEQRES  22 F  291  CYS ALA GLN LEU ASN ASP PHE LEU GLN GLU TYR GLY THR          
SEQRES  23 F  291  GLN GLY CYS GLN VAL                                          
HELIX    1 AA1 PRO A   90  CYS A   97  1                                   8    
HELIX    2 AA2 SER A  315  GLU A  324  1                                  10    
HELIX    3 AA3 GLY A  329  GLY A  335  1                                   7    
HELIX    4 AA4 THR A  606  GLY A  612  1                                   7    
HELIX    5 AA5 ASN A  620  SER A  630  1                                  11    
HELIX    6 AA6 SER A  642  ALA A  650  1                                   9    
HELIX    7 AA7 CYS C 1010  THR C 1031  1                                  22    
HELIX    8 AA8 GLU C 1032  LEU C 1037  5                                   6    
HELIX    9 AA9 PRO C 1038  GLN C 1057  1                                  20    
HELIX   10 AB1 SER C 1075  ALA C 1089  1                                  15    
HELIX   11 AB2 SER C 1096  LEU C 1108  1                                  13    
HELIX   12 AB3 SER C 1109  GLN C 1111  5                                   3    
HELIX   13 AB4 GLY C 1134  GLU C 1137  5                                   4    
HELIX   14 AB5 THR C 1138  GLN C 1157  1                                  20    
HELIX   15 AB6 ALA C 1161  SER C 1184  1                                  24    
HELIX   16 AB7 GLY C 1189  THR C 1203  1                                  15    
HELIX   17 AB8 PRO C 1206  ALA C 1221  1                                  16    
HELIX   18 AB9 PRO C 1258  GLU C 1276  1                                  19    
HELIX   19 AC1 ALA C 1279  SER C 1294  1                                  16    
HELIX   20 AC2 SER C 1301  HIS C 1320  1                                  20    
HELIX   21 AC3 LEU D 1497  LEU D 1504  1                                   8    
HELIX   22 AC4 ARG D 1613  TYR D 1619  1                                   7    
HELIX   23 AC5 SER D 1714  SER D 1720  1                                   7    
HELIX   24 AC6 ALA D 1726  GLY D 1741  1                                  16    
HELIX   25 AC7 PRO B   90  CYS B   97  1                                   8    
HELIX   26 AC8 PRO B  115  SER B  120  1                                   6    
HELIX   27 AC9 SER B  315  GLU B  324  1                                  10    
HELIX   28 AD1 GLY B  329  GLY B  335  1                                   7    
HELIX   29 AD2 THR B  606  GLY B  612  1                                   7    
HELIX   30 AD3 ASN B  620  ASN B  629  1                                  10    
HELIX   31 AD4 SER B  630  ASP B  632  5                                   3    
HELIX   32 AD5 SER B  642  ALA B  650  1                                   9    
HELIX   33 AD6 CYS E 1010  THR E 1031  1                                  22    
HELIX   34 AD7 GLU E 1032  LEU E 1037  5                                   6    
HELIX   35 AD8 PRO E 1038  GLN E 1057  1                                  20    
HELIX   36 AD9 SER E 1075  ALA E 1089  1                                  15    
HELIX   37 AE1 SER E 1096  LEU E 1108  1                                  13    
HELIX   38 AE2 SER E 1109  GLN E 1111  5                                   3    
HELIX   39 AE3 ASN E 1135  GLN E 1157  1                                  23    
HELIX   40 AE4 ALA E 1161  SER E 1184  1                                  24    
HELIX   41 AE5 GLY E 1189  THR E 1203  1                                  15    
HELIX   42 AE6 PRO E 1206  ALA E 1221  1                                  16    
HELIX   43 AE7 PRO E 1258  GLU E 1276  1                                  19    
HELIX   44 AE8 ALA E 1279  SER E 1294  1                                  16    
HELIX   45 AE9 SER E 1301  THR E 1322  1                                  22    
HELIX   46 AF1 LEU F 1497  LEU F 1504  1                                   8    
HELIX   47 AF2 ARG F 1613  TYR F 1619  1                                   7    
HELIX   48 AF3 SER F 1714  SER F 1720  1                                   7    
HELIX   49 AF4 ALA F 1726  GLY F 1741  1                                  16    
SHEET    1 AA1 4 PHE A  82  LEU A  87  0                                        
SHEET    2 AA1 4 LEU A  37  GLN A  44 -1  N  VAL A  39   O  LEU A  85           
SHEET    3 AA1 4 ARG A  22  PRO A  28 -1  N  ARG A  22   O  GLN A  44           
SHEET    4 AA1 4 LEU A 652  SER A 655 -1  O  SER A 655   N  LEU A  25           
SHEET    1 AA2 5 VAL A  30  HIS A  32  0                                        
SHEET    2 AA2 5 ILE A 127  SER A 135  1  O  LEU A 133   N  VAL A  31           
SHEET    3 AA2 5 GLU A 107  HIS A 113 -1  N  ALA A 112   O  GLN A 128           
SHEET    4 AA2 5 VAL A  51  ARG A  59 -1  N  ARG A  59   O  GLN A 109           
SHEET    5 AA2 5 VAL A  72  SER A  77 -1  O  LEU A  76   N  VAL A  52           
SHEET    1 AA3 3 HIS A 140  THR A 145  0                                        
SHEET    2 AA3 3 ARG A 155  LEU A 163 -1  O  PHE A 161   N  PHE A 142           
SHEET    3 AA3 3 ILE A 197  VAL A 203 -1  O  PHE A 198   N  VAL A 160           
SHEET    1 AA4 5 ILE A 149  TYR A 150  0                                        
SHEET    2 AA4 5 SER A 227  VAL A 233  1  O  GLU A 232   N  TYR A 150           
SHEET    3 AA4 5 GLY A 211  PHE A 219 -1  N  GLY A 211   O  VAL A 233           
SHEET    4 AA4 5 THR A 173  GLU A 179 -1  N  GLU A 179   O  LYS A 214           
SHEET    5 AA4 5 ARG A 185  TYR A 192 -1  O  VAL A 186   N  VAL A 178           
SHEET    1 AA5 3 PHE A 241  PRO A 247  0                                        
SHEET    2 AA5 3 MET A 262  TYR A 270 -1  O  GLN A 267   N  LYS A 244           
SHEET    3 AA5 3 GLN A 309  LEU A 314 -1  O  ILE A 312   N  LEU A 264           
SHEET    1 AA6 5 TYR A 251  LEU A 253  0                                        
SHEET    2 AA6 5 TRP A 360  VAL A 363  1  O  VAL A 363   N  ILE A 252           
SHEET    3 AA6 5 ARG A 337  GLU A 346 -1  N  ARG A 337   O  PHE A 362           
SHEET    4 AA6 5 VAL A 279  LEU A 287 -1  N  ARG A 283   O  ALA A 342           
SHEET    5 AA6 5 SER A 301  LYS A 304 -1  O  THR A 303   N  ALA A 280           
SHEET    1 AA7 4 LYS A 293  PHE A 295  0                                        
SHEET    2 AA7 4 VAL A 279  LEU A 287 -1  N  LEU A 286   O  THR A 294           
SHEET    3 AA7 4 ARG A 337  GLU A 346 -1  O  ALA A 342   N  ARG A 283           
SHEET    4 AA7 4 GLU A 353  LEU A 357 -1  O  GLU A 354   N  ILE A 345           
SHEET    1 AA8 2 SER A 368  ASP A 370  0                                        
SHEET    2 AA8 2 LEU A 389  GLU A 392 -1  O  LEU A 389   N  ASP A 370           
SHEET    1 AA9 2 PRO A 383  LEU A 386  0                                        
SHEET    2 AA9 2 ILE A 433  ILE A 436 -1  O  ILE A 433   N  LEU A 386           
SHEET    1 AB1 4 SER A 414  GLN A 423  0                                        
SHEET    2 AB1 4 VAL A 403  SER A 411 -1  N  ALA A 407   O  GLN A 419           
SHEET    3 AB1 4 GLU A 443  ALA A 450 -1  O  SER A 449   N  LYS A 404           
SHEET    4 AB1 4 ALA A 456  ALA A 463 -1  O  ALA A 456   N  ALA A 450           
SHEET    1 AB2 3 PHE A 472  GLU A 476  0                                        
SHEET    2 AB2 3 THR A 488  VAL A 496 -1  O  ARG A 494   N  SER A 474           
SHEET    3 AB2 3 THR A 527  PHE A 532 -1  O  VAL A 531   N  LEU A 489           
SHEET    1 AB3 4 GLN A 514  PRO A 522  0                                        
SHEET    2 AB3 4 HIS A 504  SER A 511 -1  N  TYR A 505   O  GLU A 521           
SHEET    3 AB3 4 SER A 540  HIS A 549 -1  O  PHE A 546   N  TYR A 506           
SHEET    4 AB3 4 HIS A 552  ASP A 561 -1  O  ASN A 556   N  ALA A 545           
SHEET    1 AB4 3 GLU A 572  VAL A 575  0                                        
SHEET    2 AB4 3 SER A 586  ALA A 600 -1  O  GLU A 592   N  GLU A 572           
SHEET    3 AB4 3 VAL C 786  TRP C 798 -1  O  ARG C 791   N  THR A 593           
SHEET    1 AB5 3 GLU A 572  VAL A 575  0                                        
SHEET    2 AB5 3 SER A 586  ALA A 600 -1  O  GLU A 592   N  GLU A 572           
SHEET    3 AB5 3 SER C 812  LEU C 813 -1  O  LEU C 813   N  LEU A 598           
SHEET    1 AB6 4 ASN C 781  TRP C 782  0                                        
SHEET    2 AB6 4 ALA A 603  ASP A 605 -1  N  ALA A 603   O  TRP C 782           
SHEET    3 AB6 4 THR C 805  ILE C 808 -1  O  GLU C 807   N  LEU A 604           
SHEET    4 AB6 4 VAL C 825  ARG C 828 -1  O  LEU C 827   N  TRP C 806           
SHEET    1 AB7 5 VAL C 774  ARG C 775  0                                        
SHEET    2 AB7 5 GLY C 924  LEU C 931  1  O  ALA C 926   N  ARG C 775           
SHEET    3 AB7 5 VAL C 909  GLY C 917 -1  N  ALA C 915   O  ASP C 925           
SHEET    4 AB7 5 LEU C 863  SER C 870 -1  N  SER C 866   O  ARG C 916           
SHEET    5 AB7 5 GLN C 885  VAL C 889 -1  O  VAL C 887   N  VAL C 865           
SHEET    1 AB8 3 PHE C 833  HIS C 836  0                                        
SHEET    2 AB8 3 VAL C 854  ASN C 857 -1  O  VAL C 854   N  HIS C 836           
SHEET    3 AB8 3 ALA C 894  PRO C 896 -1  O  ARG C 895   N  LEU C 855           
SHEET    1 AB9 3 LEU C 849  LEU C 851  0                                        
SHEET    2 AB9 3 PHE C 899  PRO C 903 -1  O  VAL C 901   N  LEU C 849           
SHEET    3 AB9 3 LEU C 875  LEU C 877 -1  N  CYS C 876   O  VAL C 902           
SHEET    1 AC1 4 HIS C 940  LEU C 948  0                                        
SHEET    2 AC1 4 GLY C1376  TYR C1384 -1  O  LEU C1378   N  TYR C 946           
SHEET    3 AC1 4 TYR C 977  SER C 983 -1  N  SER C 983   O  THR C1377           
SHEET    4 AC1 4 LEU C1354  GLU C1356 -1  O  GLU C1356   N  VAL C 980           
SHEET    1 AC2 3 GLY C1338  GLN C1345  0                                        
SHEET    2 AC2 3 ASN C1328  GLY C1335 -1  N  SER C1333   O  LYS C1340           
SHEET    3 AC2 3 ILE C1366  ASN C1367 -1  O  ASN C1367   N  THR C1330           
SHEET    1 AC3 3 LEU C1397  ILE C1399  0                                        
SHEET    2 AC3 3 ARG D1465  ARG D1474 -1  O  TRP D1473   N  GLN C1398           
SHEET    3 AC3 3 THR C1402  VAL C1403 -1  N  THR C1402   O  THR D1469           
SHEET    1 AC4 4 LEU C1397  ILE C1399  0                                        
SHEET    2 AC4 4 ARG D1465  ARG D1474 -1  O  TRP D1473   N  GLN C1398           
SHEET    3 AC4 4 GLU D1534  GLN D1542 -1  O  ALA D1540   N  VAL D1466           
SHEET    4 AC4 4 PHE D1494  ALA D1496 -1  N  HIS D1495   O  VAL D1541           
SHEET    1 AC5 5 HIS D1514  GLU D1516  0                                        
SHEET    2 AC5 5 HIS D1521  PHE D1526 -1  O  LEU D1523   N  GLU D1516           
SHEET    3 AC5 5 ALA D1484  THR D1489 -1  N  VAL D1488   O  VAL D1522           
SHEET    4 AC5 5 PRO D1551  ASP D1558 -1  O  TYR D1557   N  ILE D1485           
SHEET    5 AC5 5 ARG D1565  GLY D1571 -1  O  VAL D1568   N  ALA D1554           
SHEET    1 AC6 2 THR D1581  SER D1584  0                                        
SHEET    2 AC6 2 VAL D1587  CYS D1590 -1  O  GLN D1589   N  LEU D1582           
SHEET    1 AC7 6 TYR D1701  LEU D1703  0                                        
SHEET    2 AC7 6 MET D1664  ARG D1670  1  N  LEU D1668   O  LEU D1703           
SHEET    3 AC7 6 PHE D1640  HIS D1652 -1  N  THR D1645   O  ARG D1665           
SHEET    4 AC7 6 TYR D1625  ARG D1637 -1  N  GLN D1628   O  THR D1648           
SHEET    5 AC7 6 GLU D1682  GLY D1687 -1  O  ILE D1685   N  PHE D1627           
SHEET    6 AC7 6 SER D1707  GLU D1711 -1  O  GLU D1710   N  LEU D1684           
SHEET    1 AC8 4 PHE B  82  LEU B  87  0                                        
SHEET    2 AC8 4 LEU B  37  GLN B  44 -1  N  VAL B  39   O  LEU B  85           
SHEET    3 AC8 4 ARG B  22  PRO B  28 -1  N  LEU B  24   O  GLN B  42           
SHEET    4 AC8 4 LEU B 652  SER B 655 -1  O  SER B 655   N  LEU B  25           
SHEET    1 AC9 5 VAL B  30  HIS B  32  0                                        
SHEET    2 AC9 5 ILE B 127  SER B 135  1  O  LEU B 133   N  VAL B  31           
SHEET    3 AC9 5 GLU B 107  HIS B 113 -1  N  ALA B 112   O  GLN B 128           
SHEET    4 AC9 5 VAL B  51  ARG B  59 -1  N  PHE B  57   O  VAL B 111           
SHEET    5 AC9 5 VAL B  72  SER B  77 -1  O  LEU B  76   N  VAL B  52           
SHEET    1 AD1 3 HIS B 140  THR B 145  0                                        
SHEET    2 AD1 3 ARG B 155  LEU B 163 -1  O  PHE B 161   N  PHE B 142           
SHEET    3 AD1 3 ILE B 197  VAL B 203 -1  O  PHE B 198   N  VAL B 160           
SHEET    1 AD2 5 ILE B 149  TYR B 150  0                                        
SHEET    2 AD2 5 SER B 227  VAL B 233  1  O  GLU B 232   N  TYR B 150           
SHEET    3 AD2 5 GLY B 211  PHE B 219 -1  N  GLY B 211   O  VAL B 233           
SHEET    4 AD2 5 THR B 173  GLU B 179 -1  N  MET B 177   O  SER B 216           
SHEET    5 AD2 5 ARG B 185  TYR B 192 -1  O  VAL B 186   N  VAL B 178           
SHEET    1 AD3 3 PHE B 241  PRO B 247  0                                        
SHEET    2 AD3 3 MET B 262  TYR B 270 -1  O  GLN B 267   N  LYS B 244           
SHEET    3 AD3 3 GLN B 309  LEU B 314 -1  O  ILE B 312   N  LEU B 264           
SHEET    1 AD4 5 TYR B 251  LEU B 253  0                                        
SHEET    2 AD4 5 TRP B 360  VAL B 363  1  O  VAL B 363   N  ILE B 252           
SHEET    3 AD4 5 LEU B 338  GLU B 346 -1  N  TYR B 339   O  TRP B 360           
SHEET    4 AD4 5 VAL B 279  LEU B 287 -1  N  TYR B 281   O  ILE B 344           
SHEET    5 AD4 5 SER B 301  LYS B 304 -1  O  THR B 303   N  ALA B 280           
SHEET    1 AD5 4 LYS B 293  PHE B 295  0                                        
SHEET    2 AD5 4 VAL B 279  LEU B 287 -1  N  LEU B 286   O  THR B 294           
SHEET    3 AD5 4 LEU B 338  GLU B 346 -1  O  ILE B 344   N  TYR B 281           
SHEET    4 AD5 4 GLU B 353  LEU B 357 -1  O  GLU B 354   N  ILE B 345           
SHEET    1 AD6 2 SER B 368  ASP B 370  0                                        
SHEET    2 AD6 2 LEU B 389  GLU B 392 -1  O  LEU B 389   N  ASP B 370           
SHEET    1 AD7 2 PRO B 383  LEU B 386  0                                        
SHEET    2 AD7 2 ILE B 433  ILE B 436 -1  O  ILE B 433   N  LEU B 386           
SHEET    1 AD8 4 SER B 414  GLN B 423  0                                        
SHEET    2 AD8 4 VAL B 403  SER B 411 -1  N  ALA B 407   O  GLN B 419           
SHEET    3 AD8 4 GLU B 443  ALA B 450 -1  O  SER B 449   N  LYS B 404           
SHEET    4 AD8 4 ALA B 456  ALA B 463 -1  O  ALA B 456   N  ALA B 450           
SHEET    1 AD9 3 PHE B 472  GLU B 476  0                                        
SHEET    2 AD9 3 THR B 488  VAL B 496 -1  O  VAL B 496   N  PHE B 472           
SHEET    3 AD9 3 THR B 527  PHE B 532 -1  O  THR B 527   N  LEU B 493           
SHEET    1 AE1 4 GLN B 514  PRO B 522  0                                        
SHEET    2 AE1 4 HIS B 504  SER B 511 -1  N  TYR B 505   O  GLU B 521           
SHEET    3 AE1 4 SER B 540  HIS B 549 -1  O  TYR B 542   N  LEU B 510           
SHEET    4 AE1 4 HIS B 552  ASP B 561 -1  O  ASN B 556   N  ALA B 545           
SHEET    1 AE2 3 GLU B 572  VAL B 575  0                                        
SHEET    2 AE2 3 SER B 586  ALA B 600 -1  O  HIS B 590   N  SER B 574           
SHEET    3 AE2 3 VAL E 786  TRP E 798 -1  O  ARG E 791   N  THR B 593           
SHEET    1 AE3 3 GLU B 572  VAL B 575  0                                        
SHEET    2 AE3 3 SER B 586  ALA B 600 -1  O  HIS B 590   N  SER B 574           
SHEET    3 AE3 3 SER E 812  LEU E 813 -1  O  LEU E 813   N  LEU B 598           
SHEET    1 AE4 4 ASN E 781  TRP E 782  0                                        
SHEET    2 AE4 4 GLY B 602  ASP B 605 -1  N  ALA B 603   O  TRP E 782           
SHEET    3 AE4 4 THR E 805  HIS E 809 -1  O  HIS E 809   N  GLY B 602           
SHEET    4 AE4 4 VAL E 825  ARG E 828 -1  O  LEU E 827   N  TRP E 806           
SHEET    1 AE5 5 VAL E 774  ARG E 775  0                                        
SHEET    2 AE5 5 GLY E 924  LEU E 931  1  O  ALA E 926   N  ARG E 775           
SHEET    3 AE5 5 VAL E 909  GLY E 917 -1  N  ALA E 915   O  ASP E 925           
SHEET    4 AE5 5 LEU E 863  SER E 870 -1  N  SER E 870   O  LYS E 912           
SHEET    5 AE5 5 GLN E 885  VAL E 889 -1  O  VAL E 887   N  VAL E 865           
SHEET    1 AE6 3 PHE E 833  HIS E 836  0                                        
SHEET    2 AE6 3 VAL E 854  ASN E 857 -1  O  TYR E 856   N  HIS E 834           
SHEET    3 AE6 3 ALA E 894  PRO E 896 -1  O  ARG E 895   N  LEU E 855           
SHEET    1 AE7 3 LEU E 849  LEU E 851  0                                        
SHEET    2 AE7 3 PHE E 899  PRO E 903 -1  O  VAL E 901   N  LEU E 849           
SHEET    3 AE7 3 LEU E 875  LEU E 877 -1  N  CYS E 876   O  VAL E 902           
SHEET    1 AE8 4 HIS E 940  LEU E 948  0                                        
SHEET    2 AE8 4 GLY E1376  TYR E1384 -1  O  LEU E1378   N  TYR E 946           
SHEET    3 AE8 4 TYR E 977  SER E 983 -1  N  SER E 983   O  THR E1377           
SHEET    4 AE8 4 LEU E1354  GLU E1356 -1  O  GLU E1356   N  VAL E 980           
SHEET    1 AE9 3 GLY E1338  GLN E1345  0                                        
SHEET    2 AE9 3 ASN E1328  GLY E1335 -1  N  SER E1333   O  LYS E1340           
SHEET    3 AE9 3 ILE E1366  ASN E1367 -1  O  ASN E1367   N  THR E1330           
SHEET    1 AF1 3 LEU E1397  ILE E1399  0                                        
SHEET    2 AF1 3 ARG F1465  ARG F1474 -1  O  TRP F1473   N  GLN E1398           
SHEET    3 AF1 3 THR E1402  VAL E1403 -1  N  THR E1402   O  THR F1469           
SHEET    1 AF2 4 LEU E1397  ILE E1399  0                                        
SHEET    2 AF2 4 ARG F1465  ARG F1474 -1  O  TRP F1473   N  GLN E1398           
SHEET    3 AF2 4 GLU F1534  GLN F1542 -1  O  ALA F1540   N  VAL F1466           
SHEET    4 AF2 4 PHE F1494  ALA F1496 -1  N  HIS F1495   O  VAL F1541           
SHEET    1 AF3 5 HIS F1514  GLU F1516  0                                        
SHEET    2 AF3 5 HIS F1521  PHE F1526 -1  O  LEU F1523   N  GLU F1516           
SHEET    3 AF3 5 ALA F1484  THR F1489 -1  N  VAL F1488   O  VAL F1522           
SHEET    4 AF3 5 PRO F1551  ASP F1558 -1  O  TYR F1557   N  ILE F1485           
SHEET    5 AF3 5 ARG F1565  GLY F1571 -1  O  VAL F1568   N  ALA F1554           
SHEET    1 AF4 2 THR F1581  SER F1584  0                                        
SHEET    2 AF4 2 VAL F1587  CYS F1590 -1  O  GLN F1589   N  LEU F1582           
SHEET    1 AF5 6 TYR F1701  LEU F1703  0                                        
SHEET    2 AF5 6 MET F1664  ARG F1670  1  N  LEU F1668   O  LEU F1703           
SHEET    3 AF5 6 PHE F1640  HIS F1652 -1  N  PHE F1643   O  PHE F1667           
SHEET    4 AF5 6 TYR F1625  ARG F1637 -1  N  GLN F1628   O  THR F1648           
SHEET    5 AF5 6 GLU F1682  GLY F1687 -1  O  ILE F1685   N  PHE F1627           
SHEET    6 AF5 6 SER F1707  GLU F1711 -1  O  GLU F1710   N  LEU F1684           
SSBOND   1 CYS A   68    CYS A   97                          1555   1555  2.04  
SSBOND   2 CYS A  567    CYS C  820                          1555   1555  2.06  
SSBOND   3 CYS A  635    CYS A  669                          1555   1555  2.03  
SSBOND   4 CYS C  876    CYS D 1590                          1555   1555  2.02  
SSBOND   5 CYS C 1394    CYS D 1566                          1555   1555  2.04  
SSBOND   6 CYS D 1471    CYS D 1535                          1555   1555  2.03  
SSBOND   7 CYS D 1583    CYS D 1588                          1555   1555  2.04  
SSBOND   8 CYS D 1595    CYS D 1673                          1555   1555  2.03  
SSBOND   9 CYS D 1618    CYS D 1742                          1555   1555  2.03  
SSBOND  10 CYS D 1718    CYS D 1727                          1555   1555  2.04  
SSBOND  11 CYS B   68    CYS B   97                          1555   1555  2.03  
SSBOND  12 CYS B  567    CYS E  820                          1555   1555  2.00  
SSBOND  13 CYS B  635    CYS B  669                          1555   1555  2.04  
SSBOND  14 CYS E  876    CYS F 1590                          1555   1555  2.03  
SSBOND  15 CYS E 1394    CYS F 1566                          1555   1555  2.03  
SSBOND  16 CYS F 1471    CYS F 1535                          1555   1555  2.03  
SSBOND  17 CYS F 1583    CYS F 1588                          1555   1555  2.03  
SSBOND  18 CYS F 1595    CYS F 1673                          1555   1555  2.03  
SSBOND  19 CYS F 1618    CYS F 1742                          1555   1555  2.03  
SSBOND  20 CYS F 1718    CYS F 1727                          1555   1555  2.04  
CRYST1  121.500  161.080  131.600  90.00 107.26  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008230  0.000000  0.002558        0.00000                         
SCALE2      0.000000  0.006208  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007957        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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